| Version |
2.5 |
| Creation Date |
2005-11-16 15:48:42 |
| Update Date |
2010-04-08 16:39:44 |
| Accession Number |
HMDB00904 |
| Secondary Accession Numbers |
Not Available |
| Common Name |
Citrulline |
| Description |
Citrulline is an amino acid made from ornithine and carbamoyl phosphate in one of the central reactions in the urea cycle. It is also produced from arginine as a by-product of the reaction catalyzed by NOS family (NOS; EC 1.14.13.39). In this reaction arginine is first oxidized into N-hydroxyl-arginine, which is then further oxidized to citrulline concomitant with the release of nitric oxide.; EC 1.14.13.39). Citrulline's name is derived from citrullus, the Latin word for watermelon, from which it was first isolated. |
| Synonyms |
- (2S)-2-amino-5-(carbamoylamino)pentanoic acid
- (S)-2-Amino-5-ureidopentanoate
- (S)-2-Amino-5-ureidopentanoic acid
- (S)-2-amino-5-(aminocarbonyl)aminopentanoic acid
- 2-Amino-5-uredovalerate
- 2-Amino-5-uredovaleric acid
- 2-Amino-5-ureidovalerate
- 2-Amino-5-ureidovaleric acid
- A-amino-d-ureidovalerate
- A-amino-d-ureidovaleric acid
- Alpha-amino-delta-ureidovalerate
- Alpha-amino-delta-ureidovaleric acid
- Alpha-amino-gamma-ureidovalerate
- Alpha-amino-gamma-ureidovaleric acid
- Amino-ureidovalerate
- Amino-ureidovaleric acid
- CIR
- CIT
- Cytrulline
- D-ureidonorvaline
- DL-citrulline
- Delta-ureidonorvaline
- Gammaureidonorvaline
- H-cit-oh
- L(+)-2-Amino-5-ureidovalerate
- L(+)-2-Amino-5-ureidovaleric acid
- L(+)-citrulline
- L-2-Amino-5-ureido-valerate
- L-2-Amino-5-ureido-valeric acid
- L-2-Amino-5-ureidovalerate
- L-2-Amino-5-ureidovaleric acid
- L-N5-carbamoyl-Ornithine
- L-citrulline
- L-cytrulline
- N()-carbamylornithine
- N(5)-(aminocarbonyl)-DL-Ornithine
- N(delta)-carbamylornithine
- N-carbamylornithine
- N5-(Aminocarbonyl)-L-ornithine
- N5-(Aminocarbonyl)ornithine
- N5-(aminocarbonyl)-Ornithine
- N5-Carbamoyl-L-ornithine
- N5-carbamoylornithine
- N5-carbamylornithine
- N5-(aminocarbonyl)ornithine
- ND-carbamylornithine
- Ndelta-carbamy-ornithine
- Ndelta-carbamylornithine
- Ngamma-carbamylornithine
- Sitrulline
- Ureidonorvaline
- Ureidovalerate
- Ureidovaleric acid
- (2S)-2-amino-5-(carbamoylamino)pentanoate
- (S)-2-amino-5-(aminocarbonyl)aminopentanoate
|
| Chemical IUPAC Name |
(2S)-2-amino-5-(carbamoylamino)pentanoic acid |
| Chemical Formula |
C6H13N3O3 |
| Chemical Structure |
 |
| Chemical Taxonomy |
| Kingdom |
|
| Super Class |
- Amino acids and Amino Acid conjugates
|
| Class |
|
| Sub Class |
|
| Family |
|
| Species |
- primary amine
- primary aliphatic amine (alkylamine)
- carboxylic acid
- urea
- alpha-aminoacid
|
| Biofunction |
- Component of Alanine and aspartate metabolism
- Component of Arginine and proline metabolism
|
| Application |
| — |
| Source |
|
|
| Average Molecular Weight |
175.186 |
| Monoisotopic Molecular Weight |
175.095688 |
| Isomeric SMILES |
N[C@@H](CCCNC(N)=O)C(O)=O |
| Canonical SMILES |
NC(CCCNC(N)=O)C(O)=O |
| KEGG Compound ID |
C00327  |
| BioCyc ID |
L-CITRULLINE  |
| BiGG ID |
34627  |
| Wikipedia Link |
Citrulline  |
| NuGOwiki Link |
HMDB00904  |
| Metagene Link |
HMDB00904  |
| METLIN ID |
16  |
| PubChem Compound |
9750  |
| PubChem Substance |
11532235  |
| ChEBI ID |
18211  |
| CAS Registry Number |
372-75-8 |
| InChI Identifier |
InChI=1/C6H13N3O3/c7-4(5(10)11)2-1-3-9-6(8)12/h4H,1-3,7H2,(H,10,11)(H3,8,9,12)/t4-/m0/s1 |
| Synthesis Reference |
Kakimoto, Toshio; Shibatani, Takeji; Nishimura, Noriyuki; Chibata, Ichiro. Enzymic production of L-citrulline by Pseudomonas putida. Applied Microbiology (1971), 22(6), 992-9. |
| Melting Point (Experimental) |
235.5 oC |
| Experimental Water Solubility |
212 mg/mL [HMP experimental]
Source: PhysProp
|
| Predicted Water Solubility |
12.8 mg/mL at 25 oC [MEYLAN,WM et al. (1996)]; 21.800001 mg/mL [Predicted by ALOGPS]
Calculated using ALOGPS
|
| Physiological Charge |
0 |
| State |
Solid |
| Experimental LogP/Hydrophobicity |
-3.19 [SANGSTER (1994)]
Source: PhysProp
|
| Predicted LogP/Hydrophobicity |
-3.27 [Predicted by ALOGPS]; -3.9 [Predicted by PubChem via XLOGP]
Calculated using ALOGPS
|
| Material Safety Data Sheet (MSDS) |
|
| MOL File |
Show |
| SDF File |
Show |
| PDB File |
Show |
| 2D Structure |
|
| 3D Structure |
|
| Experimental PDB ID |
1H70  |
| Experimental PDB File |
Show |
| Experimental PDB Structure |
|
| Experimental 1H NMR Spectrum |
Download Spectrum Download FID (Varian) Show Experimental Conditions  |
| Experimental 13C NMR Spectrum |
Download Spectrum Download FID (Bruker) Show Experimental Conditions  |
| Experimental 13C HSQC Spectrum |
Download Spectrum Download FID (Bruker) Show Experimental Conditions  |
| Predicted 1H NMR Spectrum |
Show Image Show Peaklist
|
| Predicted 13C NMR Spectrum |
Show Image Show Peaklist
|
| Mass Spectrum |
|
| Simplified TOCSY Spectrum |
Show Image Show Peaklist |
| BMRB Spectrum |
Show Image Show Peaklist |
| Cellular Location |
- Cytoplasm (Predicted from LogP)
- mitochondria
|
| Biofluid Location |
- Blood
- Cerebrospinal Fluid
- Urine
|
| Tissue Location |
| Tissue |
References |
| Bladder |
— |
| Epidermis |
— |
| Fibroblasts |
— |
| Intestine |
— |
| Kidney |
— |
| Liver |
— |
| Myelin |
— |
| Nerve Cells |
— |
| Neuron |
— |
| Placenta |
— |
| Platelet |
— |
|
| Concentrations (Normal) |
| Biofluid |
Blood |
| Value |
38.0 (30.0-46.0) uM |
| Age |
Adult:>18 yrs old |
| Sex |
N/A |
| Patient information |
Normal |
| Comments |
Not Available |
| References |
- Schram KH: Urinary nucleosides. Mass Spectrom Rev. 1998 May-Jun;17(3):131-251. [PubMed
]
- Biagini GA, Kirk K, Schofield PJ, Edwards MR: Role of K+ and amino acids in osmoregulation by the free-living microaerophilic protozoon Hexamita inflata. Microbiology. 2000 Feb;146 ( Pt 2):427-33. [PubMed
]
- Crenn P, Coudray-Lucas C, Thuillier F, Cynober L, Messing B: Postabsorptive plasma citrulline concentration is a marker of absorptive enterocyte mass and intestinal failure in humans. Gastroenterology. 2000 Dec;119(6):1496-505. [PubMed
]
- Oshiro S, Kochinda T, Tana T, Yamazato M, Kobayashi K, Komine Y, Muratani H, Saheki T, Iseki K, Takishita S: A patient with adult-onset type II citrullinemia on long-term hemodialysis: reversal of clinical symptoms and brain MRI findings. Am J Kidney Dis. 2002 Jan;39(1):189-92. [PubMed
]
- Chadefaux-Vekemans B, Rabier D, Chabli A, Blanc A, Aupetit J, Bardet J, Kamoun P: Improving the prenatal diagnosis of citrullinemia using citrulline/ornithine+arginine ratio in amniotic fluid. Prenat Diagn. 2002 Jun;22(6):456-8. [PubMed
]
- Cynober LA: Plasma amino acid levels with a note on membrane transport: characteristics, regulation, and metabolic significance. Nutrition. 2002 Sep;18(9):761-6. [PubMed
]
- Engelborghs S, Marescau B, De Deyn PP: Amino acids and biogenic amines in cerebrospinal fluid of patients with Parkinson's disease. Neurochem Res. 2003 Aug;28(8):1145-50. [PubMed
]
- Haberle J, Pauli S, Schmidt E, Schulze-Eilfing B, Berning C, Koch HG: Mild citrullinemia in Caucasians is an allelic variant of argininosuccinate synthetase deficiency (citrullinemia type 1). Mol Genet Metab. 2003 Nov;80(3):302-6. [PubMed
]
- Noris M, Todeschini M, Cassis P, Pasta F, Cappellini A, Bonazzola S, Macconi D, Maucci R, Porrati F, Benigni A, Picciolo C, Remuzzi G: L-arginine depletion in preeclampsia orients nitric oxide synthase toward oxidant species. Hypertension. 2004 Mar;43(3):614-22. Epub 2004 Jan 26. [PubMed
]
- Rainesalo S, Keranen T, Palmio J, Peltola J, Oja SS, Saransaari P: Plasma and cerebrospinal fluid amino acids in epileptic patients. Neurochem Res. 2004 Jan;29(1):319-24. [PubMed
]
- Mandel H, Levy N, Izkovitch S, Korman SH: Elevated plasma citrulline and arginine due to consumption of Citrullus vulgaris (watermelon). J Inherit Metab Dis. 2005;28(4):467-72. [PubMed
]
- Jianfeng G, Weiming Z, Ning L, Fangnan L, Li T, Nan L, Jieshou L: Serum citrulline is a simple quantitative marker for small intestinal enterocytes mass and absorption function in short bowel patients. J Surg Res. 2005 Aug;127(2):177-82. [PubMed
]
- http://www.doctorsdata.com/
|
| Biofluid |
Blood |
| Value |
38.0 (30.0-46.0) uM |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Patient information |
Normal |
| Comments |
Not Available |
| References |
- Cynober LA: Plasma amino acid levels with a note on membrane transport: characteristics, regulation, and metabolic significance. Nutrition. 2002 Sep;18(9):761-6. [PubMed
]
|
| Biofluid |
Blood |
| Value |
36.0 +/- 8.0 uM |
| Age |
Children:1-13 yrs old |
| Sex |
Male |
| Patient information |
Normal |
| Comments |
Not Available |
| References |
- Geigy Scientific Tables, 8th Rev edition, pp. 92. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
|
| Biofluid |
Blood |
| Value |
37.0 +/- 9.0 uM |
| Age |
Adult:>18 yrs old |
| Sex |
Male |
| Patient information |
Normal |
| Comments |
Not Available |
| References |
- Geigy Scientific Tables, 8th Rev edition, pp. 92. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
|
| Biofluid |
Blood |
| Value |
35.0 +/- 10.0 uM |
| Age |
Adult:>18 yrs old |
| Sex |
Female |
| Patient information |
Normal |
| Comments |
Not Available |
| References |
- Geigy Scientific Tables, 8th Rev edition, pp. 92. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
|
| Biofluid |
Blood |
| Value |
27.5 (10.0-45.0) uM |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Patient information |
Normal |
| Comments |
Not Available |
| References |
|
| Biofluid |
CSF |
| Value |
1.5 +/- 0.5 uM |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Patient information |
Normal |
| Comments |
Not Available |
| References |
- Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
|
| Biofluid |
CSF |
| Value |
2.62 (1.35-3.89) uM |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Patient information |
Normal |
| Comments |
Not Available |
| References |
- Engelborghs S, Marescau B, De Deyn PP: Amino acids and biogenic amines in cerebrospinal fluid of patients with Parkinson's disease. Neurochem Res. 2003 Aug;28(8):1145-50. [PubMed
]
|
| Biofluid |
CSF |
| Value |
2.8 +/- 1.0 uM |
| Age |
Adult:>18 yrs old |
| Sex |
Male |
| Patient information |
Normal |
| Comments |
Not Available |
| References |
- Hagenfeldt L, Bjerkenstedt L, Edman G, Sedvall G, Wiesel FA: Amino acids in plasma and CSF and monoamine metabolites in CSF: interrelationship in healthy subjects. J Neurochem. 1984 Mar;42(3):833-7. [PubMed
]
|
| Biofluid |
CSF |
| Value |
2.8 +/- 1.8 uM |
| Age |
Adult:>18 yrs old |
| Sex |
N/A |
| Patient information |
Normal |
| Comments |
Not Available |
| References |
- Hagenfeldt L, Bjerkenstedt L, Edman G, Sedvall G, Wiesel FA: Amino acids in plasma and CSF and monoamine metabolites in CSF: interrelationship in healthy subjects. J Neurochem. 1984 Mar;42(3):833-7. [PubMed
]
|
| Biofluid |
CSF |
| Value |
5.81+/- 1.23 uM |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Patient information |
Normal |
| Comments |
Not Available |
| References |
- Do KQ, Lauer CJ, Schreiber W, Zollinger M, Gutteck-Amsler U, Cuenod M, Holsboer F: gamma-Glutamylglutamine and taurine concentrations are decreased in the cerebrospinal fluid of drug-naive patients with schizophrenic disorders. J Neurochem. 1995 Dec;65(6):2652-62. [PubMed
]
|
| Biofluid |
Urine |
| Value |
1.08 (0.065-2.1) umol/mmol creatinine |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Patient information |
Normal |
| Comments |
Not Available |
| References |
|
| Biofluid |
Urine |
| Value |
0.50 +/- 0.54 umol/mmol creatinine |
| Age |
Children:1-13 yrs old |
| Sex |
Male |
| Patient information |
Normal |
| Comments |
Not Available |
| References |
- Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by Cornelius Lentner.
- West Cadwell, N.J. : Medical education Div., Ciba-Geigy Corp.
- Basel, Switzerland c1981-1992.
|
| Biofluid |
Urine |
| Value |
1.1 +/- 0.84 umol/mmol creatinine |
| Age |
Adult:>18 yrs old |
| Sex |
Male |
| Patient information |
Normal |
| Comments |
Not Available |
| References |
- Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by Cornelius Lentner.
- West Cadwell, N.J. : Medical education Div., Ciba-Geigy Corp.
- Basel, Switzerland c1981-1992.
|
| Biofluid |
Urine |
| Value |
0.99 +/- 0.69 umol/mmol creatinine |
| Age |
Adult:>18 yrs old |
| Sex |
Female |
| Patient information |
Normal |
| Comments |
Not Available |
| References |
- Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by Cornelius Lentner.
- West Cadwell, N.J. : Medical education Div., Ciba-Geigy Corp.
- Basel, Switzerland c1981-1992.
