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Human Metabolome Database Version 2.5

 

Showing metabocard for 1,3-Diaminopropane (HMDB00002)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-08-06 11:58:08
Accession Number HMDB00002
Secondary Accession Numbers Not Available
Common Name 1,3-Diaminopropane
Description 1,3-Diaminopropane is a stable, flammable and highly hydroscopic fluid. It is a polyamine that is normally quite toxic if swallowed, inhaled or absorbed through the skin. It is a catabolic byproduct of spermidine. It is also a precursor in the enzymatic synthesis of beta-alanine. 1, 3-Diaminopropane is involved in the arginine/proline metabolic pathways and the beta-alanine metabolic pathway.
Synonyms
  1. 1,3-Diamino-n-propane
  2. 1,3-Propylenediamine
  3. 1,3-Trimethylenediamine
  4. 1,3-propanediamine
  5. 3-Aminopropylamine
  6. Propane-1,3-diamine
  7. Trimethylenediamine
  8. a,w-Propanediamine
Chemical IUPAC Name propane-1,3-diamine
Chemical Formula C3H10N2
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Amines
Class
  • Polyamines
Sub Class
  • Miscellaneous polyamines
Family
  • Mammalian Metabolite
Species
  • primary amine
  • primary aliphatic amine (alkylamine)
Biofunction
Application
Source
  • Endogenous
Average Molecular Weight 74.125
Monoisotopic Molecular Weight 74.084396
Isomeric SMILES NCCCN
Canonical SMILES NCCCN
KEGG Compound ID C00986 Link Image
BioCyc ID CPD-313 Link Image
BiGG ID 36543 Link Image
Wikipedia Link Not Available
NuGOwiki Link HMDB00002 Link Image
Metagene Link HMDB00002 Link Image
METLIN ID 5081 Link Image
PubChem Compound 428 Link Image
PubChem Substance 11369168 Link Image
ChEBI ID 15725 Link Image
CAS Registry Number 109-76-2
InChI Identifier InChI=1/C3H10N2/c4-2-1-3-5/h1-5H2
Synthesis Reference Takayanagi, Yasuyuki; Oohinata, Takahiro. Preparation of 1,3-diaminopropane from acrylonitrile and ammonia. Jpn. Kokai Tokkyo Koho (1994), 5 pp.
Melting Point (Experimental) -12 oC
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 1000 mg/mL at 25 oC [MEYLAN,WM et al. (1996)]; 437.0 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 2
State Liquid
Experimental LogP/Hydrophobicity -1.43 [HANSCH,C ET AL. (1995)] Source: PhysProp
Predicted LogP/Hydrophobicity -1 [Predicted by PubChem via XLOGP]; -1.41 [Predicted by ALOGPS] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show Link Image
SDF File Show Link Image
PDB File Show Link Image
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Varian)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Show Image
Show Peaklist
BMRB Spectrum Show Image
Show Peaklist
Cellular Location
  • Cytoplasm
Biofluid Location
  • Blood
  • Urine
Tissue Location Not Available
Concentrations (Normal)
Biofluid Blood
Value 0.04 +/- 0.03 uM
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Byun JA, Lee SH, Jung BH, Choi MH, Moon MH, Chung BC: Analysis of polyamines as carbamoyl derivatives in urine and serum by liquid chromatography-tandem mass spectrometry. Biomed Chromatogr. 2008 Jan;22(1):73-80. [PubMed Link Image]
Biofluid Urine
