| Version |
2.5 |
| Creation Date |
2005-11-16 15:48:42 |
| Update Date |
2011-06-02 16:32:26 |
| Accession Number |
HMDB00819 |
| Secondary Accession Numbers |
Not Available |
| Common Name |
Normetanephrine |
| Description |
A methylated metabolite of norepinephrine that is excreted in the urine and found in certain tissues. It is a marker for tumors. |
| Synonyms |
- (+/-)-Normetanephrine
- (+/-)-alpha-(aminomethyl)-4-hydroxy-3-methoxy-Benzenemethanol
- 3-O-methyl-Noradrenaline
- 3-methoxy-Noradrenaline
- 4-(2-Amino-1-hydroxyethyl)-2-methoxyphenol
- L-Normetanephrine
- N111
- Normetadrenaline
- O-Methylnoradrenaline
- alpha-(aminomethyl)-4-hydroxy-3-methoxy-Benzenemethanol
- dl-N-Normetanephrine
- dl-Normetanephrine
- m-O-Methylnorepinephrine
|
| Chemical IUPAC Name |
4-(2-amino-1-hydroxy-ethyl)-2-methoxy-phenol |
| Chemical Formula |
C9H13NO3 |
| Chemical Structure |
 |
| Chemical Taxonomy |
| Kingdom |
|
| Super Class |
|
| Class |
- Catecholamines and Derivatives
|
| Sub Class |
|
| Family |
|
| Species |
- secondary alcohol
- 1,2-aminoalcohol
- phenol or hydroxyhetarene
- alkyl aryl ether
- primary amine
- primary aliphatic amine (alkylamine)
- aromatic compound
|
| Biofunction |
| — |
| Application |
| — |
| Source |
|
|
| Average Molecular Weight |
183.204 |
| Monoisotopic Molecular Weight |
183.089539 |
| Isomeric SMILES |
COC1=CC(=CC=C1O)C(O)CN |
| Canonical SMILES |
COC1=CC(=CC=C1O)C(O)CN |
| KEGG Compound ID |
C05589  |
| BioCyc ID |
Not Available |
| BiGG ID |
46080  |
| Wikipedia Link |
Normetanephrine  |
| NuGOwiki Link |
HMDB00819  |
| Metagene Link |
HMDB00819  |
| METLIN ID |
66  |
| PubChem Compound |
1237  |
| PubChem Substance |
8151051  |
| ChEBI ID |
Not Available |
| CAS Registry Number |
97-31-4 |
| InChI Identifier |
InChI=1/C9H13NO3/c1-13-9-4-6(8(12)5-10)2-3-7(9)11/h2-4,8,11-12H,5,10H2,1H3 |
| Synthesis Reference |
Sejbal, Jan; Krecek, Vaclav. Method of preparing normetanephrine. Czech. (1992), 4 pp. |
| Melting Point (Experimental) |
204 |
| Experimental Water Solubility |
Not Available
Source: PhysProp
|
| Predicted Water Solubility |
1000.0 mg/mL [MEYLAN,WM et al. (1996)]; 8.44 mg/mL [Predicted by ALOGPS]
Calculated using ALOGPS
|
| Physiological Charge |
1 |
| State |
Solid |
| Experimental LogP/Hydrophobicity |
-1.05 [HANSCH,C ET AL. (1995)]
Source: PhysProp
|
| Predicted LogP/Hydrophobicity |
-0.71 [Predicted by ALOGPS]; 0 [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 |
Not Available |
| 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 |
Not Available |
| BMRB Spectrum |
Not Available |
| Cellular Location |
- Cytoplasm (Predicted from Solubility)
|
| Biofluid Location |
- Blood
- Cerebrospinal Fluid
- Urine
|
| Tissue Location |
| Tissue |
References |
| Adrenal Gland |
— |
| Adrenal Medulla |
— |
| Brain |
— |
| Platelet |
— |
|
| Concentrations (Normal) |
| Biofluid |
Blood |
| Value |
0.00035 +/- 0.00016 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 |
Blood |
| Value |
0.00022 +/- 0.00052 uM |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Patient information |
Normal |
| Comments |
Subjects who had not abused methamphetamine (MAP) and did not experience flashbacks; n=20 |
| References |
- Yui K, Goto K, Ikemoto S, Ishiguro T: Plasma monoamine metabolites and spontaneous recurrence of methamphetamine-induced paranoid-hallucinatory psychosis: relation of noradrenergic activity to the occurrence of flashbacks. Psychiatry Res. 1996 Jul 31;63(2-3):93-107. [PubMed
]
|
| Biofluid |
Blood |
| Value |
0.00045 +/- 0.00120 uM |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Patient information |
Normal |
| Comments |
subjects who did not experience methamphetamine (MAP) psychosis despite abuse of MAP |
| References |
- Yui K, Goto K, Ikemoto S, Ishiguro T: Plasma monoamine metabolites and spontaneous recurrence of methamphetamine-induced paranoid-hallucinatory psychosis: relation of noradrenergic activity to the occurrence of flashbacks. Psychiatry Res. 1996 Jul 31;63(2-3):93-107. [PubMed
]
|
| Biofluid |
CSF |
| Value |
0.0052 uM |
| Age |
N/A |
| Sex |
N/A |
| Patient information |
Normal |
| Comments |
Not Available |
| References |
- Beck O, Faull KF: Extractive acylation and mass spectrometric assay of 3-methoxytyramine, normetanephrine, and metanephrine in cerebrospinal fluid. Anal Biochem. 1985 Sep;149(2):492-500. [PubMed
]
|
| Biofluid |
Urine |
| Value |
0.00085 +/- 0.00317 umol/mmol creatinine |
| Age |
Adult:>18 yrs old |
| Sex |
N/A |
| Patient information |
Normal |
| Comments |
Not Available |
| References |
- Eisenhofer G, Lenders JW, Linehan WM, Walther MM, Goldstein DS, Keiser HR: Plasma normetanephrine and metanephrine for detecting pheochromocytoma in von Hippel-Lindau disease and multiple endocrine neoplasia type 2. N Engl J Med. 1999 Jun 17;340(24):1872-9. [PubMed
]
- Elmasry A, Lindberg E, Hedner J, Janson C, Boman G: Obstructive sleep apnoea and urine catecholamines in hypertensive males: a population-based study. Eur Respir J. 2002 Mar;19(3):511-7. [PubMed
]
- Barbas C, Garcia A, de Miguel L, Simo C: Evaluation of filter paper collection of urine samples for detection and measurement of organic acidurias by capillary electrophoresis. J Chromatogr B Analyt Technol Biomed Life Sci. 2002 Nov 15;780(1):73-82. [PubMed
]
- Goldstein DS, Eisenhofer G, Kopin IJ: Sources and significance of plasma levels of catechols and their metabolites in humans. J Pharmacol Exp Ther. 2003 Jun;305(3):800-11. Epub 2003 Mar 20. [PubMed
]
- Eisenhofer G, Lenders JW, Goldstein DS, Mannelli M, Csako G, Walther MM, Brouwers FM, Pacak K: Pheochromocytoma catecholamine phenotypes and prediction of tumor size and location by use of plasma free metanephrines. Clin Chem. 2005 Apr;51(4):735-44. Epub 2005 Feb 17. [PubMed
]
- Shoemaker JD, Elliott WH: Automated screening of urine samples for carbohydrates, organic and amino acids after treatment with urease. J Chromatogr. 1991 Jan 2;562(1-2):125-38. [PubMed
]
- Iinuma K, Ikeda I, Ogihara T, Hashizume K, Kurata K, Kumahara Y: Radioimmunoassay of metanephrine and normetanephrine for diagnosis of pheochromocytoma. Clin Chem. 1986 Oct;32(10):1879-83. [PubMed
]
- Lenders JW, Keiser HR, Goldstein DS, Willemsen JJ, Friberg P, Jacobs MC, Kloppenborg PW, Thien T, Eisenhofer G: Plasma metanephrines in the diagnosis of pheochromocytoma. Ann Intern Med. 1995 Jul 15;123(2):101-9. [PubMed
]
- Eisenhofer G, Keiser H, Friberg P, Mezey E, Huynh TT, Hiremagalur B, Ellingson T, Duddempudi S, Eijsbouts A, Lenders JW: Plasma metanephrines are markers of pheochromocytoma produced by catechol-O-methyltransferase within tumors. J Clin Endocrinol Metab. 1998 Jun;83(6):2175-85. [PubMed
]
- Merck Manual
|
| Biofluid |
Urine |
| Value |
<0.322 umol/mmol creatinine |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Patient information |
Normal |
| Comments |
Not Available |
| References |
|
| Biofluid |
Urine |
| Value |
0.062 +/- 0.037 umol/mmol creatinine |
| 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 Cornelius Lentner.