|
| Biofluid |
Urine |
| Value |
0.19 umol/mmol creatinine |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Patient information |
Normal |
| Comments |
Not Available |
| References |
- Guo K, Li L: Differential (12)C-/(13)C-Isotope Dansylation Labeling and Fast Liquid Chromatography/Mass Spectrometry for Absolute and Relative Quantification of the Metabolome. Anal Chem. 2009 Mar 23. [PubMed
]
|
|
| Concentrations (Abnormal) |
| Biofluid |
Blood |
| Value |
13.0 (6.0-20.0) uM |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Condition |
Intestinal failure |
| Comments |
Not Available |
| References |
- Crenn P, Coudray-Lucas C, Thuillier F, Cynober L, Messing B: Postabsorptive plasma citrulline concentration is a marker of absorptive enterocyte mass and intestinal failure in humans. Gastroenterology. 2000 Dec;119(6):1496-505. [PubMed
]
|
| Biofluid |
Blood |
| Value |
25.4 (23.4-27.4) uM |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Condition |
Epilepsy |
| Comments |
Acute seizures |
| References |
- Rainesalo S, Keranen T, Palmio J, Peltola J, Oja SS, Saransaari P: Plasma and cerebrospinal fluid amino acids in epileptic patients. Neurochem Res. 2004 Jan;29(1):319-24. [PubMed
]
|
| Biofluid |
Blood |
| Value |
26.8 (25.4-28.2) uM |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Condition |
Epilepsy |
| Comments |
Refractory localization-related epilepsy (RLE) |
| References |
- Rainesalo S, Keranen T, Palmio J, Peltola J, Oja SS, Saransaari P: Plasma and cerebrospinal fluid amino acids in epileptic patients. Neurochem Res. 2004 Jan;29(1):319-24. [PubMed
]
|
| Biofluid |
Blood |
| Value |
26.9 (25.2-28.6) uM |
| Age |
Children:1-13 yrs old |
| Sex |
Both |
| Condition |
Epilepsy |
| Comments |
Juvenile myoclonic epilepsy (JME) |
| References |
- Rainesalo S, Keranen T, Palmio J, Peltola J, Oja SS, Saransaari P: Plasma and cerebrospinal fluid amino acids in epileptic patients. Neurochem Res. 2004 Jan;29(1):319-24. [PubMed
]
|
| Biofluid |
Blood |
| Value |
94.97 +/- 11.18 uM |
| Age |
Elderly:>65 yrs old |
| Sex |
Both |
| Condition |
Alzheimer's disease |
| Comments |
Not Available |
| References |
- Fonteh AN, Harrington RJ, Tsai A, Liao P, Harrington MG: Free amino acid and dipeptide changes in the body fluids from Alzheimer's disease subjects. Amino Acids. 2007 Feb;32(2):213-24. Epub 2006 Oct 10. [PubMed
]
|
| Biofluid |
Blood |
| Value |
200.0 (100.0-300.0) uM |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Condition |
Argininosuccinic aciduria |
| Comments |
Not Available |
| References |
|
| Biofluid |
Blood |
| Value |
10.00 (5.00-15.00) uM |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Comments |
Not Available |
| References |
|
| Biofluid |
CSF |
| Value |
5.38 +/- 0.94 uM |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Condition |
Schizophrenia |
| Comments |
Not Available |
| References |
- Do KQ, Lauer CJ, Schreiber W, Zollinger M, Gutteck-Amsler U, Cuenod M, Holsboer F: gamma-Glutamylglutamine and taurine concentrations are decreased in the cerebrospinal fluid of drug-naive patients with schizophrenic disorders. J Neurochem. 1995 Dec;65(6):2652-62. [PubMed
]
|
| Biofluid |
CSF |
| Value |
27.0 +/- 2.6 uM |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Condition |
Alzheimer's disease |
| Comments |
Not Available |
| References |
- Fonteh AN, Harrington RJ, Tsai A, Liao P, Harrington MG: Free amino acid and dipeptide changes in the body fluids from Alzheimer's disease subjects. Amino Acids. 2007 Feb;32(2):213-24. Epub 2006 Oct 10. [PubMed
]
|
| Biofluid |
Urine |
| Value |
21.0 +/- 2.8 umol/mmol creatinine |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Condition |
Alzheimer's disease |
| Comments |
Not Available |
| References |
- Fonteh AN, Harrington RJ, Tsai A, Liao P, Harrington MG: Free amino acid and dipeptide changes in the body fluids from Alzheimer's disease subjects. Amino Acids. 2007 Feb;32(2):213-24. Epub 2006 Oct 10. [PubMed
]
|
|
| Associated Disorders |
| Condition |
References |
| Alzheimer's disease |
- Fonteh AN, Harrington RJ, Tsai A, Liao P, Harrington MG: Free amino acid and dipeptide changes in the body fluids from Alzheimer's disease subjects. Amino Acids. 2007 Feb;32(2):213-24. Epub 2006 Oct 10. [PubMed
]
|
| Argininosuccinic aciduria |
|
| Epilepsy |
- Rainesalo S, Keranen T, Palmio J, Peltola J, Oja SS, Saransaari P: Plasma and cerebrospinal fluid amino acids in epileptic patients. Neurochem Res. 2004 Jan;29(1):319-24. [PubMed
]
|
| Intestinal failure |
- Crenn P, Coudray-Lucas C, Thuillier F, Cynober L, Messing B: Postabsorptive plasma citrulline concentration is a marker of absorptive enterocyte mass and intestinal failure in humans. Gastroenterology. 2000 Dec;119(6):1496-505. [PubMed
]
|
| Schizophrenia |
- Do KQ, Lauer CJ, Schreiber W, Zollinger M, Gutteck-Amsler U, Cuenod M, Holsboer F: gamma-Glutamylglutamine and taurine concentrations are decreased in the cerebrospinal fluid of drug-naive patients with schizophrenic disorders. J Neurochem. 1995 Dec;65(6):2652-62. [PubMed
]
|
|
| OMIM ID |
|
| Pathways |
|
| General References |
- DeLong GR, Glick TH: Ammonia metabolism in Reye syndrome and the effect of citrulline. Ann Neurol. 1982 Jan;11(1):53-8. [PubMed
]
- Jianfeng G, Weiming Z, Ning L, Fangnan L, Li T, Nan L, Jieshou L: Serum citrulline is a simple quantitative marker for small intestinal enterocytes mass and absorption function in short bowel patients. J Surg Res. 2005 Aug;127(2):177-82. [PubMed
]
- Cynober LA: Plasma amino acid levels with a note on membrane transport: characteristics, regulation, and metabolic significance. Nutrition. 2002 Sep;18(9):761-6. [PubMed
]
- Liappis N, Pohl B, Weber HP, el-Karkani H: [Free amino acids in the saliva of children with phenylketonuria] Klin Padiatr. 1986 Jan-Feb;198(1):25-8. [PubMed
]
- Rainesalo S, Keranen T, Palmio J, Peltola J, Oja SS, Saransaari P: Plasma and cerebrospinal fluid amino acids in epileptic patients. Neurochem Res. 2004 Jan;29(1):319-24. [PubMed
]
- Fleisher LD, Harris CJ, Mitchell DA, Nadler HL: Citrullinemia: prenatal diagnosis of an affected fetus. Am J Hum Genet. 1983 Jan;35(1):85-90. [PubMed
]
- Potter MA, Zeesman S, Brennan B, Kobayashi K, Gao HZ, Tabata A, Saheki T, Whelan DT: Pregnancy in a healthy woman with untreated citrullinemia. Am J Med Genet A. 2004 Aug 15;129(1):77-82. [PubMed
]
- Wheatley DN, Kilfeather R, Stitt A, Campbell E: Integrity and stability of the citrulline-arginine pathway in normal and tumour cell lines. Cancer Lett. 2005 Sep 28;227(2):141-52. [PubMed
]
- Melis GC, Boelens PG, van der Sijp JR, Popovici T, De Bandt JP, Cynober L, van Leeuwen PA: The feeding route (enteral or parenteral) affects the plasma response of the dipetide Ala-Gln and the amino acids glutamine, citrulline and arginine, with the administration of Ala-Gln in preoperative patients. Br J Nutr. 2005 Jul;94(1):19-26. [PubMed
]
- Reparon-Schuijt CC, van Esch WJ, van Kooten C, Schellekens GA, de Jong BA, van Venrooij WJ, Breedveld FC, Verweij CL: Secretion of anti-citrulline-containing peptide antibody by B lymphocytes in rheumatoid arthritis. Arthritis Rheum. 2001 Jan;44(1):41-7. [PubMed
]
- Maruyama H, Ogawa M, Nishio T, Kobayashi K, Saheki T, Sunohara N: Citrullinemia type II in a 64-year-old man with fluctuating serum citrulline levels. J Neurol Sci. 2001 Jan 1;182(2):167-70. [PubMed
]
- McLaurin J, Moscarello MA: The preparation of antibodies reactive against citrulline-containing charge isomers of myelin basic protein but not against the arginine-containing charge isomers. Anal Biochem. 1990 Dec;191(2):272-7. [PubMed
]
- Facchinetti F, Longo M, Piccinini F, Neri I, Volpe A: L-arginine infusion reduces blood pressure in preeclamptic women through nitric oxide release. J Soc Gynecol Investig. 1999 Jul-Aug;6(4):202-7. [PubMed
]
- Origuchi Y, Ushijima T, Sakaguchi M, Akaboshi I, Matsuda I: Citrullinemia presenting as uncontrollable epilepsy. Brain Dev. 1984;6(3):328-31. [PubMed
]
- Booth FA, Haworth JC, Dilling LA, Perry TL, Greenberg CR, Seargeant LE, Penn AM, Rhead WJ: Mitochondrial encephalomyopathy with associated aminoacidopathy in a male sibship. J Pediatr. 1989 Jul;115(1):81-8. [PubMed
]
- Engelborghs S, Marescau B, De Deyn PP: Amino acids and biogenic amines in cerebrospinal fluid of patients with Parkinson's disease. Neurochem Res. 2003 Aug;28(8):1145-50. [PubMed
]
- Le Boucher J, Charret C, Coudray-Lucas C, Giboudeau J, Cynober L: Amino acid determination in biological fluids by automated ion-exchange chromatography: performance of Hitachi L-8500A. Clin Chem. 1997 Aug;43(8 Pt 1):1421-8. [PubMed
]
- Crenn P, Coudray-Lucas C, Thuillier F, Cynober L, Messing B: Postabsorptive plasma citrulline concentration is a marker of absorptive enterocyte mass and intestinal failure in humans. Gastroenterology. 2000 Dec;119(6):1496-505. [PubMed
]
- Hagenfeldt L, Bjerkenstedt L, Edman G, Sedvall G, Wiesel FA: Amino acids in plasma and CSF and monoamine metabolites in CSF: interrelationship in healthy subjects. J Neurochem. 1984 Mar;42(3):833-7. [PubMed
]
- Wikipedia

|
| Metabolic Enzymes |
- Argininosuccinate synthase
- Protein-arginine deiminase type-4
- Protein-arginine deiminase type-3
- NG,NG-dimethylarginine dimethylaminohydrolase 2
- Nitric oxide synthase, inducible
- Ornithine carbamoyltransferase, mitochondrial precursor
- Nitric-oxide synthase, brain
- Nitric-oxide synthase, endothelial
- Nitric oxide synthase 2A (Inducible, hepatocytes)
- cDNA FLJ61209, highly similar to NG,NG-dimethylarginine dimethylaminohydrolase 1 (EC 3.5.3.18)
- NOS1 mutant (Nitric oxide synthase 1 (Neuronal), isoform CRA_c)
|
|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5928 |
| Enzyme 1 Name |
Argininosuccinate synthase |
| Enzyme 1 Synonyms |
- Citrulline--aspartate ligase
|
| Enzyme 1 Gene Name |
ASS1 |
| Enzyme 1 Protein Sequence |
>Argininosuccinate synthase
MSSKGSVVLAYSGGLDTSCILVWLKEQGYDVIAYLANIGQKEDFEEARKKALKLGAKKVF
IEDVSREFVEEFIWPAIQSSALYEDRYLLGTSLARPCIARKQVEIAQREGAKYVSHGATG
KGNDQVRFELSCYSLAPQIKVIAPWRMPEFYNRFKGRNDLMEYAKQHGIPIPVTPKNPWS
MDENLMHISYEAGILENPKNQAPPGLYTKTQDPAKAPNTPDILEIEFKKGVPVKVTNVKD
GTTHQTSLELFMYLNEVAGKHGVGRIDIVENRFIGMKSRGIYETPAGTILYHAHLDIEAF
TMDREVRKIKQGLGLKFAELVYTGFWHSPECEFVRHCIAKSQERVEGKVQVSVLKGQVYI
LGRESPLSLYNEELVSMNVQGDYEPTDATGFININSLRLKEYHRLQSKVTAK
|
| Enzyme 1 Number of Residues |
412 |
| Enzyme 1 Molecular Weight |
46531 |
| Enzyme 1 Theoretical pI |
8.18 |
| Enzyme 1 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- argininosuccinate synthase activity
- binding
- catalytic activity
- ligase activity
- ligase activity, forming carbon-nitrogen bonds
- nucleotide binding
- purine nucleotide binding
|
| Process |
- arginine biosynthesis
- arginine metabolism
- metabolism
- physiological process
- urea cycle intermediate metabolism
|
| Component |
| — |
|
| Enzyme 1 General Function |
Nucleotide transport and metabolism |
| Enzyme 1 Specific Function |
ATP + L-citrulline + L-aspartate = AMP + diphosphate + omega-N-(L-arginino)succinate |
| Enzyme 1 Pathways |
- Arginine and Proline Metabolism (map00330
)
|
| Enzyme 1 Reactions |
- ATP + L-citrulline + L-aspartate = AMP + diphosphate + (N(omega)-L-arginino)succinate
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
28872  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
P00966  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
ASSY_HUMAN  |
| Enzyme 1 PDB ID |
Not Available |
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>1239 bp
ATGTCCAGCAAAGGCTCCGTGGTTCTGGCCTACAGTGGCGGCCTGGACACCTCGTGCATC
CTCGTGTGGCTGAAGGAACAAGGCTATGACGTCATTGCCTATCTGGCCAACATTGGCCAG
AAGGAAGACTTCGAGGAAGCCAGGAAGAAGGCACTGAAGCTTGGGGCCAAAAAGGTGTTC
ATTGAGGATGTCAGCAGGGAGTTTGTGGAGGAGTTCATCTGGCCGGCCATCCAGTCCAGC