Value 2.55 (0.18-5.85) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Lee SH, Suh JW, Chung BC, Kim SO: Polyamine profiles in the urine of patients with leukemia. Cancer Lett. 1998 Jan 9;122(1-2):1-8. [PubMed Link Image]
Biofluid Urine
Value 0.015 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 Link Image]
Biofluid Urine
Value 0.16 (0.02-0.69) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • van den Berg GA, Muskiet FA, Kingma AW, van der Slik W, Halie MR: Simultaneous gas-chromatographic determination of free and acetyl-conjugated polyamines in urine. Clin Chem. 1986 Oct;32(10):1930-7. [PubMed Link Image]
Concentrations (Abnormal)
Biofluid Blood
Value 0.13 +/- 0.13 uM
Age Adult:>18 yrs old
Sex Female
Condition Perillyl alcohol administration for cancer treatment
Comments Not Available
References
  • Byun JA, Lee SH, Jung BH, Choi MH, Moon MH, Chung BC: Analysis of polyamines as carbamoyl derivatives in urine and serum by liquid chromatography-tandem mass spectrometry. Biomed Chromatogr. 2008 Jan;22(1):73-80. [PubMed Link Image]
Biofluid Urine
Value 0.96 (0.12-2.11) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Condition Leukemia
Comments Initial stage of leukemia
References
  • Lee SH, Suh JW, Chung BC, Kim SO: Polyamine profiles in the urine of patients with leukemia. Cancer Lett. 1998 Jan 9;122(1-2):1-8. [PubMed Link Image]
Associated Disorders
Condition References
Leukemia
  • Lee SH, Suh JW, Chung BC, Kim SO: Polyamine profiles in the urine of patients with leukemia. Cancer Lett. 1998 Jan 9;122(1-2):1-8. [PubMed Link Image]
Perillyl alcohol administration for cancer treatment
  • Byun JA, Lee SH, Jung BH, Choi MH, Moon MH, Chung BC: Analysis of polyamines as carbamoyl derivatives in urine and serum by liquid chromatography-tandem mass spectrometry. Biomed Chromatogr. 2008 Jan;22(1):73-80. [PubMed Link Image]
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Beta-Alanine Metabolism SMP00007 Link Image map00410 Link Image
General References
  1. van den Berg GA, Muskiet FA, Kingma AW, van der Slik W, Halie MR: Simultaneous gas-chromatographic determination of free and acetyl-conjugated polyamines in urine. Clin Chem. 1986 Oct;32(10):1930-7. [PubMed Link Image]
  2. Kim KR, Paik MJ, Kim JH, Dong SW, Jeong DH: Rapid gas chromatographic profiling and screening of biologically active amines. J Pharm Biomed Anal. 1997 Jun;15(9-10):1309-18. [PubMed Link Image]
  3. Bremer HJ, Kohne E: The excretion of diamines in human urine. II. Cadaverine, putrescine, 1,3-diaminopropane, 2,2'-dithiobis(ethylamine) and spermidine in urine of patients with cystinuria and cystinlysinuria. Clin Chim Acta. 1971 May;32(3):407-18. [PubMed Link Image]
  4. Fleisher JH, Russell DH: Estimation of urinary diamines and polyamines by thin-layer chromatography. J Chromatogr. 1975 Jul 16;110(2):335-40. [PubMed Link Image]
  5. Blackburn P, Peterson CM: Thiol-disulfide interchange between cystine and N-2-mercaptoethyl-1, 3-diaminopropane as a potential treatment for cystinuria. Anal Biochem. 1984 Jan;136(1):31-8. [PubMed Link Image]