- West Cadwell, N.J. : Medical education Div., Ciba-Geigy Corp.
- Basel, Switzerland c1981-1992.
|
| Biofluid |
Urine |
| Value |
0.85 +/- 3.17 umol/mmol creatinine |
| Age |
Infant:0-1 yr old |
| Sex |
Both |
| Patient information |
Normal |
| Comments |
Not Available |
| References |
- Shoemaker JD, Elliott WH: Automated screening of urine samples for carbohydrates, organic and amino acids after treatment with urease. J Chromatogr. 1991 Jan 2;562(1-2):125-38. [PubMed
]
|
|
| Concentrations (Abnormal) |
| Biofluid |
Blood |
| Value |
0.00093 +/- 0.00158 uM |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Condition |
Amphetamine psychosis |
| Comments |
Neuroleptic-treated flashbackers during flashbacks |
| References |
- Yui K, Goto K, Ikemoto S, Ishiguro T: Plasma monoamine metabolites and spontaneous recurrence of methamphetamine-induced paranoid-hallucinatory psychosis: relation of noradrenergic activity to the occurrence of flashbacks. Psychiatry Res. 1996 Jul 31;63(2-3):93-107. [PubMed
]
|
| Biofluid |
Blood |
| Value |
0.00077 +/- 0.00129 uM |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Condition |
Amphetamine psychosis |
| Comments |
flashbackers during flashbacks |
| References |
- Yui K, Goto K, Ikemoto S, Ishiguro T: Plasma monoamine metabolites and spontaneous recurrence of methamphetamine-induced paranoid-hallucinatory psychosis: relation of noradrenergic activity to the occurrence of flashbacks. Psychiatry Res. 1996 Jul 31;63(2-3):93-107. [PubMed
]
|
| Biofluid |
Blood |
| Value |
0.00063 +/- 0.00101 uM |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Condition |
Amphetamine psychosis |
| Comments |
later-treated flashbackers during flashbacks |
| References |
- Yui K, Goto K, Ikemoto S, Ishiguro T: Plasma monoamine metabolites and spontaneous recurrence of methamphetamine-induced paranoid-hallucinatory psychosis: relation of noradrenergic activity to the occurrence of flashbacks. Psychiatry Res. 1996 Jul 31;63(2-3):93-107. [PubMed
]
|
| Biofluid |
Blood |
| Value |
0.00023 +/- 0.00039 uM |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Condition |
Amphetamine psychosis |
| Comments |
flashbackers during periods of normality |
| References |
- Yui K, Goto K, Ikemoto S, Ishiguro T: Plasma monoamine metabolites and spontaneous recurrence of methamphetamine-induced paranoid-hallucinatory psychosis: relation of noradrenergic activity to the occurrence of flashbacks. Psychiatry Res. 1996 Jul 31;63(2-3):93-107. [PubMed
]
|
| Biofluid |
Blood |
| Value |
0.00029 +/- 0.00048 uM |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Condition |
Amphetamine psychosis |
| Comments |
neuroleptic-treated flashbackers during normality |
| References |
- Yui K, Goto K, Ikemoto S, Ishiguro T: Plasma monoamine metabolites and spontaneous recurrence of methamphetamine-induced paranoid-hallucinatory psychosis: relation of noradrenergic activity to the occurrence of flashbacks. Psychiatry Res. 1996 Jul 31;63(2-3):93-107. [PubMed
]
|
| Biofluid |
Blood |
| Value |
0.00018 +/- 0.00029 uM |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Condition |
Amphetamine psychosis |
| Comments |
later-treated flashbackers during periods of normality |
| References |
- Yui K, Goto K, Ikemoto S, Ishiguro T: Plasma monoamine metabolites and spontaneous recurrence of methamphetamine-induced paranoid-hallucinatory psychosis: relation of noradrenergic activity to the occurrence of flashbacks. Psychiatry Res. 1996 Jul 31;63(2-3):93-107. [PubMed
]
|
| Biofluid |
Blood |
| Value |
0.00023 +/- 0.00034 uM |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Condition |
Amphetamine psychosis |
| Comments |
subjects who did not experience flashbacks despite a history of previous MAP psychosis |
| References |
- Yui K, Goto K, Ikemoto S, Ishiguro T: Plasma monoamine metabolites and spontaneous recurrence of methamphetamine-induced paranoid-hallucinatory psychosis: relation of noradrenergic activity to the occurrence of flashbacks. Psychiatry Res. 1996 Jul 31;63(2-3):93-107. [PubMed
]
|
| Biofluid |
Blood |
| Value |
0.00050 +/- 0.00061 uM |
| Age |
Adult:>18 yrs old |
| Sex |
Both |
| Condition |
Amphetamine psychosis |
| Comments |
MAP psychosis continued for >=6 months before blood collection |
| References |
- Yui K, Goto K, Ikemoto S, Ishiguro T: Plasma monoamine metabolites and spontaneous recurrence of methamphetamine-induced paranoid-hallucinatory psychosis: relation of noradrenergic activity to the occurrence of flashbacks. Psychiatry Res. 1996 Jul 31;63(2-3):93-107. [PubMed
]
|
| Biofluid |
CSF |
| Value |
0.000846 +/- 0.00037 uM |
| Age |
N/A |
| Sex |
N/A |
| Comments |
Not Available |
| References |
- Marshall TH, Jacobson KA, Kirk KL, Linnoila M: Liquid chromatographic assay for cerebrospinal fluid normetanephrine. Life Sci. 1987 Apr 13;40(15):1513-21. [PubMed
]
|
| Biofluid |
CSF |
| Value |
0.000185 +/- 4.424e-05 uM |
| Age |
N/A |
| Sex |
N/A |