GCACTGTATGAGGACCGCTACCTCCTGGGCACCTCTCTTGCCAGGCCCTGCATCGCCCGC
AAACAAGTGGAAATCGCCCAGCGGGAGGGGGCCAAGTATGTGTCCCACGGCGCCACAGGA
AAGGGGAACGATCAGGTCCGGTTTGAGCTCAGCTGCTACTCACTGGCCCCCCAGATAAAG
GTCATTGCTCCCTGGAGGATGCCTGAATTCTACAACCGGTTCAAGGGCCGCAATGACCTG
ATGGAGTACGCAAAGCAACACGGGATTCCCATCCCGGTCACTCCCAAGAACCCGTGGAGC
ATGGATGAGAACCTCATGCACATCAGCTACGAGGCTGGAATCCTGGAGAACCCCAAGAAC
CAAGCGCCTCCAGGTCTCTACACGAAGACCCAGGACCCAGCCAAAGCCCCCAACACCCCT
GACATTCTCGAGATCGAGTTCAAAAAAGGGGTCCCTGTGAAGGTGACCAACGTCAAGGAT
GGCACCACCCACCAGACCTCCTTGGAGCTCTTCATGTACCTGAACGAAGTCGCGGGCAAG
CATGGCGTGGGCCGTATTGACATCGTGGAGAACCGCTTCATTGGAATGAAGTCCCGAGGT
ATCTACGAGACCCCAGCAGGCACCATCCTTTACCATGCTCATTTAGACATCGAGGCCTTC
ACCATGGACCGGGAAGTGCGCAAAATCAAACAAGGCCTGGGCTTGAAATTTGCTGAGCTG
GTGTATACCGGTTTACGGCCTAGCCCTGAGTGTGAATTTGTCCGCCACTGCATCGCCAAG
TCCCAGGAGCGAGTGGAAGGGAAAGTGCAGGTGTCCGTCCTCAAGGGCCAGGTGTACATC
CTCGGCCGGGAGTCCCCACTGTCTCTCTACAATGAGGAGCTGGTGAGCATGAACGTGCAG
GGTGATTATGAGCCAACTGATGCCACCGGGTTCATCAACATCAATTCCCTCAGGCTGAAG
GAATATCATCGTCTCCAGAGCAAGGTCACTGCCAAATAG
|
| Enzyme 1 GenBank Gene ID |
X01630  |
| Enzyme 1 GeneCard ID |
ASS1  |
| Enzyme 1 GenAtlas ID |
ASS1  |
| Enzyme 1 HGNC ID |
HGNC:758  |
| Enzyme 1 Chromosome Location |
9 |
| Enzyme 1 Locus |
9q34.1 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- Bock HG, Su TS, O'Brien WE, Beaudet AL: Sequence for human argininosuccinate synthetase cDNA. Nucleic Acids Res. 1983 Sep 24;11(18):6505-12. [PubMed
]
- Freytag SO, Bock HG, Beaudet AL, O'Brien WE: Molecular structures of human argininosuccinate synthetase pseudogenes. Evolutionary and mechanistic implications. J Biol Chem. 1984 Mar 10;259(5):3160-6. [PubMed
]
- Haberle J, Pauli S, Linnebank M, Kleijer WJ, Bakker HD, Wanders RJ, Harms E, Koch HG: Structure of the human argininosuccinate synthetase gene and an improved system for molecular diagnostics in patients with classical and mild citrullinemia. Hum Genet. 2002 Apr;110(4):327-33. Epub 2002 Mar 1. [PubMed
]
- Isashiki Y, Noda T, Kobayashi K, Sase M, Saheki T, Titani K: Identification of essential arginine residue(s) for Mg-ATP binding of human argininosuccinate synthetase. Protein Seq Data Anal. 1989 Jul;2(4):283-7. [PubMed
]
- Ji H, Reid GE, Moritz RL, Eddes JS, Burgess AW, Simpson RJ: A two-dimensional gel database of human colon carcinoma proteins. Electrophoresis. 1997 Mar-Apr;18(3-4):605-13. [PubMed
]
- Kobayashi K, Jackson MJ, Tick DB, O'Brien WE, Beaudet AL: Heterogeneity of mutations in argininosuccinate synthetase causing human citrullinemia. J Biol Chem. 1990 Jul 5;265(19):11361-7. [PubMed
]
- Kobayashi K, Rosenbloom C, Beaudet AL, O'Brien WE: Additional mutations in argininosuccinate synthetase causing citrullinemia. Mol Biol Med. 1991 Feb;8(1):95-100. [PubMed
]
- Kobayashi K, Shaheen N, Terazono H, Saheki T: Mutations in argininosuccinate synthetase mRNA of Japanese patients, causing classical citrullinemia. Am J Hum Genet. 1994 Dec;55(6):1103-12. [PubMed
]
- Shaheen N, Kobayashi K, Terazono H, Fukushige T, Horiuchi M, Saheki T: Characterization of human wild-type and mutant argininosuccinate synthetase proteins expressed in bacterial cells. Enzyme Protein. 1994-1995;48(5-6):251-64. [PubMed
]
- Vilaseca MA, Kobayashi K, Briones P, Lambruschini N, Campistol J, Tabata A, Alomar A, Rodes M, Lluch M, Saheki T: Phenotype and genotype heterogeneity in Mediterranean citrullinemia. Mol Genet Metab. 2001 Nov;74(3):396-8. [PubMed
]
- Gao HZ, Kobayashi K, Tabata A, Tsuge H, Iijima M, Yasuda T, Kalkanoglu HS, Dursun A, Tokatli A, Coskun T, Trefz FK, Skladal D, Mandel H, Seidel J, Kodama S, Shirane S, Ichida T, Makino S, Yoshino M, Kang JH, Mizuguchi M, Barshop BA, Fuchinoue S, Seneca S, Zeesman S, Knerr I, Rodes M, Wasant P, Yoshida I, De Meirleir L, Abdul Jalil M, Begum L, Horiuchi M, Katunuma N, Nakagawa S, Saheki T: Identification of 16 novel mutations in the argininosuccinate synthetase gene and genotype-phenotype correlation in 38 classical citrullinemia patients. Hum Mutat. 2003 Jul;22(1):24-34. [PubMed
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
5946 |
| Enzyme 2 Name |
Protein-arginine deiminase type-4 |
| Enzyme 2 Synonyms |
- Protein-arginine deiminase type IV
- Peptidylarginine deiminase IV
- HL-60 PAD
|
| Enzyme 2 Gene Name |
PADI4 |
| Enzyme 2 Protein Sequence |
>Protein-arginine deiminase type-4
MAQGTLIRVTPEQPTHAVCVLGTLTQLDICSSAPEDCTSFSINASPGVVVDIAHSPPAKK
KSTGSSTWPLDPGVEVTLTMKAASGSTGDQKVQISYYGPKTPPVKALLYLTAVEISLCAD
ITRTGKVKPTRAVKDQRTWTWGPCGQGAILLVNCDRDNLESSAMDCEDDEVLDSEDLQDM
SLMTLSTKTPKDFFTNHTLVLHVARSEMDKVRVFQATRGKLSSKCSVVLGPKWPSHYLMV
PGGKHNMDFYVEALAFPDTDFPGLITLTISLLDTSNLELPEAVVFQDSVVFRVAPWIMTP
NTQPPQEVYACSIFENEDFLKSVTTLAMKAKCKLTICPEEENMDDQWMQDEMEIGYIQAP
HKTLPVVFDSPRNRGLKEFPIKRVMGPDFGYVTRGPQTGGISGLDSFGNLEVSPPVTVRG
KEYPLGRILFGDSCYPSNDSRQMHQALQDFLSAQQVQAPVKLYSDWLSVGHVDEFLSFVP
APDRKGFRLLLASPRSCYKLFQEQQNEGHGEALLFEGIKKKKQQKIKNILSNKTLREHNS
FVERCIDWNRELLKRELGLAESDIIDIPQLFKLKEFSKAEAFFPNMVNMLVLGKHLGIPK
PFGPVINGRCCLEEKVCSLLEPLGLQCTFINDFFTYHIRHGEVHCGTNVRRKPFSFKWWN
MVP
|
| Enzyme 2 Number of Residues |
663 |
| Enzyme 2 Molecular Weight |
74096 |
| Enzyme 2 Theoretical pI |
6.56 |
| Enzyme 2 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
- protein-arginine deiminase activity
|
| Process |
- biopolymer metabolism
- biopolymer modification
- macromolecule metabolism
- metabolism
- physiological process
- protein modification
|
| Component |
| — |
|
| Enzyme 2 General Function |
Not Available |
| Enzyme 2 Specific Function |
Catalyzes the citrullination/deimination of arginine residues of proteins. Citrullinates histone H3 at 'Arg-8' and/or 'Arg-17' and histone H4 at 'Arg-3', which prevents their methylation by CARM1 and HRMT1L2/PRMT1 and represses transcription. Citrullinates EP300/P300 at 'Arg-2142', which favors its interaction with NCOA2/GRIP1 |
| Enzyme 2 Pathways |
Not Available |
| Enzyme 2 Reactions |
- protein L-arginine + H2O = protein L-citrulline + NH3
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
5913971  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
Q9UM07  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
PADI4_HUMAN  |
| Enzyme 2 PDB ID |
1WD8  |
| Enzyme 2 PDB File |
Show |
| Enzyme 2 3D Structure |
|
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>1992 bp
ATGGCCCAGGGGACATTGATCCGTGTGACCCCAGAGCAGCCCACCCATGCCGTGTGTGTG
CTGGGCACCTTGACTCAGCTTGACATCTGCAGCTCTGCCCCTGAGGACTGCACGTCCTTC
AGCATCAACGCCTCCCCAGGGGTGGTCGTGGATATTGCCCACAGCCCTCCAGCCAAGAAG
AAATCCACAGGTTCCTCCACATGGCCCCTGGACCCTGGGGTAGAGGTGACCCTGACGATG
AAAGCGGCCAGTGGTAGCACAGGCGACCAGAAGGTTCAGATTTCATACTACGGACCCAAG
ACTCCACCAGTCAAAGCTCTACTCTACCTCACCGCGGTGGAAATCTCCCTGTGCGCAGAC
ATCACCCGCACCGGCAAAGTGAAGCCAACCAGAGCTGTGAAAGATCAGAGGACCTGGACC
TGGGGCCCTTGTGGACAGGGTGCCATCCTGCTGGTGAACTGTGACAGAGACAATCTCGAA
TCTTCTGCCATGGACTGCGAGGATGATGAAGTGCTTGACAGCGAAGACCTGCAGGACATG
TCGCTGATGACCCTGAGCACGAAGACCCCCAAGGACTTCTTCACAAACCATACACTGGTG
CTCCACGTGGCCAGGTCTGAGATGGACAAAGTGAGGGTGTTTCAGGCCACACGGGGCAAA
CTGTCCTCCAAGTGCAGCGTAGTCTTGGGTCCCAAGTGGCCCTCTCACTACCTGATGGTC
CCCGGTGGAAAGCACAACATGGACTTCTACGTGGAGGCCCTCGCTTTCCCGGACACCGAC
TTCCCGGGGCTCATTACCCTCACCATCTCCCTGCTGGACACGTCCAACCTGGAGCTCCCC
GAGGCTGTGGTGTTCCAAGACAGCGTGGTCTTCCGCGTGGCGCCCTGGATCATGACCCCC
AACACCCAGCCCCCGCAGGAGGTGTACGCGTGCAGTATTTTTGAAAATGAGGACTTCCTG
AAGTCAGTGACTACTCTGGCCATGAAAGCCAAGTGCAAGCTGACCATCTGCCCTGAGGAG
GAGAACATGGATGACCAGTGGATGCAGGATGAAATGGAGATCGGCTACATCCAAGCCCCA
CACAAAACGCTGCCCGTGGTCTTCGACTCTCCAAGGAACAGAGGCCTGAAGGAGTTTCCC
ATCAAACGAGTGATGGGTCCAGATTTTGGCTATGTAACTCGAGGGCCCCAAACAGGGGGT
ATCAGTGGACTGGACTCCTTTGGGAACCTGGAAGTGAGCCCCCCAGTCACAGTCAGGGGC
AAGGAATACCCGCTGGGCAGGATTCTCTTCGGGGACAGCTGTTATCCCAGCAATGACAGC
CGGCAGATGCACCAGGCCCTGCAGGACTTCCTCAGTGCCCAGCAGGTGCAGGCCCCTGTG
AAGCTCTATTCTGACTGGCTGTCCGTGGGCCACGTGGACGAGTTCCTGAGCTTTGTGCCA
GCACCCGACAGGAAGGGCTTCCGGCTGCTCCTGGCCAGCCCCAGGTCCTGCTACAAACTG
TTCCAGGAGCAGCAGAATGAGGGCCACGGGGAGGCCCTGCTGTTCGAAGGGATCAAGAAA
AAAAAACAGCAGAAAATAAAGAACATTCTGTCAAACAAGACATTGAGAGAACATAATTCA
TTTGTGGAGAGATGCATCGACTGGAACCGCGAGCTGCTGAAGCGGGAGCTGGGCCTGGCC
GAGAGTGACATCATTGACATCCCGCAGCTCTTCAAGCTCAAAGAGTTCTCTAAGGCGGAA
GCTTTTTTCCCCAACATGGTGAACATGCTGGTGCTAGGGAAGCACCTGGGCATCCCCAAG
CCCTTCGGGCCCGTCATCAACGGCCGCTGCTGCCTGGAGGAGAAGGTGTGTTCCCTGCTG
GAGCCACTGGGCCTCCAGTGCACCTTCATCAACGACTTCTTCACCTACCACATCAGGCAT
GGGGAGGTGCACTGCGGCACCAACGTGCGCAGAAAGCCCTTCTCCTTCAAGTGGTGGAAC
ATGGTGCCCTGA
|
| Enzyme 2 GenBank Gene ID |
AB017919  |
| Enzyme 2 GeneCard ID |
PADI4  |
| Enzyme 2 GenAtlas ID |
PADI4  |
| Enzyme 2 HGNC ID |
HGNC:18368  |
| Enzyme 2 Chromosome Location |
1 |
| Enzyme 2 Locus |
1p36.13 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- Nakashima K, Hagiwara T, Ishigami A, Nagata S, Asaga H, Kuramoto M, Senshu T, Yamada M: Molecular characterization of peptidylarginine deiminase in HL-60 cells induced by retinoic acid and 1alpha,25-dihydroxyvitamin D(3). J Biol Chem. 1999 Sep 24;274(39):27786-92. [PubMed
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
5950 |
| Enzyme 3 Name |
Protein-arginine deiminase type-3 |
| Enzyme 3 Synonyms |
- Protein-arginine deiminase type III
- Peptidylarginine deiminase III
|
| Enzyme 3 Gene Name |
PADI3 |
| Enzyme 3 Protein Sequence |
>Protein-arginine deiminase type-3
MSLQRIVRVSLEHPTSAVCVAGVETLVDIYGSVPEGTEMFEVYGTPGVDIYISPNMERGR
ERADTRRWRFDATLEIIVVMNSPSNDLNDSHVQISYHSSHEPLPLAYAVLYLTCVDISLD
CDLNCEGRQDRNFVDKRQWVWGPSGYGGILLVNCDRDDPSCDVQDNCDQHVHCLQDLEDM
SVMVLRTQGPAALFDDHKLVLHTSSYDAKRAQVFHICGPEDVCEAYRHVLGQDKVSYEVP
RLHGDEERFFVEGLSFPDAGFTGLISFHVTLLDDSNEDFSASPIFTDTVVFRVAPWIMTP
STLPPLEVYVCRVRNNTCFVDAVAELARKAGCKLTICPQAENRNDRWIQDEMELGYVQAP
HKTLPVVFDSPRNGELQDFPYKRILGPDFGYVTREPRDRSVSGLDSFGNLEVSPPVVANG
KEYPLGRILIGGNLPGSSGRRVTQVVRDFLHAQKVQPPVELFVDWLAVGHVDEFLSFVPA
PDGKGFRMLLASPGACFKLFQEKQKCGHGRALLFQGVVDDEQVKTISINQVLSNKDLINY
NKFVQSCIDWNREVLKRELGLAECDIIDIPQLFKTERKKATAFFPDLVNMLVLGKHLGIP
KPFGPIINGCCCLEEKVRSLLEPLGLHCTFIDDFTPYHMLHGEVHCGTNVCRKPFSFKWW
NMVP
|
| Enzyme 3 Number of Residues |
664 |
| Enzyme 3 Molecular Weight |
74744 |
| Enzyme 3 Theoretical pI |
5.22 |
| Enzyme 3 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
- protein-arginine deiminase activity
|
| Process |
- biopolymer metabolism
- biopolymer modification
- macromolecule metabolism
- metabolism
- physiological process
- protein modification
|
| Component |
| — |
|
| Enzyme 3 General Function |
Not Available |
| Enzyme 3 Specific Function |
Catalyzes the deimination of arginine residues of proteins |
| Enzyme 3 Pathways |
Not Available |
| Enzyme 3 Reactions |
- protein L-arginine + H2O = protein L-citrulline + NH3
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
6172379  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
Q9ULW8  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
PADI3_HUMAN  |
| Enzyme 3 PDB ID |
Not Available |
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>1995 bp
ATGTCGCTGCAGAGAATCGTGCGTGTGTCCCTGGAGCATCCCACCAGCGCGGTGTGTGTG
GCTGGCGTGGAGACCCTCGTGGACATTTATGGGTCAGTGCCTGAGGGCACAGAAATGTTT
GAGGTCTATGGGACGCCTGGCGTGGACATCTACATCTCTCCCAACATGGAGAGGGGCCGG
GAGCGTGCAGACACCAGGCGGTGGCGCTTTGACGCGACTTTGGAGATCATCGTGGTCATG
AACTCCCCCAGCAATGACCTCAACGACAGCCATGTTCAGATTTCCTACCACTCCAGCCAT
GAGCCTCTGCCCCTAGCCTATGCGGTGCTCTACCTCACCTGTGTTGACATCTCTCTGGAT
TGCGACCTGAACTGTGAGGGAAGGCAGGACAGGAACTTTGTAGACAAGCGGCAGTGGGTC
TGGGGGCCCAGTGGGTATGGCGGCATCTTGCTGGTGAACTGTGACCGTGATGATCCGAGC
TGTGATGTCCAGGACAATTGTGACCAGCACGTGCACTGCCTGCAAGACCTGGAAGACATG
TCTGTCATGGTCCTGCGGACGCAGGGCCCTGCAGCCCTCTTTGATGACCACAAACTTGTC
CTCCATACCTCCAGCTATGATGCCAAACGGGCACAGGTCTTCCACATCTGCGGTCCTGAG
GATGTGTGTGAGGCCTATAGGCATGTGCTGGGCCAAGATAAGGTGTCCTATGAGGTACCC
CGCTTGCATGGGGATGAGGAGCGCTTCTTCGTGGAAGGCCTGTCCTTCCCTGATGCCGGC
TTCACAGGACTCATCTCCTTCCATGTCACTCTGCTGGACGACTCCAACGAGGATTTCTCG
GCATCCCCTATCTTCACTGACACTGTGGTGTTCCGAGTGGCACCCTGGATCATGACGCCC
AGCACTCTGCCACCCCTAGAGGTGTATGTGTGCCGTGTGAGGAACAACACGTGTTTTGTG
GATGCGGTGGCAGAGCTGGCCAGGAAGGCCGGCTGCAAGCTGACCATCTGCCCACAGGCC