  6. Aigner-Held R, Campbell RA, Daves GD Jr: Polyamine-pyridoxal Schiff bases in urine. Proc Natl Acad Sci U S A. 1979 Dec;76(12):6652-5. [PubMed Link Image]
  7. Somayaji VV, Guay V, Peng Z, Sykes TR, Noujaim AA: Synthesis and evaluation of a new bifunctional chelating agent for the preparation of radioimmunoconjugates. Q J Nucl Med. 1995 Dec;39(4):300-10. [PubMed Link Image]
  8. van den Berg GA, Schaaf JM, Nagel GT, Teelken AW, Muskiet FA: Determination of polyamines and metabolites in cerebrospinal fluid by isotope dilution mass fragmentography, and a clinical application. Clin Chim Acta. 1987 Jun 15;165(2-3):147-54. [PubMed Link Image]
  9. Muskiet FA, van den Berg GA, Kingma AW, Fremouw-Ottevangers DC, Halie MR: Total polyamines and their non-alpha-amino acid metabolites simultaneously determined in urine by capillary gas chromatography, with nitrogen-phosphorus detector; and some clinical applications. Clin Chem. 1984 May;30(5):687-95. [PubMed Link Image]
  10. Lee SH, Suh JW, Chung BC, Kim SO: Polyamine profiles in the urine of patients with leukemia. Cancer Lett. 1998 Jan 9;122(1-2):1-8. [PubMed Link Image]
Metabolic Enzymes
  1. Spermine synthase
  2. Deoxyhypusine synthase
  3. Amiloride-sensitive amine oxidase [copper-containing]
  4. Membrane primary amine oxidase
  5. Retina-specific copper amine oxidase
  6. S-adenosylmethionine decarboxylase proenzyme
  7. Ornithine decarboxylase
  8. cDNA FLJ75710, highly similar to Homo sapiens deoxyhypusine synthase (DHPS), transcript variant 1, mRNA (Deoxyhypusine synthase, isoform CRA_b)
Enzyme 1 [top]
Enzyme 1 ID 5449
Enzyme 1 Name Spermine synthase
Enzyme 1 Synonyms
  1. SPMSY
  2. Spermidine aminopropyltransferase
Enzyme 1 Gene Name SMS
Enzyme 1 Protein Sequence >Spermine synthase
MAAARHSTLDFMLGAKADGETILKGLQSIFQEQGMAESVHTWQDHGYLATYTNKNGSFAN
LRIYPHGLVLLDLQSYDGDAQGKEEIDSILNKVEERMKELSQDSTGRVKRLPPIVRGGAI
DRYWPTADGRLVEYDIDEVVYDEDSPYQNIKILHSKQFGNILILSGDVNLAESDLAYTRA
IMGSGKEDYTGKDVLILGGGDGGILCEIVKLKPKMVTMVEIDQMVIDGCKKYMRKTCGDV
LDNLKGDCYQVLIEDCIPVLKRYAKEGREFDYVINDLTAVPISTSPEEDSTWEFLRLILD
LSMKVLKQDGKYFTQGNCVNLTEALSLYEEQLGRLYCPVEFSKEIVCVPSYLELWVFYTV
WKKAKP
Enzyme 1 Number of Residues 366
Enzyme 1 Molecular Weight 41267.9
Enzyme 1 Theoretical pI 4.62
Enzyme 1 GO Classification
Function
  • catalytic activity
  • spermine synthase activity
  • transferase activity
  • transferase activity, transferring alkyl or aryl (other than methyl) groups
Process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid derivative metabolic process
  • cellular biogenic amine metabolic process
  • cellular metabolic process
  • metabolic process
  • polyamine biosynthetic process
  • polyamine metabolic process
  • spermine biosynthetic process
Component
Enzyme 1 General Function Involved in spermine synthase activity
Enzyme 1 Specific Function Required for normal viability, growth and fertility
Enzyme 1 Pathways
Enzyme 1 Reactions
  • S-adenosylmethioninamine + spermidine = S-methyl-5'-thioadenosine + spermine [RN:R02869]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 2198557 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P52788 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name SPSY_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1101 bp