| Comments |
Not Available |
| References |
- Foti A, Adachi M, DeQuattro V: The relationships of free to conjugated normetanephrine in plasma and spinal fluid of hypertensive patients. J Clin Endocrinol Metab. 1982 Jul;55(1):81-5. [PubMed
]
|
| Biofluid |
CSF |
| Value |
4.533e-05 +/- 1.256e-05 uM |
| Age |
N/A |
| Sex |
N/A |
| Comments |
Not Available |
| References |
- Foti A, Adachi M, DeQuattro V: The relationships of free to conjugated normetanephrine in plasma and spinal fluid of hypertensive patients. J Clin Endocrinol Metab. 1982 Jul;55(1):81-5. [PubMed
]
|
|
| Associated Disorders |
| Condition |
References |
| Amphetamine psychosis |
- Yui K, Goto K, Ikemoto S, Ishiguro T: Plasma monoamine metabolites and spontaneous recurrence of methamphetamine-induced paranoid-hallucinatory psychosis: relation of noradrenergic activity to the occurrence of flashbacks. Psychiatry Res. 1996 Jul 31;63(2-3):93-107. [PubMed
]
|
|
| OMIM ID |
Not Available |
| Pathways |
|
| General References |
- Schmidt J, Mohr VD, Metzger P, Zirngibl H: Posttraumatic hypertension secondary to adrenal hemorrhage mimicking pheochromocytoma: case report. J Trauma. 1999 May;46(5):973-5. [PubMed
]
- Eisenhofer G, Huysmans F, Pacak K, Walther MM, Sweep FC, Lenders JW: Plasma metanephrines in renal failure. Kidney Int. 2005 Feb;67(2):668-77. [PubMed
]
- Orsulak PJ, Kizuka P, Grab E, Schildkraut JJ: Determination of urinary normetanephrine and metanephrine by radial-compression liquid chromatography and electrochemical detection. Clin Chem. 1983 Feb;29(2):305-9. [PubMed
]
- Linos DA: Management approaches to adrenal incidentalomas (adrenalomas). A view from Athens, Greece. Endocrinol Metab Clin North Am. 2000 Mar;29(1):141-57. [PubMed
]
- Oishi S, Sasaki M, Sato T, Isogai M: Coexistence of MEN 2A and papillary thyroid carcinoma and a recurrent pheochromocytoma 23 years after surgery: report of a case and a review of the Japanese literature. Jpn J Clin Oncol. 1995 Aug;25(4):153-8. [PubMed
]
- Eisenhofer G, Keiser H, Friberg P, Mezey E, Huynh TT, Hiremagalur B, Ellingson T, Duddempudi S, Eijsbouts A, Lenders JW: Plasma metanephrines are markers of pheochromocytoma produced by catechol-O-methyltransferase within tumors. J Clin Endocrinol Metab. 1998 Jun;83(6):2175-85. [PubMed
]
- Filaire E, Legrand B, Bret K, Sagnol M, Cottet-Emard JM, Pequignot JM: Psychobiologic responses to 4 days of increased training and recovery in cyclists. Int J Sports Med. 2002 Nov;23(8):588-94. [PubMed
]
- Filaire E, Legrand B, Lac G, Pequignot JM: Training of elite cyclists: effects on mood state and selected hormonal responses. J Sports Sci. 2004 Nov-Dec;22(11-12):1025-33. [PubMed
]
- Higa S, Suzuki T, Sakoda S, Kishimoto S, Takaba Y, Nakajima A, Markey SP: Disturbed function of the pineal gland in familial amyloid polyneuropathy. J Neural Transm. 1987;69(1-2):97-103. [PubMed
]
- Goldstein DS, Eisenhofer G, Kopin IJ: Sources and significance of plasma levels of catechols and their metabolites in humans. J Pharmacol Exp Ther. 2003 Jun;305(3):800-11. Epub 2003 Mar 20. [PubMed
]
- Wester P, Bergstrom U, Eriksson A, Gezelius C, Hardy J, Winblad B: Ventricular cerebrospinal fluid monoamine transmitter and metabolite concentrations reflect human brain neurochemistry in autopsy cases. J Neurochem. 1990 Apr;54(4):1148-56. [PubMed
]
- Eisenhofer G, Goldstein DS, Sullivan P, Csako G, Brouwers FM, Lai EW, Adams KT, Pacak K: Biochemical and clinical manifestations of dopamine-producing paragangliomas: utility of plasma methoxytyramine. J Clin Endocrinol Metab. 2005 Apr;90(4):2068-75. Epub 2005 Jan 11. [PubMed
]
- Pacak K, Ilias I, Adams KT, Eisenhofer G: Biochemical diagnosis, localization and management of pheochromocytoma: focus on multiple endocrine neoplasia type 2 in relation to other hereditary syndromes and sporadic forms of the tumour. J Intern Med. 2005 Jan;257(1):60-8. [PubMed
]
- Guller U, Turek J, Eubanks S, Delong ER, Oertli D, Feldman JM: Detecting pheochromocytoma: defining the most sensitive test. Ann Surg. 2006 Jan;243(1):102-7. [PubMed
]
- Eisenhofer G, Lenders JW, Goldstein DS, Mannelli M, Csako G, Walther MM, Brouwers FM, Pacak K: Pheochromocytoma catecholamine phenotypes and prediction of tumor size and location by use of plasma free metanephrines. Clin Chem. 2005 Apr;51(4):735-44. Epub 2005 Feb 17. [PubMed
]
- Wikipedia

|
| Metabolic Enzymes |
- Amine oxidase [flavin-containing] B
- Amine oxidase [flavin-containing] A
- Catechol O-methyltransferase
- cDNA, FLJ93072, Homo sapiens monoamine oxidase B (MAOB), nuclear gene encoding mitochondrial protein, mRNA (Monoamine oxidase B, isoform CRA_a)
|
|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5393 |
| Enzyme 1 Name |
Amine oxidase [flavin-containing] B |
| Enzyme 1 Synonyms |
- Monoamine oxidase type B
- MAO-B
|
| Enzyme 1 Gene Name |
MAOB |
| Enzyme 1 Protein Sequence |
>Amine oxidase [flavin-containing] B
MSNKCDVVVVGGGISGMAAAKLLHDSGLNVVVLEARDRVGGRTYTLRNQKVKYVDLGGSY