GAGAACCGCAACGACCGCTGGATCCAGGATGAGATGGAGCTGGGCTACGTTCAGGCGCCG
CACAAGACCCTCCCGGTGGTCTTTGACTCCCCAAGGAATGGGGAACTGCAGGATTTCCCT
TACAAAAGAATCCTGGGTCCAGATTTTGGTTACGTGACTCGGGAACCACGCGACAGGTCT
GTGAGTGGCCTGGACTCCTTTGGGAACCTGGAGGTCAGCCCTCCAGTGGTGGCCAATGGG
AAAGAGTACCCCCTGGGGAGGATCCTCATTGGGGGCAACCTGCCTGGGTCAAGTGGCCGC
AGGGTCACCCAGGTGGTGCGGGACTTCCTCCATGCCCAGAAGGTGCAGCCCCCCGTGGAG
CTCTTTGTGGACTGGTTGGCCGTGGGCCATGTGGATGAGTTTCTGAGCTTTGTCCCTGTC
CCCGATGGGAAGGGCTTCCGGATGCTCCTGGCCAGCCCTGGGGCCTGCTTCAAGCTCTTC
CAGGAAAAGCAGAAGTGTGGCCACGGGAGGGCCCTCCTGTTCCAGGGGGTTGTTGATGAT
GAGCAGGTCAAGACCATCTCCATCAACCAGGTGCTCTCCAATAAAGACCTCATCAACTAC
AATAAGTTTGTGCAGAGCTGCATCGACTGGAACCGTGAGGTGCTGAAGCGGGAGCTGGGC
CTGGCAGAGTGTGACATCATTGACATCCCACAGCTCTTCAAGACCGAGAGGAAAAAAGCA
ACGGCCTTCTTCCCTGACTTGGTGAACATGCTGGTGCTGGGGAAGCACCTGGGCATCCCC
AAGCCCTTTGGGCCCATCATCAATGGCTGCTGCTGCCTGGAGGAGAAGGTGCGGTCCCTG
CTGGAGCCTCTGGGCCTCCACTGCACCTTCATTGATGACTTCACTCCATACCACATGCTG
CATGGGGAGGTGCACTGTGGCACCAATGTGTGCAGAAAGCCCTTCTCTTTCAAGTGGTGG
AACATGGTGCCCTGA
|
| Enzyme 3 GenBank Gene ID |
AB026831  |
| Enzyme 3 GeneCard ID |
PADI3  |
| Enzyme 3 GenAtlas ID |
PADI3  |
| Enzyme 3 HGNC ID |
HGNC:18337  |
| Enzyme 3 Chromosome Location |
1 |
| Enzyme 3 Locus |
1p36.13 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- Kanno T, Kawada A, Yamanouchi J, Yosida-Noro C, Yoshiki A, Shiraiwa M, Kusakabe M, Manabe M, Tezuka T, Takahara H: Human peptidylarginine deiminase type III: molecular cloning and nucleotide sequence of the cDNA, properties of the recombinant enzyme, and immunohistochemical localization in human skin. J Invest Dermatol. 2000 Nov;115(5):813-23. [PubMed
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
6045 |
| Enzyme 4 Name |
NG,NG-dimethylarginine dimethylaminohydrolase 2 |
| Enzyme 4 Synonyms |
- Dimethylargininase-2
- Dimethylarginine dimethylaminohydrolase 2
- DDAHII
- DDAH-2
- S-phase protein
- Protein G6a
|
| Enzyme 4 Gene Name |
DDAH2 |
| Enzyme 4 Protein Sequence |
>NG,NG-dimethylarginine dimethylaminohydrolase 2
MGTPGEGLGRCSHALIRGVPESLASGEGAGAGLPALDLAKAQREHGVLGGKLRQRLGLQL
LELPPEESLPLGPLLGDTAVIQGDTALITRPWSPARRPEVDGVRKALQDLGLRIVEIGDE
NATLDGTDVLFTGREFFVGLSKWTNHRGAEIVADTFRDFAVSTVPVSGPSHLRGLCGMGG
PRTVVAGSSDAAQKAVRAMAVLTDHPYASLTLPDDAAADCLFLRPGLPGVPPFLLHRGGG
DLPNSQEALQKLSDVTLVPVSCSELEKAGAGLSSLCLVLSTRPHS
|
| Enzyme 4 Number of Residues |
285 |
| Enzyme 4 Molecular Weight |
29644 |
| Enzyme 4 Theoretical pI |
5.90 |
| Enzyme 4 GO Classification |
Not Available |
| Enzyme 4 General Function |
Amino acid transport and metabolism |
| Enzyme 4 Specific Function |
Hydrolyzes N(G),N(G)-dimethyl-L-arginine (ADMA) and N(G)-monomethyl-L-arginine (MMA) which act as inhibitors of NOS. Has therefore a role in nitric oxide generation |
| Enzyme 4 Pathways |
Not Available |
| Enzyme 4 Reactions |
- N(G),N(G)-dimethyl-L-arginine + H2O = dimethylamine + L-citrulline
|
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
4454710  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
O95865  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
DDAH2_HUMAN  |
| Enzyme 4 PDB ID |
Not Available |
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
>858 bp
ATGGGGACGCCGGGGGAGGGGCTGGGCCGCTGCTCCCATGCCCTGATCCGGGGAGTCCCA
GAGAGCCTGGCGTCGGGGGAAGGTGCGGGGGCTGGCCTTCCCGCTCTGGATCTGGCCAAA
GCTCAAAGGGAGCACGGGGTGCTGGGAGGTAAACTGAGGCAACGACTGGGGCTACAGCTG
CTAGAACTGCCACCTGAGGAGTCATTGCCGCTGGGACCGCTGCTTGGCGACACGGCCGTG
ATCCAAGGGGACACGGCCCTAATCACGCGGCCCTGGAGCCCCGCTCGTAGGCCAGAGGTC
GATGGAGTCCGCAAAGCCCTGCAAGACCTGGGGCTCCGAATTGTGGAAATAGGAGACGAG
AACGCGACGCTGGATGGCACTGACGTTCTCTTCACCGGCCGGGAGTTTTTCGTAGGCCTC
TCCAAATGGACCAATCACCGAGGAGCTGAGATCGTGGCGGACACGTTCCGGGACTTCGCC
GTCTCCACTGTGCCAGTCTCGGGTCCCTCCCACCTGCGCGGTCTCTGCGGCATGGGGGGA
CCTCGCACTGTTGTGGCAGGCAGCAGCGACGCTGCCCAAAAGGCTGTCCGGGCAATGGCA
GTGCTGACAGATCACCCATATGCCTCCCTGACCCTCCCAGATGACGCAGCTGCTGACTGC
CTCTTTCTTCGTCCTGGGTTGCCTGGTGTGCCCCCTTTCCTCCTGCACCGTGGAGGTGGG
GATCTGCCCAACAGCCAGGAGGCACTGCAGAAGCTCTCTGATGTCACCCTGGTACCTGTG
TCCTGCTCAGAACTGGAGAAGGCTGGCGCCGGGCTCAGCTCCCTCTGCTTGGTGCTCAGC
ACACGCCCCCACAGCTGA
|
| Enzyme 4 GenBank Gene ID |
AF070667  |
| Enzyme 4 GeneCard ID |
DDAH2  |
| Enzyme 4 GenAtlas ID |
DDAH2  |
| Enzyme 4 HGNC ID |
HGNC:2716  |
| Enzyme 4 Chromosome Location |
6 |
| Enzyme 4 Locus |
6p21.3 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
- Leiper JM, Santa Maria J, Chubb A, MacAllister RJ, Charles IG, Whitley GS, Vallance P: Identification of two human dimethylarginine dimethylaminohydrolases with distinct tissue distributions and homology with microbial arginine deiminases. Biochem J. 1999 Oct 1;343 Pt 1:209-14. [PubMed
]
- Ribas G, Neville M, Wixon JL, Cheng J, Campbell RD: Genes encoding three new members of the leukocyte antigen 6 superfamily and a novel member of Ig superfamily, together with genes encoding the regulatory nuclear chloride ion channel protein (hRNCC) and an N omega-N omega-dimethylarginine dimethylaminohydrolase homologue, are found in a 30-kb segment of the MHC class III region. J Immunol. 1999 Jul 1;163(1):278-87. [PubMed
]
- Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed
]
|
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
6214 |
| Enzyme 5 Name |
Nitric oxide synthase, inducible |
| Enzyme 5 Synonyms |
- NOS type II
- Inducible NO synthase
- Inducible NOS
- iNOS
- Hepatocyte NOS
- HEP- NOS
|
| Enzyme 5 Gene Name |
NOS2A |
| Enzyme 5 Protein Sequence |
>Nitric oxide synthase, inducible
MACPWKFLFKTKFHQYAMNGEKDINNNVEKAPCATSSPVTQDDLQYHNLSKQQNESPQPL
VETGKKSPESLVKLDATPLSSPRHVRIKNWGSGMTFQDTLHHKAKGILTCRSKSCLGSIM
TPKSLTRGPRDKPTPPDELLPQAIEFVNQYYGSFKEAKIEEHLARVEAVTKEIETTGTYQ
LTGDELIFATKQAWRNAPRCIGRIQWSNLQVFDARSCSTAREMFEHICRHVRYSTNNGNI
RSAITVFPQRSDGKHDFRVWNAQLIRYAGYQMPDGSIRGDPANVEFTQLCIDLGWKPKYG
RFDVVPLVLQANGRDPELFEIPPDLVLEVAMEHPKYEWFRELELKWYALPAVANMLLEVG
GLEFPGCPFNGWYMGTEIGVRDFCDVQRYNILEEVGRRMGLETHKLASLWKDQAVVEINI
AVLHSFQKQNVTIMDHHSAAESFMKYMQNEYRSRGGCPADWIWLVPPMSGSITPVFHQEM
LNYVLSPFYYYQVEAWKTHVWQDEKRRPKRREIPLKVLVKAVLFACMLMRKTMASRVRVT
ILFATETGKSEALAWDLGALFSCAFNPKVVCMDKYRLSCLEEERLLLVVTSTFGNGDCPG
NGEKLKKSLFMLKELNNKFRYAVFGLGSSMYPRFCAFAHDIDQKLSHLGASQLTPMGEGD
ELSGQEDAFRSWAVQTFKAACETFDVRGKQHIQIPKLYTSNVTWDPHHYRLVQDSQPLDL
SKALSSMHAKNVFTMRLKSRQNLQSPTSSRATILVELSCEDGQGLNYLPGEHLGVCPGNQ
PALVQGILERVVDGPTPHQTVRLEALDESGSYWVSDKRLPPCSLSQALTYFLDITTPPTQ
LLLQKLAQVATEEPERQRLEALCQPSEYSKWKFTNSPTFLEVLEEFPSLRVSAGFLLSQL
PILKPRFYSISSSRDHTPTEIHLTVAVVTYHTRDGQGPLHHGVCSTWLNSLKPQDPVPCF
VRNASGFHLPEDPSHPCILIGPGTGIAPFRSFWQQRLHDSQHKGVRGGRMTLVFGCRRPD
EDHIYQEEMLEMAQKGVLHAVHTAYSRLPGKPKVYVQDILRQQLASEVLRVLHKEPGHLY
VCGDVRMARDVAHTLKQLVAAKLKLNEEQVEDYFFQLKSQKRYHEDIFGAVFPYEAKKDR
VAVQPSSLEMSAL
|
| Enzyme 5 Number of Residues |
1153 |
| Enzyme 5 Molecular Weight |
131119 |
| Enzyme 5 Theoretical pI |
8.01 |
| Enzyme 5 GO Classification |
| Function |
- FAD binding
- FMN binding
- NADP binding
- adenyl nucleotide binding
- binding
- calmodulin binding
- catalytic activity
- cation binding
- coenzyme binding
- cofactor binding
- electron transporter activity
- heme binding
- ion binding
- iron ion binding
- monooxygenase activity
- nitric-oxide synthase activity
- nucleotide binding
- oxidoreductase activity
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD or NADH as one donor, and incorporation of one atom of oxygen
- protein binding
- purine nucleotide binding
- tetrapyrrole binding
- transition metal ion binding
- transporter activity
|
| Process |
- biosynthesis
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- nitric oxide biosynthesis
- physiological process
|
| Component |
| — |
|
| Enzyme 5 General Function |
Inorganic ion transport and metabolism |
| Enzyme 5 Specific Function |
Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In macrophages, NO mediates tumoricidal and bactericidal actions |
| Enzyme 5 Pathways |
- Arginine and Proline Metabolism (map00330
)
|
| Enzyme 5 Reactions |
- L-arginine + n NADPH + n H+ + m O2 = citrulline + nitric oxide + n NADP+
|
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
292242  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
P35228  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
NOS2A_HUMAN  |
| Enzyme 5 PDB ID |
Not Available |
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
>3462 bp
ATGGCCTGTCCTTGGAAATTTCTGTTCAAGACCAAATTCCACCAGTATGCAATGAATGGG
GAAAAAGACATCAACAACAATGTGGAGAAAGCCCCCTGTGCCACCTCCAGTCCAGTGACA
CAGGATGACCTTCAGTATCACAACCTCAGCAAGCAGCAGAATGAGTCCCCGCAGCCCCTC
GTGGAGACGGGAAAGAAGTCTCCAGAATCTCTGGTCAAGCTGGATGCAACCCCATTGTCC
TCCCCACGGCATGTGAGGATCAAAAACTGGGGCAGCGGGATGACTTTCCAAGACACACTT
CACCATAAGGCCAAAGGGATTTTAACTTGCAGGTCCAAATCTTGCCTGGGGTCCATTATG
ACTCCCAAAAGTTTGACCAGAGGACCCAGGGACAAGCCTACCCCTCCAGATGAGCTTCTA
CCTCAAGCTATCGAATTTGTCAACCAATATTACGGCTCCTTCAAAGAGGCAAAAATAGAG
GAACATCTGGCCAGGGTGGAAGCGGTAACAAAGGAGATAGAAACAACAGGAACCTACCAA
CTGACGGGAGATGAGCTCATCTTCGCCACCAAGCAGGCCTGGCGCAATGCCCCACGCTGC
ATTGGGAGGATCCAGTGGTCCAACCTGCAGGTCTTCGATGCCCGCAGCTGTTCCACTGCC
CGGGAAATGTTTGAACACATCTGCAGACACGTGCGTTACTCCACCAACAATGGCAACATC
AGGTCGGCCATCACCGTGTTCCCCCAGCGGAGTGATGGCAAGCACGACTTCCGGGTGTGG
AATGCTCAGCTCATCCGCTATGCTGGCTACCAGATGCCAGATGGCAGCATCAGAGGGGAC
CCTGCCAACGTGGAATTCACTCAGCTGTGCATCGACCTGGGCTGGAAGCCCAAGTACGGC
CGCTTCGATGTGGTCCCCCTGGTCCTGCAGGCCAATGGCCGTGACCCTGAGCTCTTCGAA
ATCCCACCTGACCTTGTGCTTGAGGTGGCCATGGAACATCCCAAATACGAGTGGTTTCGG
GAACTGGAGCTAAAGTGGTACGCCCTGCCTGCAGTGGCCAACATGCTGCTTGAGGTGGGC
GGCCTGGAGTTCCCAGGGTGCCCCTTCAATGGCTGGTACATGGGCACAGAGATCGGAGTC
CGGGACTTCTGTGACGTCCAGCGCTACAACATCCTGGAGGAAGTGGGCAGGAGAATGGGC
CTGGAAACGCACAAGCTGGCCTCGCTCTGGAAAGACCAGGCTGTCGTTGAGATCAACATT
GCTGTGATCCATAGTTTTCAGAAGCAGAATGTGACCATCATGGACCACCACTCGGCTGCA
GAATCCTTCATGAAGTACATGCAGAATGAATACCGGTCCCGTGGGGGCTGCCCGGCAGAC
TGGATTTGGCTGGTCCCTCCCATGTCTGGGAGCATCACCCCCGTGTTTCACCAGGAGATG
CTGAACTACGTCCTGTCCCCTTTCTACTACTATCAGGTAGAGGCCTGGAAAACCCATGTC
TGGCAGGACGAGAAGCGGAGACCCAAGAGAAGAGAGATTCCATTGAAAGTCTTGGTCAAA
GCTGTGCTCTTTGCCTGTATGCTGATGCGCAAGACAATGGCGTCCCGAGTCAGAGTCACC
ATCCTCTTTGCGACAGAGACAGGAAAATCAGAGGCGCTGGCCTGGGACCTGGGGGCCTTA
TTCAGCTGTGCCTTCAACCCCAAGGTTGTCTGCATGGATAAGTACAGGCTGAGCTGCCTG
GAGGAGGAACGGCTGCTGTTGGTGGTGACCAGTACGTTTGGCAATGGAGACTGCCCTGGC
AATGGAGAGAAACTGAAGAAATCGCTCTTCATGCTGAAAGAGCTCAACAACAAATTCAGG
TACGCTGTGTTTGGCCTCGGCTCCAGCATGTACCCTCGGTTCTGCGCCTTTGCTCATGAC
ATTGATCAGAAGCTGTCCCACCTGGGGGCCTCTCAGCTCACCCCGATGGGAGAAGGGGAT
GAGCTCAGTGGGCAGGAGGACGCCTTCCGCAGCTGGGCCGTGCAAACCTTCAAGGCAGCC
TGTGAGACGTTTGATGTCCGAGGCAAACAGCACATTCAGATCCCCAAGCTCTACACCTCC
AATGTGACCTGGGACCCGCACCACTACAGGCTCGTGCAGGACTCACAGCCTTTGGACCTC
AGCAAAGCCCTCAGCAGCATGCATGCCAAGAACGTGTTCACCATGAGGCTCAAATCTCGG
CAGAATCTACAAAGTCCGACATCCAGCCGTGCCACCATCCTGGTGGAACTCTCCTGTGAG
GATGGCCAAGGCCTGAACTACCTGCCGGGGGAGCACCTTGGGGTTTGCCCAGGCAACCAG
CCGGCCCTGGTCCAAGGCATCCTGGAGCGAGTGGTGGATGGCCCCACACCCCACCAGACA
GTGCGCCTGGAGGACCTGGATGAGAGTGGCAGCTACTGGGTCAGTGACAAGAGGCTGCCC
CCCTGCTCACTCAGCCAGGCCCTCACCTACTCCCCGGACATCACCACACCCCCAACCCAG
CTGCTGCTCCAAAAGCTGGCCCAGGTGGCCACAGAAGAGCCTGAGAGACAGAGGCTGGAG
GCCCTGTGCCAGCCCTCAGAGTACAGCAAGTGGAAGTTCACCAACAGCCCCACATTCCTG
GAGGTGCTAGAGGAGTTCCCGTCCCTGCGGGTGTCTGCTGGCTTCCTGCTTTCCCAGCTC
CCCATTCTGAAGCCCAGGTTCTACTCCATCAGCTCCTCCCGGGATCACACGCCCACGGAG
ATCCACCTGACTGTGGCCGTGGTCACCTACCACACCGGAGATGGCCAGGGTCCCCTGCAC
CACGGTGTCTGCAGCACATGGCTCAACAGCCTGAAGCCCCAAGACCCAGTGCCCTGCTTT
GTGCGGAATGCCAGCGCCTTCCACCTCCCCGAGGATCCCTCCCATCCTTGCATCCTCATC
GGGCCTGGCACAGGCATCGTGCCCTTCCGCAGTTTCTGGCAGCAACGGCTCCATGACTCC
CAGCACAAGGGAGTGCGGGGAGGCCGCATGACCTTGGTGTTTGGGTGCCGCCGCCCAGAT
GAGGACCACATCTACCAGGAGGAGATGCTGGAGATGGCCCAGAAGGGGGTGCTGCATGCG
GTGCACACAGCCTATTCCCGCCTGCCTGGCAAGCCCAAGGTCTATGTTCAGGACATCCTG
CGGCAGCAGCTGGCCAGCGAGGTGCTCCGTGTGCTCCACAAGGAGCCAGGCCACCTCTAT
GTTTGCGGGGATGTGCGCATGGCCCGGGACGTGGCCCACACCCTGAAGCAGCTGGTGGCT
GCCAAGCTGAAATTGAATGAGGAGCAGGTCGAGGACTATTTCTTTCAGCTCAAGAGCCAG
AAGCGCTATCACGAAGATATCTTCGGTGCTGTATTTCCTTACGAGGCGAAGAAGGACAGG
GTGGCGGTGCAGCCCAGCAGCCTGGAGATGTCAGCGCTCTGA
|
| Enzyme 5 GenBank Gene ID |
L09210  |