ATGGCAGCAGCACGGCACAGCACGCTCGACTTCATGCTCGGCGCCAAAGCTGATGGTGAG
ACCATTCTAAAAGGCCTCCAGTCCATTTTCCAGGAGCAGGGGATGGCGGAGTCGGTGCAC
ACCTGGCAGGACCATGGCTATTTAGCAACCTACACAAACAAGAACGGCAGCTTTGCCAAT
TTGAGAATTTACCCACATGGATTGGTGTTGCTGGACCTTCAGAGTTATGATGGTGATGCG
CAAGGCAAAGAAGAGATCGACAGTATTTTGAACAAAGTAGAGGAAAGAATGAAAGAATTG
AGTCAGGACAGTACTGGGCGGGTGAAACGATTACCACCCATAGTGCGAGGAGGAGCCATC
GACAGATACTGGCCCACCGCCGACGGGCGCCTGGTTGAATATGACATAGATGAAGTGGTA
TATGACGAAGATTCACCTTATCAAAATATAAAAATTCTACACTCGAAGCAGTTTGGAAAT
ATTCTCATCCTTAGTGGGGATGTTAATTTGGCAGAGAGTGATTTGGCATATACCCGGGCC
ATCATGGGCAGTGGCAAAGAAGATTACACTGGCAAAGATGTACTCATTCTGGGAGGTGGA
GACGGAGGCATATTGTGTGAAATAGTCAAACTAAAACCAAAGATGGTCACTATGGTAGAG
ATTGACCAAATGGTGATTGATGGGTGTAAGAAATACATGCGAAAAACGTGTGGCGATGTC
TTAGACAATCTTAAAGGAGACTGCTATCAGGTTCTAATAGAAGACTGTATCCCGGTACTG
AAGAGGTACGCCAAAGAAGGGAGAGAATTTGATTATGTGATTAATGATTTGACAGCTGTT
CCAATCTCCACGTCTCCAGAAGAAGATTCCACATGGGAGTTTCTCAGACTGATTCTTGAC
CTCTCAATGAAAGTGTTGAAACAGGATGGGAAATATTTTACACAGGGGAACTGTGTCAAT
CTGACAGAAGCACTGTCGCTCTATGAAGAACAGCTGGGGCGCCTGTATTGTCCTGTGGAA
TTTTCAAAGGAGATCGTCTGTGTCCCTTCATACTTGGAATTGTGGGTATTTTACACTGTT
TGGAAGAAAGCTAAACCCTGA
Enzyme 1 GenBank Gene ID AD001528 Link Image
Enzyme 1 GeneCard ID SMS Link Image
Enzyme 1 GenAtlas ID SMS Link Image
Enzyme 1 HGNC ID HGNC:11123 Link Image
Enzyme 1 Chromosome Location Not Available
Enzyme 1 Locus Not Available
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Korhonen VP, Halmekyto M, Kauppinen L, Myohanen S, Wahlfors J, Keinanen T, Hyvonen T, Alhonen L, Eloranta T, Janne J: Molecular cloning of a cDNA encoding human spermine synthase. DNA Cell Biol. 1995 Oct;14(10):841-7. [PubMed Link Image]
  2. Grieff M, Whyte MP, Thakker RV, Mazzarella R: Sequence analysis of 139 kb in Xp22.1 containing spermine synthase and the 5' region of PEX. Genomics. 1997 Sep 1;44(2):227-31. [PubMed Link Image]
  3. 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 Link Image]
  4. 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 Link Image]
  5. 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 Link Image]
  6. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
  7. Cason AL, Ikeguchi Y, Skinner C, Wood TC, Holden KR, Lubs HA, Martinez F, Simensen RJ, Stevenson RE, Pegg AE, Schwartz CE: X-linked spermine synthase gene (SMS) defect: the first polyamine deficiency syndrome. Eur J Hum Genet. 2003 Dec;11(12):937-44. [PubMed Link Image]
  8. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed Link Image]
  9. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  10. Wu H, Min J, Zeng H, McCloskey DE, Ikeguchi Y, Loppnau P, Michael AJ, Pegg AE, Plotnikov AN: Crystal structure of human spermine synthase: implications of substrate binding and catalytic mechanism. J Biol Chem. 2008 Jun 6;283(23):16135-46. Epub 2008 Mar 26. [PubMed Link Image]
Enzyme 1 Metabolite References
  1. Oredsson SM, Anehus S, Heby O: Reversal of the growth inhibitory effect of alpha-difluoromethylornithine by putrescine but not by other divalent cations. Mol Cell Biochem. 1984 Sep;64(2):163-72. [PubMed Link Image]