VGPTQNRILRLAKELGLETYKVNEVERLIHHVKGKSYPFRGPFPPVWNPITYLDHNNFWR
TMDDMGREIPSDAPWKAPLAEEWDNMTMKELLDKLCWTESAKQLATLFVNLCVTAETHEV
SALWFLWYVKQCGGTTRIISTTNGGQERKFVGGSGQVSERIMDLLGDRVKLERPVIYIDQ
TRENVLVETLNHEMYEAKYVISAIPPTLGMKIHFNPPLPMMRNQMITRVPLGSVIKCIVY
YKEPFWRKKDYCGTMIIDGEEAPVAYTLDDTKPEGNYAAIMGFILAHKARKLARLTKEER
LKKLCELYAKVLGSLEALEPVHYEEKNWCEEQYSGGCYTTYFPPGILTQYGRVLRQPVDR
IYFAGTETATHWSGYMEGAVEAGERAAREILHAMGKIPEDEIWQSEPESVDVPAQPITTT
FLERHLPSVPGLLRLIGLTTIFSATALGFLAHKRGLLVRV
|
| Enzyme 1 Number of Residues |
520 |
| Enzyme 1 Molecular Weight |
58762.5 |
| Enzyme 1 Theoretical pI |
7.55 |
| Enzyme 1 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
|
| Process |
- metabolic process
- oxidation reduction
|
| Component |
| — |
|
| Enzyme 1 General Function |
Involved in oxidoreductase activity |
| Enzyme 1 Specific Function |
Catalyzes the oxidative deamination of biogenic and xenobiotic amines and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues. MAOB preferentially degrades benzylamine and phenylethylamine |
| Enzyme 1 Pathways |
|
| Enzyme 1 Reactions |
- RCH2NHR' + H2O + O2 = RCHO + R'NH2 + H2O2 [RN:R01853]
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
Not Available |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
P27338  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
AOFB_HUMAN  |
| Enzyme 1 PDB ID |
2BK3  |
| Enzyme 1 PDB File |
Show |
| Enzyme 1 3D Structure |
|
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>1560 bp
ATGAGCAACAAATGCGACGTGGTCGTGGTGGGGGGCGGCATCTCAGGTATGGCAGCAGCC
AAACTTCTGCATGACTCTGGACTGAATGTGGTTGTTCTGGAAGCCCGGGACCGTGTGGGA
GGCAGGACTTACACTCTTAGGAACCAAAAGGTTAAATATGTGGACCTTGGAGGATCCTAT
GTTGGACCAACCCAGAATCGTATCTTGAGATTAGCCAAGGAGCTAGGATTGGAGACCTAC
AAAGTGAATGAGGTTGAGCGTCTGATCCACCATGTAAAGGGCAAATCATACCCCTTCAGG
GGGCCATTCCCACCTGTATGGAATCCAATTACCTACTTAGATCATAACAACTTTTGGAGG
ACAATGGATGACATGGGGCGAGAGATTCCGAGTGATGCCCCATGGAAGGCTCCCCTTGCA
GAAGAGTGGGACAACATGACAATGAAGGAGCTACTGGACAAGCTCTGCTGGACTGAATCT
GCAAAGCAGCTTGCCACTCTCTTTGTGAACCTGTGTGTCACTGCAGAGACCCATGAGGTC
TCTGCTCTCTGGTTCCTGTGGTATGTGAAGCAGTGTGGAGGCACAACAAGAATCATCTCG
ACAACAAATGGAGGACAGGAGAGGAAATTTGTGGGCGGATCTGGTCAAGTGAGTGAGCGG
ATAATGGACCTCCTTGGAGACCGAGTGAAGCTGGAGAGGCCTGTGATCTACATTGACCAG
ACAAGAGAAAATGTCCTTGTGGAGACCCTAAACCATGAGATGTATGAGGCTAAATATGTG
ATTAGTGCTATTCCTCCTACTCTGGGCATGAAGATTCACTTCAATCCCCCTCTGCCAATG
ATGAGAAACCAGATGATCACTCGTGTGCCTTTGGGTTCAGTCATCAAGTGTATAGTTTAT
TATAAAGAGCCTTTCTGGAGGAAAAAGGATTACTGTGGAACCATGATTATTGATGGAGAA
GAAGCTCCAGTTGCCTACACGTTGGATGATACCAAACCTGAAGGCAACTATGCTGCCATA
ATGGGATTTATCCTGGCCCACAAAGCCAGAAAACTGGCACGTCTTACCAAAGAGGAAAGG
TTGAAGAAACTTTGTGAACTCTATGCCAAGGTTCTGGGTTCCCTAGAAGCTCTGGAGCCA
GTGCATTATGAAGAAAAGAACTGGTGTGAGGAGCAGTACTCTGGGGGCTGCTACACAACT
TATTTCCCCCCTGGGATCCTGACTCAATATGGAAGGGTTCTACGCCAGCCAGTGGACAGG
ATTTACTTTGCAGGCACCGAGACTGCCACACACTGGAGCGGCTACATGGAGGGGGCTGTA
GAGGCCGGGGAGAGAGCAGCCCGAGAGATCCTGCATGCCATGGGGAAGATTCCAGAGGAT
GAAATCTGGCAGTCAGAACCAGAGTCTGTGGATGTCCCTGCACAGCCCATCACCACCACC
TTTTTGGAGAGACATTTGCCCTCCGTGCCAGGCCTGCTCAGGCTGATTGGATTGACCACC
ATCTTTTCAGCAACGGCTCTTGGCTTCCTGGCCCACAAAAGGGGGCTACTTGTGAGAGTC
|
| Enzyme 1 GenBank Gene ID |
S62734  |
| Enzyme 1 GeneCard ID |
MAOB  |
| Enzyme 1 GenAtlas ID |
MAOB  |
| Enzyme 1 HGNC ID |
HGNC:6834  |
| Enzyme 1 Chromosome Location |
Not Available |
| Enzyme 1 Locus |
Not Available |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- Grimsby J, Chen K, Wang LJ, Lan NC, Shih JC: Human monoamine oxidase A and B genes exhibit identical exon-intron organization. Proc Natl Acad Sci U S A. 1991 May 1;88(9):3637-41. [PubMed
]
- Bach AW, Lan NC, Johnson DL, Abell CW, Bembenek ME, Kwan SW, Seeburg PH, Shih JC: cDNA cloning of human liver monoamine oxidase A and B: molecular basis of differences in enzymatic properties. Proc Natl Acad Sci U S A. 1988 Jul;85(13):4934-8. [PubMed
]
- Chen K, Wu HF, Shih JC: The deduced amino acid sequences of human platelet and frontal cortex monoamine oxidase B are identical. J Neurochem. 1993 Jul;61(1):187-90. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Ross MT, Grafham DV, Coffey AJ, Scherer S, McLay K, Muzny D, Platzer M, Howell GR, Burrows C, Bird CP, Frankish A, Lovell FL, Howe KL, Ashurst JL, Fulton RS, Sudbrak R, Wen G, Jones MC, Hurles ME, Andrews TD, Scott CE, Searle S, Ramser J, Whittaker A, Deadman R, Carter NP, Hunt SE, Chen R, Cree A, Gunaratne P, Havlak P, Hodgson A, Metzker ML, Richards S, Scott G, Steffen D, Sodergren E, Wheeler DA, Worley KC, Ainscough R, Ambrose KD, Ansari-Lari MA, Aradhya S, Ashwell RI, Babbage AK, Bagguley CL, Ballabio A, Banerjee R, Barker GE, Barlow KF, Barrett IP, Bates KN, Beare DM, Beasley H, Beasley O, Beck A, Bethel G, Blechschmidt K, Brady N, Bray-Allen S, Bridgeman AM, Brown AJ, Brown MJ, Bonnin D, Bruford EA, Buhay C, Burch P, Burford D, Burgess J, Burrill W, Burton J, Bye JM, Carder C, Carrel L, Chako J, Chapman JC, Chavez D, Chen E, Chen G, Chen Y, Chen Z, Chinault C, Ciccodicola A, Clark SY, Clarke G, Clee CM, Clegg