| Enzyme 5 GeneCard ID |
NOS2A  |
| Enzyme 5 GenAtlas ID |
NOS2A  |
| Enzyme 5 HGNC ID |
HGNC:7873  |
| Enzyme 5 Chromosome Location |
17 |
| Enzyme 5 Locus |
17q11.2-q12 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
- Geller DA, Lowenstein CJ, Shapiro RA, Nussler AK, Di Silvio M, Wang SC, Nakayama DK, Simmons RL, Snyder SH, Billiar TR: Molecular cloning and expression of inducible nitric oxide synthase from human hepatocytes. Proc Natl Acad Sci U S A. 1993 Apr 15;90(8):3491-5. [PubMed
]
- Sherman PA, Laubach VE, Reep BR, Wood ER: Purification and cDNA sequence of an inducible nitric oxide synthase from a human tumor cell line. Biochemistry. 1993 Nov 2;32(43):11600-5. [PubMed
]
- Charles IG, Palmer RM, Hickery MS, Bayliss MT, Chubb AP, Hall VS, Moss DW, Moncada S: Cloning, characterization, and expression of a cDNA encoding an inducible nitric oxide synthase from the human chondrocyte. Proc Natl Acad Sci U S A. 1993 Dec 1;90(23):11419-23. [PubMed
]
- Maier R, Bilbe G, Rediske J, Lotz M: Inducible nitric oxide synthase from human articular chondrocytes: cDNA cloning and analysis of mRNA expression. Biochim Biophys Acta. 1994 Sep 21;1208(1):145-50. [PubMed
]
- Park CS, Pardhasaradhi K, Gianotti C, Villegas E, Krishna G: Human retina expresses both constitutive and inducible isoforms of nitric oxide synthase mRNA. Biochem Biophys Res Commun. 1994 Nov 30;205(1):85-91. [PubMed
]
- Hokari A, Zeniya M, Esumi H: Cloning and functional expression of human inducible nitric oxide synthase (NOS) cDNA from a glioblastoma cell line A-172. J Biochem (Tokyo). 1994 Sep;116(3):575-81. [PubMed
]
- Guo FH, De Raeve HR, Rice TW, Stuehr DJ, Thunnissen FB, Erzurum SC: Continuous nitric oxide synthesis by inducible nitric oxide synthase in normal human airway epithelium in vivo. Proc Natl Acad Sci U S A. 1995 Aug 15;92(17):7809-13. [PubMed
]
- Luss H, Li RK, Shapiro RA, Tzeng E, McGowan FX, Yoneyama T, Hatakeyama K, Geller DA, Mickle DA, Simmons RL, Billiar TR: Dedifferentiated human ventricular cardiac myocytes express inducible nitric oxide synthase mRNA but not protein in response to IL-1, TNF, IFNgamma, and LPS. J Mol Cell Cardiol. 1997 Apr;29(4):1153-65. [PubMed
]
- McLay JS, Chatterjee P, Nicolson AG, Jardine AG, McKay NG, Ralston SH, Grabowski P, Haites NE, MacLeod AM, Hawksworth GM: Nitric oxide production by human proximal tubular cells: a novel immunomodulatory mechanism? Kidney Int. 1994 Oct;46(4):1043-9. [PubMed
]
- Bloch KD, Wolfram JR, Brown DM, Roberts JD Jr, Zapol DG, Lepore JJ, Filippov G, Thomas JE, Jacob HJ, Bloch DB: Three members of the nitric oxide synthase II gene family (NOS2A, NOS2B, and NOS2C) colocalize to human chromosome 17. Genomics. 1995 Jun 10;27(3):526-30. [PubMed
]
- Taylor BS, Alarcon LH, Billiar TR: Inducible nitric oxide synthase in the liver: regulation and function. Biochemistry (Mosc). 1998 Jul;63(7):766-81. [PubMed
]
- Glynne PA, Darling KE, Picot J, Evans TJ: Epithelial inducible nitric-oxide synthase is an apical EBP50-binding protein that directs vectorial nitric oxide output. J Biol Chem. 2002 Sep 6;277(36):33132-8. Epub 2002 Jun 21. [PubMed
]
- Li H, Raman CS, Glaser CB, Blasko E, Young TA, Parkinson JF, Whitlow M, Poulos TL: Crystal structures of zinc-free and -bound heme domain of human inducible nitric-oxide synthase. Implications for dimer stability and comparison with endothelial nitric-oxide synthase. J Biol Chem. 1999 Jul 23;274(30):21276-84. [PubMed
]
- Fischmann TO, Hruza A, Niu XD, Fossetta JD, Lunn CA, Dolphin E, Prongay AJ, Reichert P, Lundell DJ, Narula SK, Weber PC: Structural characterization of nitric oxide synthase isoforms reveals striking active-site conservation. Nat Struct Biol. 1999 Mar;6(3):233-42. [PubMed
]
|
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
6215 |
| Enzyme 6 Name |
Ornithine carbamoyltransferase, mitochondrial precursor |
| Enzyme 6 Synonyms |
- OTCase
- Ornithine transcarbamylase
|
| Enzyme 6 Gene Name |
OTC |
| Enzyme 6 Protein Sequence |
>Ornithine carbamoyltransferase, mitochondrial precursor
MLFNLRILLNNAAFRNGHNFMVRNFRCGQPLQNKVQLKGRDLLTLKNFTGEEIKYMLWLS
ADLKFRIKQKGEYLPLLQGKSLGMIFEKRSTRTRLSTETGFALLGGHPCFLTTQDIHLGV
NESLTDTARVLSSMADAVLARVYKQSDLDTLAKEASIPIINGLSDLYHPIQILADYLTLQ
EHYSSLKGLTLSWIGDGNNILHSIMMSAAKFGMHLQAATPKGYEPDASVTKLAEQYAKEN
GTKLLLTNDPLEAAHGGNVLITDTWISMGQEEEKKKRLQAFQGYQVTMKTAKVAASDWTF
LHCLPRKPEEVDDEVFYSPRSLVFPEAENRKWTIMAVMVSLLTDYSPQLQKPKF
|
| Enzyme 6 Number of Residues |
354 |
| Enzyme 6 Molecular Weight |
39936 |
| Enzyme 6 Theoretical pI |
8.96 |
| Enzyme 6 GO Classification |
| Function |
- amine binding
- amino acid binding
- binding
- carboxyl- and carbamoyltransferase activity
- catalytic activity
- ornithine carbamoyltransferase activity
- transferase activity
- transferase activity, transferring one-carbon groups
|
| Process |
- amino acid and derivative metabolism
- amino acid metabolism
- cellular metabolism
- metabolism
- physiological process
|
| Component |
- ornithine carbamoyltransferase complex
- protein complex
|
|
| Enzyme 6 General Function |
Amino acid transport and metabolism |
| Enzyme 6 Specific Function |
Carbamoyl phosphate + L-ornithine = phosphate + L-citrulline |
| Enzyme 6 Pathways |
- Arginine and Proline Metabolism (map00330
)
|
| Enzyme 6 Reactions |
- carbamoyl phosphate + L-ornithine = phosphate + L-citrulline
|
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
|
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
189407  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
P00480  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
OTC_HUMAN  |
| Enzyme 6 PDB ID |
1FVO  |
| Enzyme 6 PDB File |
Show |
| Enzyme 6 3D Structure |
|
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 Gene Sequence |
>1065 bp
ATGCTGTTTAATCTGAGGATCCTGTTAAACAATGCAGCTTTTAGAAATGGTCACAACTTC
ATGGTTCGAAATTTTCGGTGTGGACAACCACTACAAAATAAAGTGCAGCTGAAGGGCCGT
GACCTTCTCACTCTAAAAAACTTTACCGGAGAAGAAATTAAATATATGCTATGGCTATCA
GCAGATCTGAAATTTAGGATAAAACAGAAAGGAGAGTATTTGCCTTTATTGCAGGGGAAG
TCCTTAGGCATGATTTTTGAGAAAAGAAGTACTCGAACAAGATTGTCTACAGAAACAGGC
TTTGCACTTCTGGGAGGACATCCTTGTTTTCCTACCACACAAGATATTCATTTGGGTGTG
AATGAAAGTCTCACGGACACGGCCCGTGTATTGTCTAGCATGGCAGATGCAGTATTGGCT
CGAGTGTATAAACAATCAGATTTGGACACCCTTGCTAAAGAAGCATCCATCCCAATTATC
AATGGGCTGTCAGATTTGTACCATCCTATCCAGATCCTGGCTGATTACCTCACGCTCCAG
GAACACTATAGCTCTCTGAAAGGTCTTACCCTCAGCTGTTTCGGGGATGGGAACAATATC
CTGCACTCCATCATGATGAGCGCAGCGAAATTCGGAATGCACCTTCAGGCAGCTACTCCA
AAGGGTTATGAGCCGGATGCTAGTGTAACCAAGTTGGCAGAGCAGTATGCCAAAGAGAAT
GGTACCAAGCTGTTGCTGACAAATGATCCATTGGAAGCAGCGCATGGAGGCAATGTATTA
ATTACAGACACTTGGATAAGCATGGGACGAGAAGAGGAGAAGAAAAAGCGGCTCCAAGCT
TTCCAAGGTTACCAAGTTACAATGAAGACTGCTAAAGTTGCTGCCTCTGACTGGACATTT
TTACACTGCTTGCCCAGAAAGCCAGAAGAAGTGGATGATGAAGTCTTTTATTCTCCTCGA
TCACTAGTGTTCCCAGAGGCAGAAAACAGAAAGTGGACAATCATGGCTGTCATGGTGTCC
CTGCTGACAGATTACTCACCTCAGCTCCAGAAGCCTAAATTTTGA
|
| Enzyme 6 GenBank Gene ID |
K02100  |
| Enzyme 6 GeneCard ID |
OTC  |
| Enzyme 6 GenAtlas ID |
OTC  |
| Enzyme 6 HGNC ID |
HGNC:8512  |
| Enzyme 6 Chromosome Location |
X |
| Enzyme 6 Locus |
Xp21.1 |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
- Horwich AL, Fenton WA, Williams KR, Kalousek F, Kraus JP, Doolittle RF, Konigsberg W, Rosenberg LE: Structure and expression of a complementary DNA for the nuclear coded precursor of human mitochondrial ornithine transcarbamylase. Science. 1984 Jun 8;224(4653):1068-74. [PubMed
]
- Hata A, Tsuzuki T, Shimada K, Takiguchi M, Mori M, Matsuda I: Structure of the human ornithine transcarbamylase gene. J Biochem (Tokyo). 1988 Feb;103(2):302-8. [PubMed
]
- Horwich AL, Kalousek F, Rosenberg LE: Arginine in the leader peptide is required for both import and proteolytic cleavage of a mitochondrial precursor. Proc Natl Acad Sci U S A. 1985 Aug;82(15):4930-3. [PubMed
]
- Hata A, Tsuzuki T, Shimada K, Takiguchi M, Mori M, Matsuda I: Isolation and characterization of the human ornithine transcarbamylase gene: structure of the 5'-end region. J Biochem (Tokyo). 1986 Sep;100(3):717-25. [PubMed
]
- Gilbert-Dussardier B, Rabier D, Strautnieks S, Segues B, Bonnefont JP, Munnich A: A novel arginine (245) to glutamine change in exon 8 of the ornithine carbamoyl transferase gene in two unrelated children presenting with late onset deficiency and showing the same enzymatic pattern. Hum Mol Genet. 1994 May;3(5):831-2. [PubMed
]
- Shi D, Morizono H, Ha Y, Aoyagi M, Tuchman M, Allewell NM: 1.85-A resolution crystal structure of human ornithine transcarbamoylase complexed with N-phosphonacetyl-L-ornithine. Catalytic mechanism and correlation with inherited deficiency. J Biol Chem. 1998 Dec 18;273(51):34247-54. [PubMed
]
- Shi D, Morizono H, Aoyagi M, Tuchman M, Allewell NM: Crystal structure of human ornithine transcarbamylase complexed with carbamoyl phosphate and L-norvaline at 1.9 A resolution. Proteins. 2000 Jun 1;39(4):271-7. [PubMed
]
- Tuchman M: Mutations and polymorphisms in the human ornithine transcarbamylase gene. Hum Mutat. 1993;2(3):174-8. [PubMed
]
- Tuchman M, Plante RJ: Mutations and polymorphisms in the human ornithine transcarbamylase gene: mutation update addendum. Hum Mutat. 1995;5(4):293-5. [PubMed
]
- Tuchman M, Morizono H, Reish O, Yuan X, Allewell NM: The molecular basis of ornithine transcarbamylase deficiency: modelling the human enzyme and the effects of mutations. J Med Genet. 1995 Sep;32(9):680-8. [PubMed
]
- Maddalena A, Spence JE, O'Brien WE, Nussbaum RL: Characterization of point mutations in the same arginine codon in three unrelated patients with ornithine transcarbamylase deficiency. J Clin Invest. 1988 Oct;82(4):1353-8. [PubMed
]
- Grompe M, Muzny DM, Caskey CT: Scanning detection of mutations in human ornithine transcarbamoylase by chemical mismatch cleavage. Proc Natl Acad Sci U S A. 1989 Aug;86(15):5888-92. [PubMed
]
- Finkelstein JE, Francomano CA, Brusilow SW, Traystman MD: Use of denaturing gradient gel electrophoresis for detection of mutation and prospective diagnosis in late onset ornithine transcarbamylase deficiency. Genomics. 1990 Jun;7(2):167-72. [PubMed
]
- Grompe M, Caskey CT, Fenwick RG: Improved molecular diagnostics for ornithine transcarbamylase deficiency. Am J Hum Genet. 1991 Feb;48(2):212-22. [PubMed
]
- Hentzen D, Pelet A, Feldman D, Rabier D, Berthelot J, Munnich A: Fatal hyperammonemia resulting from a C-to-T mutation at a MspI site of the ornithine transcarbamylase gene. Hum Genet. 1991 Dec;88(2):153-6. [PubMed
]
- Tuchman M, Holzknecht RA, Gueron AB, Berry SA, Tsai MY: Six new mutations in the ornithine transcarbamylase gene detected by single-strand conformational polymorphism. Pediatr Res. 1992 Nov;32(5):600-4. [PubMed
]
- Tsai MY, Holzknecht RA, Tuchman M: Single-strand conformational polymorphism and direct sequencing applied to carrier testing in families with ornithine transcarbamylase deficiency. Hum Genet. 1993 May;91(4):321-5. [PubMed
]
- Tuchman M, Plante RJ, Giguere Y, Lemieux B: The ornithine transcarbamylase gene: new "private" mutations in four patients and study of a polymorphism. Hum Mutat. 1994;3(3):318-20. [PubMed
]
- Matsuura T, Hoshide R, Kiwaki K, Komaki S, Koike E, Endo F, Oyanagi K, Suzuki Y, Kato I, Ishikawa K, et al.: Four newly identified ornithine transcarbamylase (OTC) mutations (D126G, R129H, I172M and W332X) in Japanese male patients with early-onset OTC deficiency. Hum Mutat. 1994;3(4):402-6. [PubMed
]
- Tuchman M, Plante RJ, McCann MT, Qureshi AA: Seven new mutations in the human ornithine transcarbamylase gene. Hum Mutat. 1994;4(1):57-60. [PubMed
]
- Garcia-Perez MA, Paz Briones PS, Garcia-Munnoz MJ, Rubio V: A splicing mutation, a nonsense mutation (Y167X) and two missense mutations (I159T and A209V) in Spanish patients with ornithine transcarbamylase deficiency. Hum Genet. 1995 Nov;96(5):549-51. [PubMed