Enzyme 2 [top]
Enzyme 2 ID 5451
Enzyme 2 Name Deoxyhypusine synthase
Enzyme 2 Synonyms
  1. DHS
Enzyme 2 Gene Name DHPS
Enzyme 2 Protein Sequence >Deoxyhypusine synthase
MEGSLEREAPAGALAAVLKHSSTLPPESTQVRGYDFNRGVNYRALLEAFGTTGFQATNFG
RAVQQVNAMIEKKLEPLSQDEDQHADLTQSRRPLTSCTIFLGYTSNLISSGIRETIRYLV
QHNMVDVLVTTAGGVEEDLIKCLAPTYLGEFSLRGKELRENGINRIGNLLVPNENYCKFE
DWLMPILDQMVMEQNTEGVKWTPSKMIARLGKEINNPESVYYWAQKNHIPVFSPALTDGS
LGDMIFFHSYKNPGLVLDIVEDLRLINTQAIFAKCTGMIILGGGVVKHHIANANLMRNGA
DYAVYINTAQEFDGSDSGARPDEAVSWGKIRVDAQPVKVYADASLVFPLLVAETFAQKMD
AFMHEKNED
Enzyme 2 Number of Residues 369
Enzyme 2 Molecular Weight 40970.3
Enzyme 2 Theoretical pI 5.02
Enzyme 2 GO Classification
Function
Process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • peptidyl-amino acid modification
  • peptidyl-lysine modification
  • peptidyl-lysine modification to hypusine
  • protein modification process
Component
Enzyme 2 General Function Involved in peptidyl-lysine modification to hypusine
Enzyme 2 Specific Function Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue
Enzyme 2 Pathways Not Available
Enzyme 2 Reactions
  • (1) [eIF5A-precursor]-lysine + spermidine = [eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine [RN:R05329]
  • (2) (1a) spermidine + NAD+ = dehydrospermidine + NADH [RN:R07477]
  • (3) (1b) dehydrospermidine + [enzyme]-lysine = N-(4-aminobutylidene)-[enzyme]-lysine + propane-1,3-diamine [RN:R07479]
  • (4) (1c) N-(4-aminobutylidene)-[enzyme]-lysine + [eIF5A-precursor]-lysine = N-(4-aminobutylidene)-[eIF5A-precursor]-lysine + [enzyme]-lysine [RN:R07480]
  • (5) (1d) N-(4-aminobutylidene)-[eIF5A-precursor]-lysine + NADH + H+ = [eIF5A-precursor]-deoxyhypusine + NAD+ [RN:R07478]
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein Not Available
Enzyme 2 UniProtKB/Swiss-Prot ID P49366 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name DHYS_HUMAN Link Image
Enzyme 2 PDB ID 1RQD Link Image
Enzyme 2 PDB File Show
Enzyme 2 3D Structure
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1110 bp
ATGGAAGGTTCCCTGGAACGGGAGGCGCCAGCGGGGGCGCTGGCCGCCGTGCTAAAGCAC
AGCTCGACGTTGCCGCCCGAAAGCACCCAGGTCCGGGGCTACGACTTCAACCGCGGTGTG
AATTACCGCGCACTGCTGGAGGCCTTCGGCACCACCGGCTTCCAAGCAACCAACTTCGGG
CGCGCTGTACAGCAAGTCAATGCCATGATCGAGAAGAAGCTGGAACCACTGTCACAGGAT
GAAGACCAGCACGCGGACCTGACCCAGAGCCGCCGCCCACTTACCAGCTGCACCATTTTC
CTGGGATATACATCCAACCTCATCAGTTCAGGCATCCGTGAGACCATTCGCTACCTTGTG
CAGCACAACATGGTGGACGTATTGGTGACCACAGCTGGCGGCGTGGAGGAAGACCTCATC
AAGTGCCTGGCGCCCACATACTTGGGCGAGTTTAGCCTCAGGGGGAAGGAGCTCCGGGAG
AACGGGATCAATAGGATCGGAAACCTGCTGGTGCCCAATGAGAATTACTGCAAGTTTGAG
GACTGGCTGATGCCCATTCTGGACCAGATGGTGATGGAGCAGAACACAGAGGGTGTAAAG
TGGACGCCTTCTAAGATGATCGCCCGGCTGGGCAAGGAGATCAACAACCCAGAGTCCGTG
TATTACTGGGCCCAGAAGAACCACATCCCTGTGTTTAGTCCCGCACTTACAGACGGCTCG
CTGGGCGACATGATCTTCTTCCATTCCTACAAGAACCCGGGCCTGGTCCTGGACATCGTT
GAGGACCTGAGGCTCATCAACACACAGGCCATCTTTGCCAAGTGCACTGGGATGATCATT
CTGGGCGGGGGCGTGGTCAAGCACCACATTGCCAATGCCAACCTCATGCGGAACGGGGCC
GACTACGCTGTTTACATCAACACAGCCCAGGAGTTTGATGGCTCTGACTCAGGTGCCCGA
CCAGACGAGGCTGTCTCCTGGGGCAAGATCCGGGTGGATGCACAGCCCGTCAAGGTCTAT