S, Clerc-Blankenburg K, Clifford K, Cobley V, Cole CG, Conquer JS, Corby N, Connor RE, David R, Davies J, Davis C, Davis J, Delgado O, Deshazo D, Dhami P, Ding Y, Dinh H, Dodsworth S, Draper H, Dugan-Rocha S, Dunham A, Dunn M, Durbin KJ, Dutta I, Eades T, Ellwood M, Emery-Cohen A, Errington H, Evans KL, Faulkner L, Francis F, Frankland J, Fraser AE, Galgoczy P, Gilbert J, Gill R, Glockner G, Gregory SG, Gribble S, Griffiths C, Grocock R, Gu Y, Gwilliam R, Hamilton C, Hart EA, Hawes A, Heath PD, Heitmann K, Hennig S, Hernandez J, Hinzmann B, Ho S, Hoffs M, Howden PJ, Huckle EJ, Hume J, Hunt PJ, Hunt AR, Isherwood J, Jacob L, Johnson D, Jones S, de Jong PJ, Joseph SS, Keenan S, Kelly S, Kershaw JK, Khan Z, Kioschis P, Klages S, Knights AJ, Kosiura A, Kovar-Smith C, Laird GK, Langford C, Lawlor S, Leversha M, Lewis L, Liu W, Lloyd C, Lloyd DM, Loulseged H, Loveland JE, Lovell JD, Lozado R, Lu J, Lyne R, Ma J, Maheshwari M, Matthews LH, McDowall J, McLaren S, McMurray A, Meidl P, Meitinger T, Milne S, Miner G, Mistry SL, Morgan M, Morris S, Muller I, Mullikin JC, Nguyen N, Nordsiek G, Nyakatura G, O'Dell CN, Okwuonu G, Palmer S, Pandian R, Parker D, Parrish J, Pasternak S, Patel D, Pearce AV, Pearson DM, Pelan SE, Perez L, Porter KM, Ramsey Y, Reichwald K, Rhodes S, Ridler KA, Schlessinger D, Schueler MG, Sehra HK, Shaw-Smith C, Shen H, Sheridan EM, Shownkeen R, Skuce CD, Smith ML, Sotheran EC, Steingruber HE, Steward CA, Storey R, Swann RM, Swarbreck D, Tabor PE, Taudien S, Taylor T, Teague B, Thomas K, Thorpe A, Timms K, Tracey A, Trevanion S, Tromans AC, d'Urso M, Verduzco D, Villasana D, Waldron L, Wall M, Wang Q, Warren J, Warry GL, Wei X, West A, Whitehead SL, Whiteley MN, Wilkinson JE, Willey DL, Williams G, Williams L, Williamson A, Williamson H, Wilming L, Woodmansey RL, Wray PW, Yen J, Zhang J, Zhou J, Zoghbi H, Zorilla S, Buck D, Reinhardt R, Poustka A, Rosenthal A, Lehrach H, Meindl A, Minx PJ, Hillier LW, Willard HF, Wilson RK, Waterston RH, Rice CM, Vaudin M, Coulson A, Nelson DL, Weinstock G, Sulston JE, Durbin R, Hubbard T, Gibbs RA, Beck S, Rogers J, Bentley DR: The DNA sequence of the human X chromosome. Nature. 2005 Mar 17;434(7031):325-37. [PubMed
]
- Zhu QS, Grimsby J, Chen K, Shih JC: Promoter organization and activity of human monoamine oxidase (MAO) A and B genes. J Neurosci. 1992 Nov;12(11):4437-46. [PubMed
]
- Newton-Vinson P, Hubalek F, Edmondson DE: High-level expression of human liver monoamine oxidase B in Pichia pastoris. Protein Expr Purif. 2000 Nov;20(2):334-45. [PubMed
]
- Cesura AM, Gottowik J, Lahm HW, Lang G, Imhof R, Malherbe P, Rothlisberger U, Da Prada M: Investigation on the structure of the active site of monoamine oxidase-B by affinity labeling with the selective inhibitor lazabemide and by site-directed mutagenesis. Eur J Biochem. 1996 Mar 15;236(3):996-1002. [PubMed
]
- Wu HF, Chen K, Shih JC: Site-directed mutagenesis of monoamine oxidase A and B: role of cysteines. Mol Pharmacol. 1993 Jun;43(6):888-93. [PubMed
]
- Binda C, Newton-Vinson P, Hubalek F, Edmondson DE, Mattevi A: Structure of human monoamine oxidase B, a drug target for the treatment of neurological disorders. Nat Struct Biol. 2002 Jan;9(1):22-6. [PubMed
]
- Binda C, Li M, Hubalek F, Restelli N, Edmondson DE, Mattevi A: Insights into the mode of inhibition of human mitochondrial monoamine oxidase B from high-resolution crystal structures. Proc Natl Acad Sci U S A. 2003 Aug 19;100(17):9750-5. Epub 2003 Aug 11. [PubMed
]
- Binda C, Hubalek F, Li M, Herzig Y, Sterling J, Edmondson DE, Mattevi A: Crystal structures of monoamine oxidase B in complex with four inhibitors of the N-propargylaminoindan class. J Med Chem. 2004 Mar 25;47(7):1767-74. [PubMed
]
- Hubalek F, Binda C, Khalil A, Li M, Mattevi A, Castagnoli N, Edmondson DE: Demonstration of isoleucine 199 as a structural determinant for the selective inhibition of human monoamine oxidase B by specific reversible inhibitors. J Biol Chem. 2005 Apr 22;280(16):15761-6. Epub 2005 Feb 14. [PubMed
]
- Binda C, Hubalek F, Li M, Herzig Y, Sterling J, Edmondson DE, Mattevi A: Binding of rasagiline-related inhibitors to human monoamine oxidases: a kinetic and crystallographic analysis. J Med Chem. 2005 Dec 29;48(26):8148-54. [PubMed
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
5401 |
| Enzyme 2 Name |
Amine oxidase [flavin-containing] A |
| Enzyme 2 Synonyms |
- Monoamine oxidase type A
- MAO-A
|
| Enzyme 2 Gene Name |
MAOA |
| Enzyme 2 Protein Sequence |
>Amine oxidase [flavin-containing] A
MENQEKASIAGHMFDVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRTYTIRNEHV
DYVDVGGAYVGPTQNRILRLSKELGIETYKVNVSERLVQYVKGKTYPFRGAFPPVWNPIA
YLDYNNLWRTIDNMGKEIPTDAPWEAQHADKWDKMTMKELIDKICWTKTARRFAYLFVNI
NVTSEPHEVSALWFLWYVKQCGGTTRIFSVTNGGQERKFVGGSGQVSERIMDLLGDQVKL
NHPVTHVDQSSDNIIIETLNHEHYECKYVINAIPPTLTAKIHFRPELPAERNQLIQRLPM
GAVIKCMMYYKEAFWKKKDYCGCMIIEDEDAPISITLDDTKPDGSLPAIMGFILARKADR
LAKLHKEIRKKKICELYAKVLGSQEALHPVHYEEKNWCEEQYSGGCYTAYFPPGIMTQYG