]
- Zimmer KP, Matsuura T, Colombo JP, Koch HG, Ullrich K, Deufel T, Harms E, Matsuda I: A novel point mutation at codon 269 of the ornithine transcarbamylase (OTC) gene causing neonatal onset of OTC deficiency. J Inherit Metab Dis. 1995;18(3):356-7. [PubMed
]
- Gilbert-Dussardier B, Segues B, Rozet JM, Rabier D, Calvas P, de Lumley L, Bonnefond JP, Munnich A: Partial duplication [dup. TCAC (178)] and novel point mutations (T125M, G188R, A209V, and H302L) of the ornithine transcarbamylase gene in congenital hyperammonemia. Hum Mutat. 1996;8(1):74-6. [PubMed
]
- Oppliger Leibundgut EO, Wermuth B, Colombo JP, Liechti-Gallati S: Ornithine transcarbamylase deficiency: characterization of gene mutations and polymorphisms. Hum Mutat. 1996;8(4):333-9. [PubMed
]
- Segues B, Veber PS, Rabier D, Calvas P, Saudubray JM, Gilbert-Dussardier B, Bonnefont JP, Munnich A: A 3-base pair in-frame deletion in exon 8 (delGlu272/273) of the ornithine transcarbamylase gene in late-onset hyperammonemic coma. Hum Mutat. 1996;8(4):373-4. [PubMed
]
- Yoo HW, Kim GH, Lee DH: Identification of new mutations in the ornithine transcarbamylase (OTC) gene in Korean families. J Inherit Metab Dis. 1996;19(1):31-42. [PubMed
]
- Matsuda I, Tanase S: The ornithine transcarbamylase (OTC) gene: mutations in 50 Japanese families with OTC deficiency. Am J Med Genet. 1997 Sep 5;71(4):378-83. [PubMed
]
- Morizono H, Tuchman M, Rajagopal BS, McCann MT, Listrom CD, Yuan X, Venugopal D, Barany G, Allewell NM: Expression, purification and kinetic characterization of wild-type human ornithine transcarbamylase and a recurrent mutant that produces 'late onset' hyperammonaemia. Biochem J. 1997 Mar 1;322 ( Pt 2):625-31. [PubMed
]
- Oppliger Leibundgut E, Liechti-Gallati S, Colombo JP, Wermuth B: Ornithine transcarbamylase deficiency: ten new mutations and high proportion of de novo mutations in heterozygous females. Hum Mutat. 1997;9(5):409-11. [PubMed
]
- Tuchman M, Morizono H, Rajagopal BS, Plante RJ, Allewell NM: Identification of 'private' mutations in patients with ornithine transcarbamylase deficiency. J Inherit Metab Dis. 1997 Aug;20(4):525-7. [PubMed
]
- Shimadzu M, Matsumoto H, Matsuura T, Kobayashi K, Komaki S, Kiwaki K, Hoshide R, Endo F, Saheki T, Matsuda I: Ten novel mutations of the ornithine transcarbamylase (OTC) gene in OTC deficiency. Hum Mutat. 1998;Suppl 1:S5-7. [PubMed
]
- Calvas P, Segues B, Rozet JM, Rabier D, Bonnefond JP, Munnich A: Novel intragenic deletions and point mutations of the ornithine transcarbamylase gene in congenital hyperammonemia. Hum Mutat. 1998;Suppl 1:S81-4. [PubMed
]
- Nishiyori A, Yoshino M, Tananari Y, Matsuura T, Hoshide R, Mastuda I, Mori M, Kato H: Y55D mutation in ornithine transcarbamylase associated with late-onset hyperammonemia in a male. Hum Mutat. 1998;Suppl 1:S131-3. [PubMed
]
- Climent C, Garcia-Perez MA, Sanjurjo P, Ruiz-Sanz JI, Vilaseca MA, Pineda M, Campistol J, Rubio V: Identification of a cytogenetic deletion and of four novel mutations (Q69X, I172F, G188V, G197R) affecting the gene for ornithine transcarbamylase (OTC) in Spanish patients with OTC deficiency. Hum Mutat. 1999 Oct;14(4):352-3. [PubMed
]
- Popowska E, Ciara E, Rokicki D, Pronicka E: Three novel and one recurrent ornithine carbamoyltransferase gene mutations in Polish patients. J Inherit Metab Dis. 1999 Feb;22(1):92-3. [PubMed
]
- Giorgi M, Morrone A, Donati MA, Ciani F, Bardelli T, Biasucci G, Zammarchi E: Lymphocyte mRNA analysis of the ornithine transcarbamylase gene in Italian OTCD male patients and manifesting carriers: identification of novel mutations. Hum Mutat. 2000 Apr;15(4):380-1. [PubMed
]
- Climent C, Rubio V: Identification of seven novel missense mutations, two splice-site mutations, two microdeletions and a polymorphic amino acid substitution in the gene for ornithine transcarbamylase (OTC) in patients with OTC deficiency. Hum Mutat. 2002 Feb;19(2):185-6. [PubMed
]
|
| Enzyme 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
6216 |
| Enzyme 7 Name |
Nitric-oxide synthase, brain |
| Enzyme 7 Synonyms |
- NOS type I
- Neuronal NOS
- N-NOS
- nNOS
- Constitutive NOS
- NC-NOS
- bNOS
|
| Enzyme 7 Gene Name |
NOS1 |
| Enzyme 7 Protein Sequence |
>Nitric-oxide synthase, brain
MEDHMFGVQQIQPNVISVRLFKRKVGGLGFLVKERVSKPPVIISDLIRGGAAEQSGLIQA
GDIILAVNGRPLVDLSYDSALEVLRGIASETHVVLILRGPEGFTTHLETTFTGDGTPKTI
RVTQPLGPPTKAVDLSHQPPAGKEQPLAVDGASGPGNGPQHAYDDGQEAGSLPHANGLAP
RPPGQDPAKKATRVSLQGRGENNELLKEIEPVLSLLTSGSRGVKGGAPAKAEMKDMGIQV
DRDLDGKSHKPLPLGVENDRVFNDLWGKGNVPVVLNNPYSEKEQPPTSGKQSPTKNGSPS
KCPRFLKVKNWETEVVLTDTLHLKSTLETGCTEYICMGSIMHPSQHARRPEDVRTKGQLF
PLAKEFIDQYYSSIKRFGSKAHMERLEEVNKEIDTTSTYQLKDTELIYGAKHAWRNASRC
VGRIQWSKLQVFDARDCTTAHGMFNYICNHVKYATNKGNLRSAITIFPQRTDGKHDFRVW
NSQLIRYAGYKQPDGSTLGDPANVQFTEICIQQGWKPPRGRFDVLPLLLQANGNDPELFQ
IPPELVLEVPIRHPKFEWFKDLGLKWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGV
RDYCDNSRYNILEEVAKKMNLDMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSAT
ESFIKHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEMLNYRLTPSFEYQPDPWNTHV
WKGTNGTPTKRRAIGFKKLAEAVKFSAKLMGQAMAKRVKATILYATETGKSQAYAKTLCE
IFKHAFDAKVMSMEEYDIVHLEHETLVLVVTSTFGNGDPPENGEKFGCALMEMRHPNSVQ
EERKSYKVRFNSVSSYSDSQKSSGDGPDLRDNFESAGPLANVRFSVFGLGSRAYPHFCAF
GHAVDTLLEELGGERILKMREGDELCGQEEAFRTWAKKVFKAACDVFCVGDDVNIEKANN
SLISNDRSWKRNKFRLTFVAEAPELTQGLSNVHKKRVSAARLLSRQNLQSPKSSRSTIFV
RLHTNGSQELQYQPGDHLGVFPGNHEDLVNALIERLEDAPPVNQMVKVELLEERNTALGV
ISNWTDELRLPPCTIFQAFKYYLDITTPPTPLQLQQFASLATSEKEKQRLLVLSKGLQEY
EEWKWGKNPTIVEVLEEFPSIQMPATLLLTQLSLLQPRYYSISSSPDMYPDEVHLTVAIV
SYRTRDGEGPIHHGVCSSWLNRIQADELVPCFVRGAPSFHLPRNPQVPCILVGPGTGIAP
FRSFWQQRQFDIQHKGMNPCPMVLVFGCRQSKIDHIYREETLQAKNKGVFRELYTAYSRE
PDKPKKYVQDILQEQLAESVYRALKEQGGHIYVCGDVTMAADVLKAIQRIMTQQGKLSAE
DAGVFISRMRDDNRYHEDIFGVTLRTYEVTNRLRSESIAFIEESKKDTDEVFSS
|
| Enzyme 7 Number of Residues |
1434 |
| Enzyme 7 Molecular Weight |
160972 |
| Enzyme 7 Theoretical pI |
7.44 |
| Enzyme 7 GO Classification |
| Function |
- FAD binding
- FMN binding
- NADP binding
- adenyl nucleotide binding
- binding
- calmodulin binding
- catalytic activity
- cation binding
- coenzyme binding
- cofactor binding
- electron transporter activity
- heme binding
- ion binding
- iron ion binding
- monooxygenase activity
- nitric-oxide synthase activity
- nucleotide binding
- oxidoreductase activity
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD or NADH as one donor, and incorporation of one atom of oxygen
- protein binding
- purine nucleotide binding
- tetrapyrrole binding
- transition metal ion binding
- transporter activity
|
| Process |
- biosynthesis
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- nitric oxide biosynthesis
- physiological process
|
| Component |
| — |
|
| Enzyme 7 General Function |
Inorganic ion transport and metabolism |
| Enzyme 7 Specific Function |
Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In the brain and peripheral nervous system, NO displays many properties of a neurotransmitter |
| Enzyme 7 Pathways |
- Arginine and Proline Metabolism (map00330
)
|
| Enzyme 7 Reactions |
- L-arginine + n NADPH + n H+ + m O2 = citrulline + nitric oxide + n NADP+
|
| Enzyme 7 Pfam Domain Function |
|
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
642526  |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
P29475  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
NOS1_HUMAN  |
| Enzyme 7 PDB ID |
Not Available |
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 Gene Sequence |
>4305 bp
ATGGAGGATCACATGTTCGGTGTTCAGCAAATCCAGCCCAATGTCATTTCTGTTCGTCTC
TTCAAGCGCAAAGTTGGGGGCCTGGGATTTCTGGTGAAGGAGCGGGTCAGTAAGCCGCCC
GTGATCATCTCTGACCTGATTCGTGGGGGCGCCGCAGAGCAGAGTGGCCTCATCCAGGCC
GGAGACATCATTCTTGCGGTCAACGGCCGGCCCTTGGTGGACCTGAGCTATGACAGCGCC
CTGGAGGTACTCAGAGGCATTGCCTCTGAGACCCACGTGGTCCTCATTCTGAGGGGCCCT
GAAGGTTTCACCACGCACCTGGAGACCACCTTTACAGGTGATGGGACCCCCAAGACCATC
CGGGTGACACAGCCCCTGGGTCCCCCCACCAAAGCCGTGGATCTGTCCCACCAGCCACCG
GCCGGCAAAGAACAGCCCCTGGCAGTGGATGGGGCCTCGGGTCCCGGGAATGGGCCTCAG
CATGCCTACGATGATGGGCAGGAGGCTGGCTCACTCCCCCATGCCAACGGCCTGGCCCCC
AGGCCCCCAGGCCAGGACCCCGCGAAGAAAGCAACCAGAGTCAGCCTCCAAGGCAGAGGG
GAGAACAATGAACTGCTCAAGGAGATAGAGCCTGTGCTGAGCCTTCTCACCAGTGGGAGC
AGAGGGGTCAAGGGAGGGGCACCTGCCAAGGCAGAGATGAAAGATATGGGAATCCAGGTG
GACAGAGATTTGGACGGCAAGTCACACAAACCTCTGCCCCTCGGCGTGGAGAACGACCGA
GTCTTCAATGACCTATGGGGGAAGGGCAATGTGCCTGTCGTCCTCAACAACCCATATTCA
GAGAAGGAGCAGCCCCCCACCTCAGGAAAACAGTCCCCCACAAAGAATGGCAGCCCCTCC
AAGTGTCCACGCTTCCTCAAGGTCAAGAACTGGGAGACTGAGGTGGTTCTCACTGACACC
CTCCACCTTAAGAGCACATTGGAAACGGGATGCACTGAGTACATCTGCATGGGCTCCATC
ATGCATCCTTCTCAGCATGCAAGGAGGCCTGAAGACGTCCGCACAAAAGGACAGCTCTTC
CCTCTCGCCAAAGAGTTTATTGATCAATACTATTCATCAATTAAAAGATTTGGCTCCAAA
GCCCACATGGAAAGGCTGGAAGAGGTGAACAAAGAGATCGACACCACTAGCACTTACCAG
CTCAAGGACACAGAGCTCATCTATGGGGCCAAGCACGCCTGGCGGAATGCCTCGCGCTGT
GTGGGCAGGATCCAGTGGTCCAAGCTGCAGGTATTCGATGCCCGTGACTGCACCACGGCC
CACGGGATGTTCAACTACATCTGTAACCATGTCAAGTATGCCACCAACAAAGGGAACCTC
AGGTCTGCCATCACCATATTCCCCCAGAGGACAGACGGCAAGCACGACTTCCGAGTCTGG
AACTCCCAGCTCATCCGCTACGCTGGCTACAAGCAGCCTGACGGCTCCACCCTGGGGGAC
CCAGCCAATGTGCAGTTCACAGAGATATGCATACAGCAGGGCTGGAAACCGCCTAGAGGC
CGCTTCGATGTCCTGCCGCTCCTGCTTCAGGCCAACGGCAATGACCCTGAGCTCTTCCAG
ATTCCTCCAGAGCTGGTGTTGGAAGTTCCCATCAGGCACCCCAAGTTTGAGTGGTTCAAG
GACCTGGGGCTGAAGTGGTACGGCCTCCCCGCCGTGTCCAACATGCTCCTAGAGATTGGC
GGCCTGGAGTTCAGCGCCTGTCCCTTCAGTGGCTGGTACATGGGCACAGAGATTGGTGTC
CGCGACTACTGTGACAACTCCCGCTACAATATCCTGGAGGAAGTGGCCAAGAAGATGAAC
TTAGACATGAGGAAGACGTCCTCCCTGTGGAAGGACCAGGCGCTGGTGGAGATCAATATC
GCGGTTCTCTATAGCTTCCAGAGTGACAAAGTGACCATTGTTGACCATCACTCCGCCACC
GAGTCCTTCATTAAGCACATGGAGAATGAGTACCGCTGCCGGGGGGGCTGCCCTGCCGAC
TGGGTGTGGATCGTGCCCCCCATGTCCGGAAGCATCACCCCTGTGTTCCACCAGGAGATG
CTCAACTACCGGCTCACCCCCTCCTTCGAATACCAGCCTGATCCCTGGAACACGCATGTC
TGGAAAGGCACCAACGGGACCCCCACAAAGCGGCGAGCCATCGGCTTCAAGAAGCTAGCA
GAAGCTGTCAAGTTCTCGGCCAAGCTGATGGGGCAGGCTATGGCCAAGAGGGTGAAAGCG
ACCATCCTCTATGCCACAGAGACAGGCAAATCGCAAGCTTATGCCAAGACCTTGTGTGAG
ATCTTCAAACACGCCTTTGATGCCAAGGTGATGTCCATGGAAGAATATGACATTGTGCAC
CTGGAACATGAAACTCTGGTCCTTGTGGTCACCAGCACCTTTGGCAATGGAGATCCCCCT
GAGAATGGGGAGAAATTCGGCTGTGCTTTGATGGAAATGAGGCACCCCAACTCTGTGCAG
GAAGAAAGGAAGAGCTACAAGGTCCGATTCAACAGCGTCTCCTCCTACTCTGACTCCCAA
AAATCATCAGGCGATGGGCCCGACCTCAGAGACAACTTTGAGAGTGCTGGACCCCTGGCC
AATGTGAGGTTCTCAGTTTTTGGCCTCGGCTCACGAGCATACCCTCACTTTTGCGCCTTC
GGACACGCTGTGGACACCCTCCTGGAAGAACTGGGAGGGGAGAGGATCCTGAAGATGAGG
GAAGGGGATGAGCTCTGTGGGCAGGAAGAGGCTTTCAGGACCTGGGCCAAGAAGGTCTTC
AAGGCAGCCTGTGATGTCTTCTGTGTGGGAGATGATGTCAACATTGAAAAGGCCAACAAT
TCCCTCATCAGCAATGATCGCAGCTGGAAGAGAAACAAGTTCCGCCTCACCTTTGTGGCC
GAAGCTCCAGAACTCACACAAGGTCTATCCAATGTCCACAAAAAGCGAGTCTCAGCTGCC
CGGCTCCTTAGCCGTCAAAACCTCCAGAGCCCTAAATCCAGTCGGTCAACTATCTTCGTG
CGTCTCCACACCAACGGGAGCCAGGAGCTGCAGTACCAGCCTGGGGACCACCTGGGTGTC
TTCCCTGGCAACCACGAGGACCTCGTGAATGCCCTGATCGAGCGGCTGGAGGACGCGCCG
CCTGTCAACCAGATGGTGAAAGTGGAACTGCTGGAGGAGCGGAACACGGCTTTAGGTGTC
ATCAGTAACTGGACAGACGAGCTCCGCCTCCCGCCCTGCACCATCTTCCAGGCCTTCAAG
TACTACCTGGACATCACCACGCCACCAACGCCTCTGCAGCTGCAGCAGTTTGCCTCCCTA
GCTACCAGCGAGAAGGAGAAGCAGCGTCTGCTGGTCCTCAGCAAGGGTTTGCAGGAGTAC
GAGGAATGGAAATGGGGCAAGAACCCCACCATCGTGGAGGTGCTGGAGGAGTTCCCATCT
ATCCAGATGCCGGCCACCCTGCTCCTGACCCAGCTGTCCCTGCTGCAGCCCCGCTACTAT
TCCATCAGCTCCTCCCCAGACATGTACCCTGATGAAGTGCACCTCACTGTGGCCATCGTT
TCCTACCGCACTCGAGATGGAGAAGGACCAATTCACCACGGCGTATGCTCCTCCTGGCTC
AACCGGATACAGGCTGACGAACTGGTCCCCTGTTTCGTGAGAGGAGCACCCAGCTTCCAC
CTGCCCCGGAACCCCCAAGTCCCCTGCATCCTCGTTGGACCAGGCACCGGCATTGCCCCT
TTCCGAAGCTTCTGGCAACAGCGGCAATTTGATATCCAACACAAAGGAATGAACCCCTGC
CCCATGGTCCTGGTCTTCGGGTGCCGGCAATCCAAGATAGATCATATCTACAGGGAAGAG
ACCCTGCAGGCCAAGAACAAGGGGGTCTTCAGAGAGCTGTACACGGCTTACTCCCGGGAG
CCAGACAAACCAAAGAAGTACGTGCAGGACATCCTGCAGGAGCAGCTGGCGGAGTCTGTG
TACCGAGCCCTGAAGGAGCAAGGGGGCCACATATACGTCTGTGGGGACGTCACCATGGCT
GCTGATGTCCTCAAAGCCATCCAGCGCATCATGACCCAGCAGGGGAAGCTCTCGGCAGAG
GACGCCGGCGTATTCATCAGCCGGATGAGGGATGACAACCGATACCATGAGGATATTTTT