GCTGACGCCTCCCTGGTCTTCCCCCTGCTTGTGGCTGAAACCTTTGCCCAGAAGATGGAT
GCCTTCATGCATGAGAAGAACGAGGACTGA
Enzyme 2 GenBank Gene ID L39068 Link Image
Enzyme 2 GeneCard ID DHPS Link Image
Enzyme 2 GenAtlas ID DHPS Link Image
Enzyme 2 HGNC ID HGNC:2869 Link Image
Enzyme 2 Chromosome Location 1
Enzyme 2 Locus 19p13
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Joe YA, Wolff EC, Park MH: Cloning and expression of human deoxyhypusine synthase cDNA. Structure-function studies with the recombinant enzyme and mutant proteins. J Biol Chem. 1995 Sep 22;270(38):22386-92. [PubMed Link Image]
  2. Bevec D, Kappel B, Jaksche H, Csonga R, Hauber J, Klier H, Steinkasserer A: Molecular characterization of a cDNA encoding functional human deoxyhypusine synthase and chromosomal mapping of the corresponding gene locus. FEBS Lett. 1996 Jan 8;378(2):195-8. [PubMed Link Image]
  3. Yan YP, Tao Y, Chen KY: Molecular cloning and functional expression of human deoxyhypusine synthase cDNA based on expressed sequence tag information. Biochem J. 1996 Apr 15;315 ( Pt 2):429-34. [PubMed Link Image]
  4. Mantuano E, Trettel F, Olsen AS, Lennon G, Frontali M, Jodice C: Localization and genomic structure of human deoxyhypusine synthase gene on chromosome 19p13.2-distal 19p13.1. Gene. 1998 Jul 17;215(1):153-7. [PubMed Link Image]
  5. Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, Ricafrente JY, Wentland MA, Lennon G, Gibbs RA: Large-scale concatenation cDNA sequencing. Genome Res. 1997 Apr;7(4):353-8. [PubMed Link Image]
  6. 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 Link Image]
  7. 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 Link Image]
  8. Klier H, Csonga R, Steinkasserer A, Wohl T, Lottspeich F, Eder J: Purification and characterization of human deoxyhypusine synthase from HeLa cells. FEBS Lett. 1995 May 8;364(2):207-10. [PubMed Link Image]
  9. Joe YA, Wolff EC, Lee YB, Park MH: Enzyme-substrate intermediate at a specific lysine residue is required for deoxyhypusine synthesis. The role of Lys329 in human deoxyhypusine synthase. J Biol Chem. 1997 Dec 19;272(51):32679-85. [PubMed Link Image]
  10. Lee CH, Um PY, Park MH: Structure-function studies of human deoxyhypusine synthase: identification of amino acid residues critical for the binding of spermidine and NAD. Biochem J. 2001 May 1;355(Pt 3):841-9. [PubMed Link Image]
  11. Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6. [PubMed Link Image]
  12. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  13. Liao DI, Wolff EC, Park MH, Davies DR: Crystal structure of the NAD complex of human deoxyhypusine synthase: an enzyme with a ball-and-chain mechanism for blocking the active site. Structure. 1998 Jan 15;6(1):23-32. [PubMed Link Image]
  14. Umland TC, Wolff EC, Park MH, Davies DR: A new crystal structure of deoxyhypusine synthase reveals the configuration of the active enzyme and of an enzyme.NAD.inhibitor ternary complex. J Biol Chem. 2004 Jul 2;279(27):28697-705. Epub 2004 Apr 20. [PubMed Link Image]
Enzyme 2 Metabolite References