RVIRQPVGRIFFAGTETATKWSGYMEGAVEAGERAAREVLNGLGKVTEKDIWVQEPESKD
VPAVEITHTFWERNLPSVSGLLKIIGFSTSVTALGFVLYKYKLLPRS
|
| Enzyme 2 Number of Residues |
527 |
| Enzyme 2 Molecular Weight |
59681.3 |
| Enzyme 2 Theoretical pI |
7.96 |
| Enzyme 2 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
|
| Process |
- metabolic process
- oxidation reduction
|
| Component |
| — |
|
| Enzyme 2 General Function |
Involved in oxidoreductase activity |
| Enzyme 2 Specific Function |
Catalyzes the oxidative deamination of biogenic and xenobiotic amines and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues. MAOA preferentially oxidizes biogenic amines such as 5-hydroxytryptamine (5-HT), norepinephrine and epinephrine |
| Enzyme 2 Pathways |
|
| Enzyme 2 Reactions |
- RCH2NHR' + H2O + O2 = RCHO + R'NH2 + H2O2 [RN:R01853]
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
187355  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
P21397  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
AOFA_HUMAN  |
| Enzyme 2 PDB ID |
1O5W  |
| Enzyme 2 PDB File |
Show |
| Enzyme 2 3D Structure |
|
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>1584 bp
ATGGAGAATCAAGAGAAGGCGAGTATCGCGGGCCACATGTTCGACGTAGTCGTGATCGGA
GGTGGCATTTCAGGACTATCTGCTGCCAAACTCTTGACTGAATATGGCGTTAGTGTTTTG
GTTTTAGAAGCTCGGGACAGGGTTGGAGGAAGAACATATACTATAAGGAATGAGCATGTT
GATTACGTAGATGTTGGTGGAGCTTATGTGGGACCAACCCAAAACAGAATCTTACGCTTG
TCTAAGGAGCTGGGCATAGAGACTTACAAAGTGAATGTCAGTGAGCGTCTCGTTCAATAT
GTCAAGGGGAAAACATATCCATTTCGGGGCGCCTTTCCACCAGTATGGAATCCCATTGCA
TATTTGGATTACAATAATCTGTGGAGGACAATAGATAACATGGGGAAGGAGATTCCAACT
GATGCACCCTGGGAGGCTCAACATGCTGACAAATGGGACAAAATGACCATGAAAGAGCTC
ATTGACAAAATCTGCTGGACAAAGACTGCTAGGCGGTTTGCTTATCTTTTTGTGAATATC
AATGTGACCTCTGAGCCTCACGAAGTGTCTGCCCTGTGGTTCTTGTGGTATGTGAAGCAG
TGCGGGGGCACCACTCGGATATTCTCTGTCACCAATGGTGGCCAGGAACGGAAGTTTGTA
GGTGGATCTGGTCAAGTGAGCGAACGGATAATGGACCTCCTCGGAGACCAAGTGAAGCTG
AACCATCCTGTCACTCACGTTGACCAGTCAAGTGACAACATCATCATAGAGACGCTGAAC
CATGAACATTATGAGTGCAAATACGTAATTAATGCGATCCCTCCGACCTTGACTGCCAAG
ATTCACTTCAGACCAGAGCTTCCAGCAGAGAGAAACCAGTTAATTCAGCGTCTTCCAATG
GGAGCTGTCATTAAGTGCATGATGTATTACAAGGAGGCCTTCTGGAAGAAGAAGGATTAC
TGTGGCTGCATGATCATTGAAGATGAAGATGCTCCAATTTCAATAACCTTGGATGACACC
AAGCCAGATGGGTCACTGCCTGCCATCATGGGCTTCATTCTTGCCCGGAAAGCTGATCGA
CTTGCTAAGCTACATAAGGAAATAAGGAAGAAGAAAATCTGTGAGCTCTATGCCAAAGTG
CTGGGATCCCAAGAAGCTTTACATCCAGTGCATTATGAAGAGAAGAACTGGTGTGAGGAG
CAGTACTCTGGGGGCTGCTACACGGCCTACTTCCCTCCTGGGATCATGACTCAATATGGA
AGGGTGATTCGTCAACCCGTGGGCAGGATTTTCTTTGCGGGCACAGAGACTGCCACAAAG
TGGAGCGGCTACATGGAAGGGGCAGTTGAGGCTGGAGAACGAGCAGCTAGGGAGGTCTTA
AATGGTCTCGGGAAGGTGACCGAGAAAGACATCTGGGTACAAGAACCTGAATCAAAGGAC
GTTCCAGCGGTAGAAATCACCCACACCTTCTGGGAAAGGAACCTGCCCTCTGTTTCTGGC
CTGCTGAAGATCATTGGATTTTCCACATCAGTAACTGCCCTGGGGTTTGTGCTGTACAAA
TACAAGCTCCTGCCACGGTCTTGA
|
| Enzyme 2 GenBank Gene ID |
M69226  |
| Enzyme 2 GeneCard ID |
MAOA  |
| Enzyme 2 GenAtlas ID |
MAOA  |
| Enzyme 2 HGNC ID |
HGNC:6833  |
| Enzyme 2 Chromosome Location |
Not Available |
| Enzyme 2 Locus |
Not Available |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- Hsu YP, Weyler W, Chen S, Sims KB, Rinehart WB, Utterback MC, Powell JF, Breakefield XO: Structural features of human monoamine oxidase A elucidated from cDNA and peptide sequences. J Neurochem. 1988 Oct;51(4):1321-4. [PubMed
]
- Bach AW, Lan NC, Johnson DL, Abell CW, Bembenek ME, Kwan SW, Seeburg PH, Shih JC: cDNA cloning of human liver monoamine oxidase A and B: molecular basis of differences in enzymatic properties. Proc Natl Acad Sci U S A. 1988 Jul;85(13):4934-8. [PubMed
]
- Chen ZY, Hotamisligil GS, Huang JK, Wen L, Ezzeddine D, Aydin-Muderrisoglu N, Powell JF, Huang RH, Breakefield XO, Craig I, et al.: Structure of the human gene for monoamine oxidase type A. Nucleic Acids Res. 1991 Aug 25;19(16):4537-41. [PubMed
]
- Grimsby J, Chen K, Wang LJ, Lan NC, Shih JC: Human monoamine oxidase A and B genes exhibit identical exon-intron organization. Proc Natl Acad Sci U S A. 1991 May 1;88(9):3637-41. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Zhu QS, Grimsby J, Chen K, Shih JC: Promoter organization and activity of human monoamine oxidase (MAO) A and B genes. J Neurosci. 1992 Nov;12(11):4437-46. [PubMed
]
- Denney RM: The promoter of the human monoamine oxidase A gene. Prog Brain Res. 1995;106:57-66. [PubMed
]
- Denney RM, Sharma A, Dave SK, Waguespack A: A new look at the promoter of the human monoamine oxidase A gene: mapping transcription initiation sites and capacity to drive luciferase expression. J Neurochem. 1994 Sep;63(3):843-56. [PubMed
]
- Chen SA, Weyler W: Partial amino acid sequence analysis of human placenta monoamine oxidase A and bovine liver monoamine oxidase B. Biochem Biophys Res Commun. 1988 Oct 14;156(1):445-50. [PubMed
]
- Weyler W: Monoamine oxidase A from human placenta and monoamine oxidase B from bovine liver both have one FAD per subunit. Biochem J. 1989 Jun 15;260(3):725-9. [PubMed
]