GGAGTCACCCTGCGAACGTACGAAGTGACCAACCGCCTTAGATCTGAGTCCATTGCCTTC
ATTGAAGAGAGCAAAAAAGACACCGATGAGGTTTTCAGCTCCTAA
|
| Enzyme 7 GenBank Gene ID |
U17327  |
| Enzyme 7 GeneCard ID |
NOS1  |
| Enzyme 7 GenAtlas ID |
NOS1  |
| Enzyme 7 HGNC ID |
HGNC:7872  |
| Enzyme 7 Chromosome Location |
12 |
| Enzyme 7 Locus |
12q24.2-q24.31 |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 General References |
- Hall AV, Antoniou H, Wang Y, Cheung AH, Arbus AM, Olson SL, Lu WC, Kau CL, Marsden PA: Structural organization of the human neuronal nitric oxide synthase gene (NOS1). J Biol Chem. 1994 Dec 30;269(52):33082-90. [PubMed
]
- Fujisawa H, Ogura T, Kurashima Y, Yokoyama T, Yamashita J, Esumi H: Expression of two types of nitric oxide synthase mRNA in human neuroblastoma cell lines. J Neurochem. 1994 Jul;63(1):140-5. [PubMed
]
- Nakane M, Schmidt HH, Pollock JS, Forstermann U, Murad F: Cloned human brain nitric oxide synthase is highly expressed in skeletal muscle. FEBS Lett. 1993 Jan 25;316(2):175-80. [PubMed
]
- Park CS, Gianotti C, Park R, Krishna G: Neuronal isoform of nitric oxide synthase is expressed at low levels in human retina. Cell Mol Neurobiol. 1996 Aug;16(4):499-515. [PubMed
]
- Wang Y, Goligorsky MS, Lin M, Wilcox JN, Marsden PA: A novel, testis-specific mRNA transcript encoding an NH2-terminal truncated nitric-oxide synthase. J Biol Chem. 1997 Apr 25;272(17):11392-401. [PubMed
]
|
| Enzyme 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
6217 |
| Enzyme 8 Name |
Nitric-oxide synthase, endothelial |
| Enzyme 8 Synonyms |
- EC-NOS
- NOS type III
- NOSIII
- Endothelial NOS
- eNOS
- Constitutive NOS
- cNOS
|
| Enzyme 8 Gene Name |
NOS3 |
| Enzyme 8 Protein Sequence |
>Nitric-oxide synthase, endothelial
MGNLKSVAQEPGPPCGLGLGLGLGLCGKQGPATPAPEPSRAPASLLPPAPEHSPPSSPLT
QPPEGPKFPRVKNWEVGSITYDTLSAQAQQDGPCTPRRCLGSLVFPRKLQGRPSPGPPAP
EQLLSQARDFINQYYSSIKRSGSQAHEQRLQEVEAEVAATGTYQLRESELVFGAKQAWRN
APRCVGRIQWGKLQVFDARDCRSAQEMFTYICNHIKYATNRGNLRSAITVFPQRCPGRGD
FRIWNSQLVRYAGYRQQDGSVRGDPANVEITELCIQHGWTPGNGRFDVLPLLLQAPDEPP
ELFLLPPELVLEVPLEHPTLEWFAALGLRWYALPAVSNMLLEIGGLEFPAAPFSGWYMST
EIGTRNLCDPHRYNILEDVAVCMDLDTRTTSSLWKDKAAVEINVAVLHSYQLAKVTIVDH
HAATASFMKHLENEQKARGGCPADWAWIVPPISGSLTPVFHQEMVNYFLSPAFRYQPDPW
KGSAAKGTGITRKKTFKEVANAVKISASLMGTVMAKRVKATILYGSETGRAQSYAQQLGR
LFRKAFDPRVLCMDEYDVVSLEHETLVLVVTSTFGNGDPPENGESFAAALMEMSGPYNSS
PRPEQHKSYKIRFNSISCSDPLVSSWRRKRKESSNTDSAGALGTLRFCVFGLGSRAYPHF
CAFARAVDTRLEELGGERLLQLGQGDELCGQEEAFRGWAQAAFQAACETFCVGEDAKAAA
RDIFSPKRSWKRQRYRLSAQAEGLQLLPGLIHVHRRKMFQATIRSVENLQSSKSTRATIL
VRLDTGGQEGLQYQPGDHIGVCPPNRPGLVEALLSRVEDPPAPTEPVAVEQLEKGSPGGP
PPGWVRDPRLPPCTLRQALTFFLDITSPPSPQLLRLLSTLAEEPREQQELEALSQDPRRY
EEWKWFRCPTLLEVLEQFPSVALPAPLLLTQLPLLQPRYYSVSSAPSTHPGEIHLTVAVL
AYRTQDGLGPLHYGVCSTWLSQLKPGDPVPCFIRGAPSFRLPPDPSLPCILVGPGTGIAP
FRGFWQERLHDIESKGLQPTPMTLVFGCRCSQLDHLYRDEVQNAQQRGVFGRVLTAFSRE
PDNPKTYVQDILRTELAAEVHRVLCLERGHMFVCGDVTMATNVLQTVQRILATEGDMELD
EAGDVIGVLRDQQRYHEDIFGLTLRTQEVTSRIRTQSFSLQERQLRGAVPWAFDPPGSDT
NSP
|
| Enzyme 8 Number of Residues |
1203 |
| Enzyme 8 Molecular Weight |
133290 |
| Enzyme 8 Theoretical pI |
7.27 |
| Enzyme 8 GO Classification |
| Function |
- FMN binding
- binding
- catalytic activity
- monooxygenase activity
- nitric-oxide synthase activity
- nucleotide binding
- oxidoreductase activity
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD or NADH as one donor, and incorporation of one atom of oxygen
|
| Process |
- biosynthesis
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- nitric oxide biosynthesis
- physiological process
|
| Component |
| — |
|
| Enzyme 8 General Function |
Inorganic ion transport and metabolism |
| Enzyme 8 Specific Function |
Produces nitric oxide (NO) which is implicated in vascular smooth muscle relaxation through a cGMP-mediated signal transduction pathway. No mediates vascular endothelial growth factor (VEGF)-induced angiogenesis in coronary vessels and promotes blood clotting through the activation of platelets |
| Enzyme 8 Pathways |
- Arginine and Proline Metabolism (map00330
)
|
| Enzyme 8 Reactions |
- L-arginine + n NADPH + n H+ + m O2 = citrulline + nitric oxide + n NADP+
|
| Enzyme 8 Pfam Domain Function |
|
| Enzyme 8 Signals |
|
| Enzyme 8 Transmembrane Regions |
|
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
189212  |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
P29474  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
NOS3_HUMAN  |
| Enzyme 8 PDB ID |
Not Available |
| Enzyme 8 Cellular Location |
Not Available |
| Enzyme 8 Gene Sequence |
>3612 bp
ATGGGCAACTTGAAGAGCGTGGCCCAGGAGCCTGGGCCACCCTGCGGCCTGGGGCTGGGG
CTGGGCCTTGGGCTGTGCGGCAAGCAGGGCCCAGCCACCCCGGCCCCTGAGCCCAGCCGG
GCCCCAGCATCCCTACTCCCACCAGCGCCAGAACACAGCCCCCCGAGCTCCCCGCTAACC
CAGCCCCCAGAGGGGCCCAAGTTCCCTCGTGTGAAGAACTGGGAGGTGGGGAGCATCACC
TATGACACCCTCAGCGCCCAGGCGCAGCAGGATGGGCCCTGCACCCCAAGACGCTGCCTG
GGCTCCCTGGTATTTCCACGGAAACTACAGGGCCGGCCCTCCCCCGGCCCCCCGGCCCCT
GAGCAGCTGCTGAGTCAGGCCCGGGACTTCATCAACCAGTACTACAGCTCCATTAAGAGG
AGCGGCTCCCAGGCCCACGAACAGCGGCTTCAAGAGGTGGAAGCCGAGGTGGCAGCCACA
GGCACCTACCAGCTTAGGGAGAGCGAGCTGGTGTTCGGGGCTAAGCAGGCCTGGCGCAAC
GCTCCCCGCTGCGTGGGCCGGATCCAGTGGGGGAAGCTGCAGGTGTTCGATGCCCGGGAC
TGCAGGTCTGCACAGGAAATGTTCACCTACATCTGCAACCACATCAAGTATGCCACCAAC
CGGGGCAACCTTCGCTCGGCCATCACAGTGTTCCCGCAGCGCTGCCCTGGCCGAGGAGAC
TTCCGAATCTGGAACAGCCAGCTGGTGCGCTACGCGGGCTACCGGCAGCAGGACGGCTCT
GTGCGGGGGGACCCAGCCAACGTGGAGATCACCGAGCTCTGCATTCAGCACGGCTGGACC
CCAGGAAACGGTCGCTTCGACGTGCTGCCCCTGCTGCTGCAGGCCCCAGATGAGCCCCCA
GAACTCTTCCTTCTGCCCCCCGAGCTGGTCCTTGAGGTGCCCCTGGAGCACCCCACGCTG
GAGTGGTTTGCAGCCCTGGGCCTGCGCTGGTACGCCCTCCCGGCAGTGTCCAACATGCTG
CTGGAAATTGGGGGCCTGGAGTTCCCCGCAGCCCCCTTCAGTGGCTGGTACATGAGCACT
GAGATCGGCACGAGGAACCTGTGTGACCCTCACCGCTACAACATCCTGGAGGATGTGGCT
GTCTGCATGGACCTGGATACCCGGACCACCTCGTCCCTGTGGAAAGACAAGGCAGCAGTG
GAAATCAACGTGGCCGTGCTGCACAGTTACCAGCTAGCCAAAGTCACCATCGTGGACCAC
CACGCCGCCACGGCCTCTTTCATGAAGCACCTGGAGAATGAGCAGAAGGCCAGGGGGGGC
TGCCCTGCAGACTGGGCCTGGATCGTGCCCCCCATCTCGGGCAGCCTCACTCCTGTTTTC
CATCAGGAGATGGTCAACTATTTCCTGTCCCCGGCCTTCCGCTACCAGCCAGACCCCTGG
AAGGGGAGTGCCGCCAAGGGCACCGGCATCACCAGGAAGAAGACCTTTAAAGAAGTGGCC
AACGCCGTGAAGATCTCCGCCTCGCTCATGGGCACGGTGATGGCGAAGCGAGTGAAGGCG
ACAATCCTGTATGGCTCCGAGACCGGCCGGGCCCAGAGCTACGCACAGCAGCTGGGGAGA
CTCTTCCGGAAGGCTTTTGATCCCCGGGTCCTGTGTATGGATGAGTATGACGTGGTGTCC
CTCGAACACGAGACGCTGGTGCTGGTGGTAACCAGCACATTTGGGAATGGGGATCCCCCG
GAGAATGGAGAGAGCTTTGCAGCTGCCCTGATGGAGATGTCCGGCCCCTACAACAGCTCC
CCTCGGCCGGAACAGCACAAGAGTTATAAGATCCGCTTCAACAGCATCTCCTGCTCAGAC
CCACTGGTGTCCTCTTGGCGGCGGAAGAGGAAGGAGTCCAGTAACACAGACAGTGCAGGG
GCCCTGGGCACCCTCAGGTTCTGTGTGTTCGGGCTCGGCTCCCGGGCATACCCCCACTTC
TGCGCCTTTGCTCGTGCCGTGGACACACGGCTGGAGGAACTGGGCGGGGAGCGGCTGCTG
CAGCTGGGCCAGGGCGACGAGCTGTGCGGCCAGGAGGAGGCCTTCCGAGGCTGGGCCCAG
GCTGCCTTCCAGGCCGCCTGTGAGACCTTCTGTGTGGGAGAGGATGCCAAGGCCGCCGCC
CGAGACATCTTCAGCCCCAAACGGAGCTGGAAGCGCCAGAGGTACCGGCTGAGCGCCCAG
GCCGAGGGCCTGCAGTTGCTGCCAGGTCTGATCCACGTGCACAGGCGGAAGATGTTCCAG
GCTACAATCCGCTCAGTGGAAAACCTGCAAAGCAGCAAGTCCACGAGGGCCACCATCCTG
GTGCGCCTGGACACCGGAGGCCAGGAGGGGCTGCAGTACCAGCCGGGGGACCACATAGGT
GTCTGCCCGCCCAACCGGCCCGGCCTTGTGGAGGCGCTGCTGAGCCGCGTGGAGGACCCG
CCGGCGCCCACTGAGCCCGTGGCAGTAGAGCAGCTGGAGAAGGGCAGCCCTGGTGGCCCT
CCCCCCGGCTGGGTGCGGGACCCCCGGCTGCCCCCGTGCACGCTGCGCCAGGCTCTCACC
TTCTTCCTGGACATCACCTCCCCACCCAGCCCTCAGCTCTTGCGGCTGCTCAGCACCTTG
GCAGAAGAGCCCAGGGAACAGCAGGAGCTGGAGGCCCTCAGCCAGGATCCCCGACGCTAC
GAGGAGTGGAAGTGGTTCCGCTGCCCCACGCTGCTGGAGGTGCTGGAGCAGTTCCCGTCG
GTGGCGCTGCCTGCCCCACTGCTCCTCACCCAGCTGCCTCTGCTCCAGCCCCGGTACTAC
TCAGTCAGCTCGGCACCCAGCACCCACCCAGGAGAGATCCACCTCACTGTAGCTGTGCTG
GCATACAGGACTCAGGATGGGCTGGGCCCCCTGCACTATGGAGTCTGCTCCACGTGGCTA
AGCCAGCTCAAGCCCGGAGACCCTGTGCCCTGCTTCATCCGGGGGGCTCCCTCCTTCCGG
CTGCCACCCGATCCCAGCTTGCCCTGCATCCTGGTGGGTCCAGGCACTGGCATTGCCCCC
TTCCGGGGATTCTGGCAGGAGCGGCTGCATGACATTGAGAGCAAAGGGCTGCAGCCCACT
CCCATGACTTTGGTGTTCGGCTGCCGATGCTCCCAACTTGACCATCTCTACCGCGACGAG
GTGCAGAACGCCCAGCAGCGCGGGGTGTTTGGCCGAGTCCTCACCGCCTTCTCCCGGGAA
CCTGACAACCCCAAGACCTACGTGCAGGACATCCTGAGGACGGAGCTGGCTGCGGAGGTG
CACCGCGTGCTGTGCCTCGAGCGGGGCCACATGTTTGTCTGCGGCGATGTTACCATGGCA
ACCAACGTCCTGCAGACCGTGCAGCGCATCCTGGCGACGGAGGGCGACATGGAGCTGGAC
GAGGCCGGCGACGTCATCGGCGTGCTGCGGGATCAGCAACGCTACCACGAAGACATTTTC
GGGCTCACGCTGCGCACCCAGGAGGTGACAAGCCGCATACGCACCCAGAGCTTTTCCTTG
CAGGAGCGTCAGTTGCGGGGCGCAGTGCCCTGGGCGTTCGACCCTCCCGGCTCAGACACC
AACAGCCCCTGA
|
| Enzyme 8 GenBank Gene ID |
M93718  |
| Enzyme 8 GeneCard ID |
NOS3  |
| Enzyme 8 GenAtlas ID |
NOS3  |
| Enzyme 8 HGNC ID |
HGNC:7876  |
| Enzyme 8 Chromosome Location |
7 |
| Enzyme 8 Locus |
7q36 |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 General References |
- Janssens SP, Shimouchi A, Quertermous T, Bloch DB, Bloch KD: Cloning and expression of a cDNA encoding human endothelium-derived relaxing factor/nitric oxide synthase. J Biol Chem. 1992 Jul 25;267(21):14519-22. [PubMed
]
- Marsden PA, Schappert KT, Chen HS, Flowers M, Sundell CL, Wilcox JN, Lamas S, Michel T: Molecular cloning and characterization of human endothelial nitric oxide synthase. FEBS Lett. 1992 Aug 3;307(3):287-93. [PubMed
]
- Marsden PA, Heng HH, Scherer SW, Stewart RJ, Hall AV, Shi XM, Tsui LC, Schappert KT: Structure and chromosomal localization of the human constitutive endothelial nitric oxide synthase gene. J Biol Chem. 1993 Aug 15;268(23):17478-88. [PubMed
]
- Nadaud S, Bonnardeaux A, Lathrop M, Soubrier F: Gene structure, polymorphism and mapping of the human endothelial nitric oxide synthase gene. Biochem Biophys Res Commun. 1994 Feb 15;198(3):1027-33. [PubMed
]
- Miyahara K, Kawamoto T, Sase K, Yui Y, Toda K, Yang LX, Hattori R, Aoyama T, Yamamoto Y, Doi Y, et al.: Cloning and structural characterization of the human endothelial nitric-oxide-synthase gene. Eur J Biochem. 1994 Aug 1;223(3):719-26. [PubMed
]
- Robinson LJ, Weremowicz S, Morton CC, Michel T: Isolation and chromosomal localization of the human endothelial nitric oxide synthase (NOS3) gene. Genomics. 1994 Jan 15;19(2):350-7. [PubMed
]
- Sase K, Michel T: Expression of constitutive endothelial nitric oxide synthase in human blood platelets. Life Sci. 1995;57(22):2049-55. [PubMed
]
- Fischmann TO, Hruza A, Niu XD, Fossetta JD, Lunn CA, Dolphin E, Prongay AJ, Reichert P, Lundell DJ, Narula SK, Weber PC: Structural characterization of nitric oxide synthase isoforms reveals striking active-site conservation. Nat Struct Biol. 1999 Mar;6(3):233-42. [PubMed
]
- Rosenfeld RJ, Garcin ED, Panda K, Andersson G, Aberg A, Wallace AV, Morris GM, Olson AJ, Stuehr DJ, Tainer JA, Getzoff ED: Conformational changes in nitric oxide synthases induced by chlorzoxazone and nitroindazoles: crystallographic and computational analyses of inhibitor potency. Biochemistry. 2002 Nov 26;41(47):13915-25. [PubMed
]
- Yoshimura M, Yasue H, Nakayama M, Shimasaki Y, Sumida H, Sugiyama S, Kugiyama K, Ogawa H, Ogawa Y, Saito Y, Miyamoto Y, Nakao K: A missense Glu298Asp variant in the endothelial nitric oxide synthase gene is associated with coronary spasm in the Japanese. Hum Genet. 1998 Jul;103(1):65-9. [PubMed
]
|
| Enzyme 8 Metabolite References |
Not Available |
|
Enzyme 9
[top]
|
| Enzyme 9 ID |
15242 |
| Enzyme 9 Name |
Nitric oxide synthase 2A (Inducible, hepatocytes) |
| Enzyme 9 Synonyms |
Not Available |
| Enzyme 9 Gene Name |
NOS2A |
| Enzyme 9 Protein Sequence |
>Nitric oxide synthase 2A (Inducible, hepatocytes)
MACPWKFLFKTKFHQYAMNGEKDINNNVEKAPCATSSPVTQDDLQYHNLSKQQNESPQPL
VETGKKSPESLVKLDATPLSSPRHVRIKNWGSGMTFQDTLHHKAKGILTCRSKSCLGSIM
TPKSLTRGPRDKPTPPDELLPQAIEFVNQYYGSFKEAKIEEHLARVEAVTKEIETTGTYQ
LTGDELIFATKQAWRNAPRCIGRIQWSNLQVFDARSCSTAREMFEHICRHVRYSTNNGNI
RSAITVFPQRSDGKHDFRVWNAQLIRYAGYQMPDGSIRGDPANVEFTQLCIDLGWKPKYG
RFDVVPLVLQANGRDPELFEIPPDLVLEVAMEHPKYEWFRELELKWYALPAVANMLLEVG
GLEFPGCPFNGWYMGTEIGVRDFCDVQRYNILEEVGRRMGLETHKLASLWKDQAVVEINI
AVLHSFQKQNVTIMDHHSAAESFMKYMQNEYRSRGGCPADWIWLVPPMSGSITPVFHQEM
LNYVLSPFYYYQVEAWKTHVWQDEKRRPKRREIPLKVLVKAVLFACMLMRKTMASRVRVT