  1. Park JH, Wolff EC, Folk JE, Park MH: Reversal of the deoxyhypusine synthesis reaction. Generation of spermidine or homospermidine from deoxyhypusine by deoxyhypusine synthase. J Biol Chem. 2003 Aug 29;278(35):32683-91. Epub 2003 Jun 4. [PubMed Link Image]
Enzyme 3 [top]
Enzyme 3 ID 5627
Enzyme 3 Name Amiloride-sensitive amine oxidase [copper-containing]
Enzyme 3 Synonyms
  1. DAO
  2. Diamine oxidase
  3. Amiloride-binding protein
  4. ABP
  5. Histaminase
  6. Kidney amine oxidase
  7. KAO
Enzyme 3 Gene Name ABP1
Enzyme 3 Protein Sequence >Amiloride-sensitive amine oxidase [copper-containing]
MPALGWAVAAILMLQTAMAEPSPGTLPRKAGVFSDLSNQELKAVHSFLWSKKELRLQPSS
TTTMAKNTVFLIEMLLPKKYHVLRFLDKGERHPVREARAVIFFGDQEHPNVTEFAVGPLP
GPCYMRALSPRPGYQSSWASRPISTAEYALLYHTLQEATKPLHQFFLNTTGFSFQDCHDR
CLAFTDVAPRGVASGQRRSWLIIQRYVEGYFLHPTGLELLVDHGSTDAGHWAVEQVWYNG
KFYGSPEELARKYADGEVDVVVLEDPLPGGKGHDSTEEPPLFSSHKPRGDFPSPIHVSGP
RLVQPHGPRFRLEGNAVLYGGWSFAFRLRSSSGLQVLNVHFGGERIAYEVSVQEAVALYG
GHTPAGMQTKYLDVGWGLGSVTHELAPGIDCPETATFLDTFHYYDADDPVHYPRALCLFE
MPTGVPLRRHFNSNFKGGFNFYAGLKGQVLVLRTTSTVYNYDYIWDFIFYPNGVMEAKMH
ATGYVHATFYTPEGLRHGTRLHTHLIGNIHTHLVHYRVDLDVAGTKNSFQTLQMKLENIT
NPWSPRHRVVQPTLEQTQYSWERQAAFRFKRKLPKYLLFTSPQENPWGHKRTYRLQIHSM
ADQVLPPGWQEEQAITWARYPLAVTKYRESELCSSSIYHQNDPWHPPVVFEQFLHNNENI
ENEDLVAWVTVGFLHIPHSEDIPNTATPGNSVGFLLRPFNFFPEDPSLASRDTVIVWPRD
NGPNYVQRWIPEDRDCSMPPPFSYNGTYRPV
Enzyme 3 Number of Residues 751
Enzyme 3 Molecular Weight 85377.1
Enzyme 3 Theoretical pI 7.10
Enzyme 3 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • cofactor binding
  • copper ion binding
  • ion binding
  • metal ion binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-NH2 group of donors
  • oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor
  • primary amine oxidase activity
  • quinone binding
  • transition metal ion binding
Process
  • amine metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • oxidation reduction
Component
Enzyme 3 General Function Involved in copper ion binding
Enzyme 3 Specific Function Catalyzes the degradation of compounds such as putrescine, histamine, spermine, and spermidine, substances involved in allergic and immune responses, cell proliferation, tissue differentiation, tumor formation, and possibly apoptosis. Placental DAO is thought to play a role in the regulation of the female reproductive function
Enzyme 3 Pathways
Enzyme 3 Reactions
  • histamine + H2O + O2 = (imidazol-4-yl)acetaldehyde + NH3 + H2O2 [RN:R02150]
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • 1-19
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 73486661 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P19801 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name ABP1_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >2256 bp
ATGCCGGCCCTGGGCTGGGCCGTGGCTGCCATCCTGATGCTGCAGACGGCCATGGCGGAG
CCCTCCCCGGGGACTCTGCCCAGGAAGGCAGGGGTGTTTTCAGACCTAAGCAACCAAGAG
CTGAAGGCAGTGCACAGCTTCCTCTGGTCCAAGAAGGAGCTGAGGCTGCAGCCCTCCAGT
ACCACCACCATGGCCAAGAACACCGTGTTTCTCATCGAGATGCTGCTGCCCAAGAAGTAC
CATGTGCTGAGGTTTCTGGATAAAGGTGAAAGGCATCCTGTGCGGGAAGCCCGTGCCGTC
ATCTTCTTTGGTGACCAGGAGCATCCCAATGTCACCGAGTTTGCTGTGGGGCCCCTGCCA
GGGCCCTGCTACATGCGAGCACTGTCCCCCAGGCCTGGGTACCAGTCCTCCTGGGCATCG