- Li M, Hubalek F, Newton-Vinson P, Edmondson DE: High-level expression of human liver monoamine oxidase A in Pichia pastoris: comparison with the enzyme expressed in Saccharomyces cerevisiae. Protein Expr Purif. 2002 Feb;24(1):152-62. [PubMed
]
- Wu HF, Chen K, Shih JC: Site-directed mutagenesis of monoamine oxidase A and B: role of cysteines. Mol Pharmacol. 1993 Jun;43(6):888-93. [PubMed
]
- De Colibus L, Li M, Binda C, Lustig A, Edmondson DE, Mattevi A: Three-dimensional structure of human monoamine oxidase A (MAO A): relation to the structures of rat MAO A and human MAO B. Proc Natl Acad Sci U S A. 2005 Sep 6;102(36):12684-9. Epub 2005 Aug 29. [PubMed
]
- Brunner HG, Nelen M, Breakefield XO, Ropers HH, van Oost BA: Abnormal behavior associated with a point mutation in the structural gene for monoamine oxidase A. Science. 1993 Oct 22;262(5133):578-80. [PubMed
]
- Son SY, Ma J, Kondou Y, Yoshimura M, Yamashita E, Tsukihara T: Structure of human monoamine oxidase A at 2.2-A resolution: the control of opening the entry for substrates/inhibitors. Proc Natl Acad Sci U S A. 2008 Apr 15;105(15):5739-44. Epub 2008 Apr 7. [PubMed
]
- Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
5504 |
| Enzyme 3 Name |
Catechol O-methyltransferase |
| Enzyme 3 Synonyms |
Not Available |
| Enzyme 3 Gene Name |
COMT |
| Enzyme 3 Protein Sequence |
>Catechol O-methyltransferase
MPEAPPLLLAAVLLGLVLLVVLLLLLRHWGWGLCLIGWNEFILQPIHNLLMGDTKEQRIL
NHVLQHAEPGNAQSVLEAIDTYCEQKEWAMNVGDKKGKIVDAVIQEHQPSVLLELGAYCG
YSAVRMARLLSPGARLITIEINPDCAAITQRMVDFAGVKDKVTLVVGASQDIIPQLKKKY
DVDTLDMVFLDHWKDRYLPDTLLLEECGLLRKGTVLLADNVICPGAPDFLAHVRGSSCFE
CTHYQSFLEYREVVDGLEKAIYKGPGSEAGP
|
| Enzyme 3 Number of Residues |
271 |
| Enzyme 3 Molecular Weight |
30036.8 |
| Enzyme 3 Theoretical pI |
5.15 |
| Enzyme 3 GO Classification |
| Function |
- O-methyltransferase activity
- binding
- catalytic activity
- catechol O-methyltransferase activity
- cation binding
- ion binding
- magnesium ion binding
- metal ion binding
- methyltransferase activity
- transferase activity
- transferase activity, transferring one-carbon groups
|
| Process |
- biological regulation
- catecholamine metabolic process
- cellular amino acid and derivative metabolic process
- cellular amino acid derivative metabolic process
- cellular biogenic amine metabolic process
- cellular metabolic process
- metabolic process
- neurotransmitter catabolic process
- neurotransmitter metabolic process
- regulation of biological quality
- regulation of neurotransmitter levels
|
| Component |
| — |
|
| Enzyme 3 General Function |
Involved in magnesium ion binding |
| Enzyme 3 Specific Function |
Catalyzes the O-methylation, and thereby the inactivation, of catecholamine neurotransmitters and catechol hormones. Also shortens the biological half-lives of certain neuroactive drugs, like L-DOPA, alpha-methyl DOPA and isoproterenol |
| Enzyme 3 Pathways |
|
| Enzyme 3 Reactions |
- S-adenosyl-L-methionine + a catechol = S-adenosyl-L-homocysteine + a guaiacol [RN:R07330]
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
180920  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
P21964  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
COMT_HUMAN  |
| Enzyme 3 PDB ID |
Not Available |
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>816 bp
ATGCCGGAGGCCCCGCCTCTGCTGTTGGCAGCTGTGTTGCTGGGCCTGGTGCTGCTGGTG
GTGCTGCTGCTGCTTCTGAGGCACTGGGGCTGGGGCCTGTGCCTTATCGGCTGGAACGAG
TTCATCCTGCAGCCCATCCACAACCTGCTCATGGGTGACACCAAGGAGCAGCGCATCCTG
AACCACGTGCTGCAGCATGCGGAGCCCGGGAACGCACAGAGCGTGCTGGAGGCCATTGAC
ACCTACTGCGAGCAGAAGGAGTGGGCCATGAACGTGGGCGACAAGAAAGGCAAGATCGTG
GACGCCGTGATTCAGGAGCACCAGCCCTCCGTGCTGCTGGAGCTGGGGGCCTACTGTGGC
TACTCAGCTGTGCGCATGGCCCGCCTGCTGTCACCAGGGGCGAGGCTCATCACCATCGAG
ATCAACCCCGACTGTGCCGCCATCACCCAGCGGATGGTGGATTTCGCTGGCGTGAAGGAC
AAGGTCACCCTTGTGGTTGGAGCGTCCCAGGACATCATCCCCCAGCTGAAGAAGAAGTAT
GATGTGGACACACTGGACATGGTCTTCCTCGACCACTGGAAGGACCGGTACCTGCCGGAC
ACGCTTCTCTTGGAGGAATGTGGCCTGCTGCGGAAGGGGACAGTGCTACTGGCTGACAAC
GTGATCTGCCCAGGTGCGCCAGACTTCCTAGCACACGTGCGCGGGAGCAGCTGCTTTGAG
TGCACACACTACCAATCGTTCCTGGAATACAGGGAGGTGGTGGACGGCCTGGAGAAGGCC
ATCTACAAGGGCCCAGGCAGCGAAGCAGGGCCCTGA
|
| Enzyme 3 GenBank Gene ID |
M65212  |
| Enzyme 3 GeneCard ID |
COMT  |
| Enzyme 3 GenAtlas ID |
COMT  |
| Enzyme 3 HGNC ID |
HGNC:2228  |
| Enzyme 3 Chromosome Location |
2 |
| Enzyme 3 Locus |
22q11.21-q11.23|22q11.21 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- Lundstrom K, Salminen M, Jalanko A, Savolainen R, Ulmanen I: Cloning and characterization of human placental catechol-O-methyltransferase cDNA. DNA Cell Biol. 1991 Apr;10(3):181-9. [PubMed
]
- Bertocci B, Miggiano V, Da Prada M, Dembic Z, Lahm HW, Malherbe P: Human catechol-O-methyltransferase: cloning and expression of the membrane-associated form. Proc Natl Acad Sci U S A. 1991 Feb 15;88(4):1416-20. [PubMed
]