ILFATETGKSEALAWDLGALFSCAFNPKVVCMDKYRLSCLEEERLLLVVTSTFGNGDCPG
NGEKLKKSLFMLKELNNKFRYAVFGLGSSMYPRFCAFAHDIDQKLSHLGASQLTPMGEGD
ELSGQEDAFRSWAVQTFKAACETFDVRGKQHIQIPKLYTSNVTWDPHHYRLVQDSQPLDL
SKALSSMHAKNVFTMRLKSRQNLQSPTSSRATILVELSCEDGQGLNYLPGEHLGVCPGNQ
PALVQGILERVVDGPTPHQTVRLEALDESGSYWVSDKRLPPCSLSQALTYFLDITTPPTQ
LLLQKLAQVATEEPERQRLEALCQPSEYSKWKFTNSPTFLEVLEEFPSLRVSAGFLLSQL
PILKPRFYSISSSRDHTPTEIHLTVAVVTYHTRDGQGPLHHGVCSTWLNSLKPQDPVPCF
VRNASGFHLPEDPSHPCILIGPGTGIAPFRSFWQQRLHDSQHKGVRGGRMTLVFGCRRPD
EDHIYQEEMLEMAQKGVLHAVHTAYSRLPGKPKVYVQDILRQQLASEVLRVLHKEPGHLY
VCGDVRMARDVAHTLKQLVAAKLKLNEEQVEDYFFQLKSQKRYHEDIFGAVFPYEAKKDR
VAVQPSSLEMSAL
|
| Enzyme 9 Number of Residues |
1153 |
| Enzyme 9 Molecular Weight |
131119 |
| Enzyme 9 Theoretical pI |
8.01 |
| Enzyme 9 GO Classification |
| Function |
- FAD binding
- FMN binding
- NADP binding
- adenyl nucleotide binding
- binding
- calmodulin binding
- catalytic activity
- cation binding
- coenzyme binding
- cofactor binding
- electron transporter activity
- heme binding
- ion binding
- iron ion binding
- monooxygenase activity
- nitric-oxide synthase activity
- nucleotide binding
- oxidoreductase activity
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD or NADH as one donor, and incorporation of one atom of oxygen
- protein binding
- purine nucleotide binding
- tetrapyrrole binding
- transition metal ion binding
- transporter activity
|
| Process |
- biosynthesis
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- nitric oxide biosynthesis
- physiological process
|
| Component |
| — |
|
| Enzyme 9 General Function |
Inorganic ion transport and metabolism |
| Enzyme 9 Specific Function |
Not Available |
| Enzyme 9 Pathways |
Not Available |
| Enzyme 9 Reactions |
Not Available |
| Enzyme 9 Pfam Domain Function |
|
| Enzyme 9 Signals |
|
| Enzyme 9 Transmembrane Regions |
|
| Enzyme 9 Essentiality |
Not Available |
| Enzyme 9 GenBank ID Protein |
120660146  |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
A1L3U5  |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
A1L3U5_HUMAN  |
| Enzyme 9 PDB ID |
2NSI  |
| Enzyme 9 PDB File |
Show |
| Enzyme 9 3D Structure |
|
| Enzyme 9 Cellular Location |
Not Available |
| Enzyme 9 Gene Sequence |
>3462 bp
ATGGCCTGTCCTTGGAAATTTCTGTTCAAGACCAAATTCCACCAGTATGCAATGAATGGG
GAAAAAGACATCAACAACAATGTGGAGAAAGCCCCCTGTGCCACCTCCAGTCCAGTGACA
CAGGATGACCTTCAGTATCACAACCTCAGCAAGCAGCAGAATGAGTCCCCGCAGCCCCTC
GTGGAGACGGGAAAGAAGTCTCCAGAATCTCTGGTCAAGCTGGATGCAACCCCATTGTCC
TCCCCACGGCATGTGAGGATCAAAAACTGGGGCAGCGGGATGACTTTCCAAGACACACTT
CACCATAAGGCCAAAGGGATTTTAACTTGCAGGTCCAAATCTTGCCTGGGGTCCATTATG
ACTCCCAAAAGTTTGACCAGAGGACCCAGGGACAAGCCTACCCCTCCAGATGAGCTTCTA
CCTCAAGCTATCGAATTTGTCAACCAATATTACGGCTCCTTCAAAGAGGCAAAAATAGAG
GAACATCTGGCCAGGGTGGAAGCGGTAACAAAGGAGATAGAAACAACAGGAACCTACCAA
CTGACGGGAGATGAGCTCATCTTCGCCACCAAGCAGGCCTGGCGCAATGCCCCACGCTGC
ATTGGGAGGATCCAGTGGTCCAACCTGCAGGTCTTCGATGCCCGCAGCTGTTCCACTGCC
CGGGAAATGTTTGAACACATCTGCAGACACGTGCGTTACTCCACCAACAATGGCAACATC
AGGTCGGCCATCACCGTGTTCCCCCAGCGGAGTGATGGCAAGCACGACTTCCGGGTGTGG
AATGCTCAGCTCATCCGCTATGCTGGCTACCAGATGCCAGATGGCAGCATCAGAGGGGAC
CCTGCCAACGTGGAATTCACTCAGCTGTGCATCGACCTGGGCTGGAAGCCCAAGTACGGC
CGCTTCGATGTGGTCCCCCTGGTCCTGCAGGCCAATGGCCGTGACCCTGAGCTCTTCGAA
ATCCCACCTGACCTTGTGCTTGAGGTGGCCATGGAACATCCCAAATACGAGTGGTTTCGG
GAACTGGAGCTAAAGTGGTACGCCCTGCCTGCAGTGGCCAACATGCTGCTTGAGGTGGGC
GGCCTGGAGTTCCCAGGGTGCCCCTTCAATGGCTGGTACATGGGCACAGAGATCGGAGTC
CGGGACTTCTGTGACGTCCAGCGCTACAACATCCTGGAGGAAGTGGGCAGGAGAATGGGC
CTGGAAACGCACAAGCTGGCCTCGCTCTGGAAAGACCAGGCTGTCGTTGAGATCAACATT
GCTGTGCTCCATAGTTTCCAGAAGCAGAATGTGACCATCATGGACCACCACTCGGCTGCA
GAATCCTTCATGAAGTACATGCAGAATGAATACCGGTCCCGTGGGGGCTGCCCGGCAGAC
TGGATTTGGCTGGTCCCTCCCATGTCTGGGAGCATCACCCCCGTGTTTCACCAGGAGATG
CTGAACTACGTCCTGTCCCCTTTCTACTACTATCAGGTAGAGGCCTGGAAAACCCATGTC
TGGCAGGACGAGAAGCGGAGACCCAAGAGAAGAGAGATTCCATTGAAAGTCTTGGTCAAA
GCTGTGCTCTTTGCCTGTATGCTGATGCGCAAGACAATGGCGTCCCGAGTCAGAGTCACC
ATCCTCTTTGCGACAGAGACAGGAAAATCAGAGGCGCTGGCCTGGGACCTGGGGGCCTTA
TTCAGCTGTGCCTTCAACCCCAAGGTTGTCTGCATGGATAAGTACAGGCTGAGCTGCCTG
GAGGAGGAACGGCTGCTGTTGGTGGTGACCAGTACGTTTGGCAATGGAGACTGCCCTGGC
AATGGAGAGAAACTGAAGAAATCGCTCTTCATGCTGAAAGAGCTCAACAACAAATTCAGG
TACGCTGTGTTTGGCCTCGGCTCCAGCATGTACCCTCGGTTCTGCGCCTTTGCTCATGAC
ATTGATCAGAAGCTGTCCCACCTGGGGGCCTCTCAGCTCACCCCGATGGGAGAAGGGGAT
GAGCTCAGTGGGCAGGAGGACGCCTTCCGCAGCTGGGCCGTGCAAACCTTCAAGGCAGCC
TGTGAGACGTTTGATGTCCGAGGCAAACAGCACATTCAGATCCCCAAGCTCTACACCTCC
AATGTGACCTGGGACCCGCACCACTACAGGCTCGTGCAGGACTCACAGCCTTTGGACCTC
AGCAAAGCCCTCAGCAGCATGCATGCCAAGAACGTGTTCACCATGAGGCTCAAATCTCGG
CAGAATCTACAAAGTCCGACATCCAGCCGTGCCACCATCCTGGTGGAACTCTCCTGTGAG
GATGGCCAAGGCCTGAACTACCTGCCGGGGGAGCACCTTGGGGTTTGCCCAGGCAACCAG
CCGGCCCTGGTCCAAGGCATCCTGGAGCGAGTGGTGGATGGCCCCACACCCCACCAGACA
GTGCGCCTGGAGGCCCTGGATGAGAGTGGCAGCTACTGGGTCAGTGACAAGAGGCTGCCC
CCCTGCTCACTCAGCCAGGCCCTCACCTACTTCCTGGACATCACCACACCCCCAACCCAG
CTGCTGCTCCAAAAGCTGGCCCAGGTGGCCACAGAAGAGCCTGAGAGACAGAGGCTGGAG
GCCCTGTGCCAGCCCTCAGAGTACAGCAAGTGGAAGTTCACCAACAGCCCCACATTCCTG
GAGGTGCTAGAGGAGTTCCCGTCCCTGCGGGTGTCTGCTGGCTTCCTGCTTTCCCAGCTC
CCCATTCTGAAGCCCAGGTTCTACTCCATCAGCTCCTCCCGGGATCACACGCCCACGGAG
ATCCACCTGACTGTGGCCGTGGTCACCTACCACACCCGAGATGGCCAGGGTCCCCTGCAC
CACGGCGTCTGCAGCACATGGCTCAACAGCCTGAAGCCCCAAGACCCAGTGCCCTGCTTT
GTGCGGAATGCCAGCGGCTTCCACCTCCCCGAGGATCCCTCCCATCCTTGCATCCTCATC
GGGCCTGGCACAGGCATCGCGCCCTTCCGCAGTTTCTGGCAGCAACGGCTCCATGACTCC
CAGCACAAGGGAGTGCGGGGAGGCCGCATGACCTTGGTGTTTGGGTGCCGCCGCCCAGAT
GAGGACCACATCTACCAGGAGGAGATGCTGGAGATGGCCCAGAAGGGGGTGCTGCATGCG
GTGCACACAGCCTATTCCCGCCTGCCTGGCAAGCCCAAGGTCTATGTTCAGGACATCCTG
CGGCAGCAGCTGGCCAGCGAGGTGCTCCGTGTGCTCCACAAGGAGCCAGGCCACCTCTAT
GTTTGCGGGGATGTGCGCATGGCCCGGGACGTGGCCCACACCCTGAAGCAGCTGGTGGCT
GCCAAGCTGAAATTGAATGAGGAGCAGGTCGAGGACTATTTCTTTCAGCTCAAGAGCCAG
AAGCGCTATCACGAAGATATCTTTGGTGCTGTATTTCCTTACGAGGCGAAGAAGGACAGG
GTGGCGGTGCAGCCCAGCAGCCTGGAGATGTCAGCGCTCTGA
|
| Enzyme 9 GenBank Gene ID |
BC130283  |
| Enzyme 9 GeneCard ID |
A1L3U5  |
| Enzyme 9 GenAtlas ID |
Not Available |
| Enzyme 9 HGNC ID |
Not Available |
| Enzyme 9 Chromosome Location |
17 |
| Enzyme 9 Locus |
17q11.2-q12 |
| Enzyme 9 SNPs |
SNPJam Report  |
| Enzyme 9 General References |
- Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed
]
|
| Enzyme 9 Metabolite References |
Not Available |
|
Enzyme 10
[top]
|
| Enzyme 10 ID |
16480 |
| Enzyme 10 Name |
cDNA FLJ61209, highly similar to NG,NG-dimethylarginine dimethylaminohydrolase 1 (EC 3.5.3.18) |
| Enzyme 10 Synonyms |
Not Available |
| Enzyme 10 Gene Name |
Not Available |
| Enzyme 10 Protein Sequence |
>cDNA FLJ61209, highly similar to NG,NG-dimethylarginine dimethylaminohydrolase 1 (EC 3.5.3.18)
MKDENATLDGGDVLFTGREFFVGLSKRTNQRGAEILADTFKDYAVSTVPVADGLHLKSFC
SMAGPNLIAIGSSESAQKALKIMQQMSDHRYDKLTVPDDIAANCIYLNIPNKGHVLLHRT
PEEYPESAKVYEKLKDHMLIPVSMSELEKVDGLLTCCSVLINKKVDS
|
| Enzyme 10 Number of Residues |
167 |
| Enzyme 10 Molecular Weight |
18418 |
| Enzyme 10 Theoretical pI |
6.00 |
| Enzyme 10 GO Classification |
Not Available |
| Enzyme 10 General Function |
Amino acid transport and metabolism |
| Enzyme 10 Specific Function |
Not Available |
| Enzyme 10 Pathways |
Not Available |
| Enzyme 10 Reactions |
- Nomega,Nomega'-methyl-L-arginine + H2O = dimethylamine + L-citrulline [RN:R02513] ALL_REAC R02513
|
| Enzyme 10 Pfam Domain Function |
|
| Enzyme 10 Signals |
|
| Enzyme 10 Transmembrane Regions |
|
| Enzyme 10 Essentiality |
Not Available |
| Enzyme 10 GenBank ID Protein |
Not Available |
| Enzyme 10 UniProtKB/Swiss-Prot ID |
B4E3V1  |
| Enzyme 10 UniProtKB/Swiss-Prot Entry Name |
B4E3V1_HUMAN  |
| Enzyme 10 PDB ID |
Not Available |
| Enzyme 10 Cellular Location |
Not Available |
| Enzyme 10 Gene Sequence |
Not Available |
| Enzyme 10 GenBank Gene ID |
AK304876  |
| Enzyme 10 GeneCard ID |
B4E3V1  |
| Enzyme 10 GenAtlas ID |
Not Available |
| Enzyme 10 HGNC ID |
Not Available |
| Enzyme 10 Chromosome Location |
Not Available |
| Enzyme 10 Locus |
Not Available |
| Enzyme 10 SNPs |
Not Available |
| Enzyme 10 General References |
Not Available |
| Enzyme 10 Metabolite References |
Not Available |
|
Enzyme 11
[top]
|
| Enzyme 11 ID |
16523 |
| Enzyme 11 Name |
NOS1 mutant (Nitric oxide synthase 1 (Neuronal), isoform CRA_c) |
| Enzyme 11 Synonyms |
Not Available |
| Enzyme 11 Gene Name |
NOS1 |
| Enzyme 11 Protein Sequence |
>NOS1 mutant (Nitric oxide synthase 1 (Neuronal), isoform CRA_c)
MEDHMFGVQQIQPNVISVRLFKRKVGGLGFLVKERVSKPPVIISDLIRGGAAEQSGLIQA
GDIILAVNGRPLVDLSYDSALEVLRGIASETHVVLILRGPEGFTTHLETTFTGDGTPKTI
RVTQPLGPPTKAVDLSHQPPAGKEQPLAVDGASGPGNGPQHAYDDGQEAGSLPHANGLAP
RPPGQDPAKKATRVSLQGRGENNELLKEIEPVLSLLTSGSRGVKGGAPAKAEMKDMGIQV
DRDLDGKSHKPLPLGVENDRVFNDLWGKGNVPVVLNNPYSEKEQPPTSGKQSPTKNGSPS
KCPRFLKVKNWETEVVLTDTLHLKSTLETGCTEYICMGSIMHPSQHARRPEDVRTKGQLF
PLAKEFIDQYYSSIKRFGSKAHMERLEEVNKEIDTTSTYQLKDTELIYGAKHAWRNASRC
VGRIQWSKLQVFDARDCTTAHGMFNYICNHVKYATNKGNLRSAITIFPQRTDGKHDFRVW
NSQLIRYAGYKQPDGSTLGDPANVQFTEICIQQGWKPPRGRFDVLPLLLQANGNDPELFQ
IPPELVLEVPIRHPKFEWFKDLGLKWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGV
RDYCDNSRYNILEEVAKKMNLDMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSAT
ESFIKHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEMLNYRLTPSFEYQPDPWNTHV
WKGTNGTPTKRRAIGFKKLAEAVKFSAKLMGQAMAKRVKATILYATETGKSQAYAKTLCE
IFKHAFDAKVMSMEEYDIVHLEHETLVLVVTSTFGNGDPPENGEKFGCALMEMRHPNSVQ
EERKSYKVRFNSVSSYSDSQKSSGDGPDLRDNFESAGPLANVRFSVFGLGSRAYPHFCAF
GHAVDTLLEELGGERILKMREGDELCGQEEAFRTWAKKVFKAACDVFCVGDDVNIEKANN
SLISNDRSWKRNKFRLTFVAEAPELTQGLSNVHKKRVSAARLLSRQNLQSPKSSRSTIFV
RLHTNGSQELQYQPGDHLGVFPGNHEDLVNALIERLEDAPPVNQMVKVELLEERNTALGV
ISNWTDELRLPPCTIFQAFKYYLDITTPPTPLQLQQFASLATSEKEKQRLLVLSKGLQEY
EEWKWGKNPTIVEVLEEFPSIQMPATLLLTQLSLLQPRYYSISSSPDMYPDEVHLTVAIV
SYRTRDGEGPIHHGVCSSWLNRIQADELVPCFVRGAPSFHLPRNPQVPCILVGPGTGIAP
FRSFWQQRQFDIQHKGMNPCPMVLVFGCRQSKIDHIYREETLQAKNKGVFRELYTAYSRE
PDKPKKYVQDILQEQLAESVYRALKEQGGHIYVCGDVTMAADVLKAIQRIMTQQGKLSAE
DAGVFISRMRDDNRYHEDIFGVTLRTYEVTNRLRSESIAFIEESKKDTDEVFSS
|
| Enzyme 11 Number of Residues |
1434 |
| Enzyme 11 Molecular Weight |
160972 |
| Enzyme 11 Theoretical pI |
7.44 |
| Enzyme 11 GO Classification |
| Function |
- FAD binding
- FMN binding
- NADP binding
- adenyl nucleotide binding
- binding
- calmodulin binding
- catalytic activity
- cation binding
- coenzyme binding
- cofactor binding
- electron transporter activity
- heme binding
- ion binding
- iron ion binding
- monooxygenase activity
- nitric-oxide synthase activity
- nucleotide binding
- oxidoreductase activity
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD or NADH as one donor, and incorporation of one atom of oxygen
- protein binding
- purine nucleotide binding
- tetrapyrrole binding
- transition metal ion binding
- transporter activity
|
| Process |
- biosynthesis
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- nitric oxide biosynthesis
- physiological process
|
| Component |
| — |
|
| Enzyme 11 General Function |
Inorganic ion transport and metabolism |
| Enzyme 11 Specific Function |
Not Available |
| Enzyme 11 Pathways |
Not Available |
| Enzyme 11 Reactions |
Not Available |
| Enzyme 11 Pfam Domain Function |
|
| Enzyme 11 Signals |
|
| Enzyme 11 Transmembrane Regions |
|
| Enzyme 11 Essentiality |
Not Available |
| Enzyme 11 GenBank ID Protein |
Not Available |
| Enzyme 11 UniProtKB/Swiss-Prot ID |
B3VK56  |
| Enzyme 11 UniProtKB/Swiss-Prot Entry Name |
B3VK56_HUMAN  |
| Enzyme 11 PDB ID |
1TLL  |
| Enzyme 11 PDB File |
Show |
| Enzyme 11 3D Structure |
|
| Enzyme 11 Cellular Location |
Not Available |
| Enzyme 11 Gene Sequence |
Not Available |
| Enzyme 11 GenBank Gene ID |
EU753241  |
| Enzyme 11 GeneCard ID |
B3VK56  |
| Enzyme 11 GenAtlas ID |
Not Available |
| Enzyme 11 HGNC ID |
Not Available |
| Enzyme 11 Chromosome Location |
12 |
| Enzyme 11 Locus |
12q24.2-q24.31 |
| Enzyme 11 SNPs |
SNPJam Report  |
| Enzyme 11 General References |
Not Available |
| Enzyme 11 Metabolite References |
Not Available |