- Tenhunen J, Salminen M, Lundstrom K, Kiviluoto T, Savolainen R, Ulmanen I: Genomic organization of the human catechol O-methyltransferase gene and its expression from two distinct promoters. Eur J Biochem. 1994 Aug 1;223(3):1049-59. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Collins JE, Wright CL, Edwards CA, Davis MP, Grinham JA, Cole CG, Goward ME, Aguado B, Mallya M, Mokrab Y, Huckle EJ, Beare DM, Dunham I: A genome annotation-driven approach to cloning the human ORFeome. Genome Biol. 2004;5(10):R84. Epub 2004 Sep 30. [PubMed
]
- Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Vilbois F, Caspers P, da Prada M, Lang G, Karrer C, Lahm HW, Cesura AM: Mass spectrometric analysis of human soluble catechol O-methyltransferase expressed in Escherichia coli. Identification of a product of ribosomal frameshifting and of reactive cysteines involved in S-adenosyl-L-methionine binding. Eur J Biochem. 1994 Jun 1;222(2):377-86. [PubMed
]
- Tilgmann C, Kalkkinen N: Purification and partial sequence analysis of the soluble catechol-O-methyltransferase from human placenta: comparison to the rat liver enzyme. Biochem Biophys Res Commun. 1991 Jan 31;174(2):995-1002. [PubMed
]
- Ulmanen I, Lundstrom K: Cell-free synthesis of rat and human catechol O-methyltransferase. Insertion of the membrane-bound form into microsomal membranes in vitro. Eur J Biochem. 1991 Dec 18;202(3):1013-20. [PubMed
]
- Rutherford K, Le Trong I, Stenkamp RE, Parson WW: Crystal structures of human 108V and 108M catechol O-methyltransferase. J Mol Biol. 2008 Jun 27;380(1):120-30. Epub 2008 Apr 23. [PubMed
]
- Lachman HM, Papolos DF, Saito T, Yu YM, Szumlanski CL, Weinshilboum RM: Human catechol-O-methyltransferase pharmacogenetics: description of a functional polymorphism and its potential application to neuropsychiatric disorders. Pharmacogenetics. 1996 Jun;6(3):243-50. [PubMed
]
- Tiihonen J, Hallikainen T, Lachman H, Saito T, Volavka J, Kauhanen J, Salonen JT, Ryynanen OP, Koulu M, Karvonen MK, Pohjalainen T, Syvalahti E, Hietala J: Association between the functional variant of the catechol-O-methyltransferase (COMT) gene and type 1 alcoholism. Mol Psychiatry. 1999 May;4(3):286-9. [PubMed
]
- Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [PubMed
]
- Lee SG, Joo Y, Kim B, Chung S, Kim HL, Lee I, Choi B, Kim C, Song K: Association of Ala72Ser polymorphism with COMT enzyme activity and the risk of schizophrenia in Koreans. Hum Genet. 2005 Mar;116(4):319-28. Epub 2005 Jan 12. [PubMed
]
- Rutherford K, Alphandery E, McMillan A, Daggett V, Parson WW: The V108M mutation decreases the structural stability of catechol O-methyltransferase. Biochim Biophys Acta. 2008 Jul-Aug;1784(7-8):1098-105. Epub 2008 Apr 24. [PubMed
]
- Annerbrink K, Westberg L, Nilsson S, Rosmond R, Holm G, Eriksson E: Catechol O-methyltransferase val158-met polymorphism is associated with abdominal obesity and blood pressure in men. Metabolism. 2008 May;57(5):708-11. [PubMed
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
16425 |
| Enzyme 4 Name |
cDNA, FLJ93072, Homo sapiens monoamine oxidase B (MAOB), nuclear gene encoding mitochondrial protein, mRNA (Monoamine oxidase B, isoform CRA_a) |
| Enzyme 4 Synonyms |
Not Available |
| Enzyme 4 Gene Name |
MAOB |
| Enzyme 4 Protein Sequence |
>cDNA, FLJ93072, Homo sapiens monoamine oxidase B (MAOB), nuclear gene encoding mitochondrial protein, mRNA (Monoamine oxidase B, isoform CRA_a)
MSNKCDVVVVGGGISGMAAAKLLHDSGLNVVVLEARDRVGGRTYTLRNQKVKYVDLGGSY
VGPTQNRILRLAKELGLETYKVNEVERLIHHVKGKSYPFRGPFPPVWNPITYLDHNNFWR
TMDDMGREIPSDAPWKAPLAEEWDNMTMKELLDKLCWTESAKQLATLFVNLCVTAETHEV
SALWFLWYVKQCGGTTRIISTTNGGQERKFVGGSGQVSERIMDLLGDRVKLERPVIYIDQ
TRENVLVETLNHEMYEAKYVISAIPPTLGMKIHFNPPLPMMRNQMITRVPLGSVIKCIVY
YKEPFWRKKDYCGTMIIDGEEAPVAYTLDDTKPEGNYAAIMGFILAHKARKLARLTKEER
LKKLCELYAKVLGSLEALEPVHYEEKNWCEEQYSGGCYTTYFPPGILTQYGRVLRQPVDR
IYFAGTETATHWSGYMEGAVEAGERAAREILHAMGKIPEDEIWQSEPESVDVPAQPITTT
FLERHLPSVPGLLRLIGLTTIFSATALGFLAHKRGLLVRV
|
| Enzyme 4 Number of Residues |
520 |
| Enzyme 4 Molecular Weight |
58764 |
| Enzyme 4 Theoretical pI |
7.55 |
| Enzyme 4 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
|
| Process |
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 4 General Function |
Amino acid transport and metabolism |
| Enzyme 4 Specific Function |
Not Available |
| Enzyme 4 Pathways |
Not Available |
| Enzyme 4 Reactions |
Not Available |
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
Not Available |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
B2R6R3  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
B2R6R3_HUMAN  |
| Enzyme 4 PDB ID |
2BK3  |
| Enzyme 4 PDB File |
Show |
| Enzyme 4 3D Structure |
|
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
Not Available |
| Enzyme 4 GenBank Gene ID |
AK312679  |
| Enzyme 4 GeneCard ID |
B2R6R3  |
| Enzyme 4 GenAtlas ID |
Not Available |
| Enzyme 4 HGNC ID |
Not Available |
| Enzyme 4 Chromosome Location |
Not Available |
| Enzyme 4 Locus |
Not Available |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
Not Available |
| Enzyme 4 Metabolite References |
Not Available |