AGGCCCATCTCCACAGCAGAGTATGCCCTCCTCTACCACACCCTGCAGGAAGCCACCAAG
CCCCTGCATCAGTTCTTCCTCAATACCACAGGCTTCTCATTCCAAGACTGCCATGACAGA
TGCCTGGCCTTCACCGATGTGGCCCCCCGGGGTGTGGCTTCTGGCCAGCGCCGCAGTTGG
CTTATCATACAGCGCTATGTAGAAGGCTACTTTCTGCACCCCACTGGGCTGGAGCTCCTC
GTGGATCATGGGAGCACAGATGCTGGGCACTGGGCCGTGGAGCAGGTGTGGTACAACGGG
AAGTTCTATGGGAGCCCAGAGGAACTGGCTCGGAAGTATGCAGATGGAGAGGTGGACGTG
GTGGTCCTGGAGGACCCGCTGCCTGGGGGCAAGGGGCATGACAGCACAGAGGAGCCGCCC
CTCTTCTCCTCCCACAAGCCCCGCGGGGACTTCCCCAGCCCCATCCATGTGAGCGGCCCC
CGCTTGGTCCAGCCCCACGGCCCTCGCTTCAGGCTGGAGGGCAACGCTGTGCTCTACGGC
GGCTGGAGCTTTGCCTTCCGGCTGCGCTCCTCCTCCGGGCTGCAGGTCCTGAACGTGCAC
TTCGGCGGAGAGCGCATTGCCTATGAGGTCAGCGTGCAAGAGGCAGTGGCGCTGTATGGA
GGACACACACCTGCAGGCATGCAGACCAAGTACCTCGATGTCGGCTGGGGCCTGGGCAGC
GTCACTCATGAGTTAGCCCCCGGCATCGACTGCCCGGAGACCGCCACCTTCCTGGACACT
TTCCACTACTATGATGCCGATGACCCGGTCCATTATCCCCGAGCCCTCTGCCTCTTTGAA
ATGCCCACAGGGGTGCCCCTTCGGCGGCACTTTAATTCCAACTTTAAAGGTGGCTTCAAC
TTCTATGCGGGGCTGAAGGGCCAGGTGCTGGTGCTGCGGACAACTTCAACTGTCTACAAT
TATGATTACATTTGGGACTTTATCTTCTACCCCAACGGGGTGATGGAGGCCAAGATGCAT
GCCACTGGCTACGTCCACGCCACCTTCTACACCCCCGAGGGGCTGCGCCACGGCACTCGC
CTGCACACCCACCTGATTGGCAACATACACACTCACTTGGTGCACTACCGCGTAGACCTG
GATGTGGCAGGCACCAAGAACAGCTTCCAGACACTGCAGATGAAGCTAGAAAACATCACC
AACCCCTGGAGCCCAAGACACCGCGTGGTCCAGCCAACTCTGGAGCAGACGCAGTACTCC
TGGGAGCGCCAGGCGGCCTTCCGCTTCAAAAGGAAGCTGCCTAAGTACCTGCTCTTTACC
AGCCCCCAGGAGAACCCCTGGGGCCACAAGCGCACGTACCGCCTGCAGATCCACTCCATG
GCCGACCAGGTGCTGCCCCCAGGCTGGCAGGAGGAGCAGGCCATCACCTGGGCAAGGTAC
CCCCTGGCAGTGACCAAGTACCGGGAGTCGGAGCTGTGCAGCAGCAGCATCTACCACCAG
AACGACCCCTGGCACCCGCCCGTGGTCTTTGAGCAGTTTCTTCACAACAACGAGAACATT
GAAAATGAGGACCTGGTGGCCTGGGTGACGGTGGGCTTCCTGCACATCCCCCACTCAGAG
GACATTCCCAACACAGCCACACCTGGGAACTCCGTGGGCTTCCTGCTCCGGCCATTCAAC
TTCTTCCCAGAGGACCCCTCCCTGGCATCCAGAGACACTGTGATCGTGTGGCCTCGGGAC
AACGGCCCCAACTACGTCCAGCGCTGGATCCCTGAGGACAGGGACTGCTCGATGCCTCCC
CCTTTTAGCTACAATGGGACCTATAGACCTGTGTGA
Enzyme 3 GenBank Gene ID NM_001091.2 Link Image
Enzyme 3 GeneCard ID ABP1 Link Image
Enzyme 3 GenAtlas ID ABP1 Link Image
Enzyme 3 HGNC ID HGNC:80 Link Image
Enzyme 3 Chromosome Location 7
Enzyme 3 Locus 7q34-q36
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Barbry P, Champe M, Chassande O, Munemitsu S, Champigny G, Lingueglia E, Maes P, Frelin C, Tartar A, Ullrich A, et al.: Human kidney amiloride-binding protein: cDNA structure and functional expression. Proc Natl Acad Sci U S A. 1990 Oct;87(19):7347-51. [PubMed Link Image]
  2. Chassande O, Renard S, Barbry P, Lazdunski M: The human gene for diamine oxidase, an amiloride binding protein. Molecular cloning, sequencing, and characterization of the promoter. J Biol Chem. 1994 May 20;269(20):14484-9. [PubMed Link Image]
  3. Zhang X, Kim J, McIntire WS: cDNA sequences of variant forms of human placenta diamine oxidase. Biochem Genet. 1995 Aug;33(7-8):261-8. [PubMed Link Image]
  4. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed Link Image]
  5. 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 Link Image]
  6. Novotny WF, Chassande O, Baker M, Lazdunski M, Barbry P: Diamine oxidase is the amiloride-binding protein and is inhibited by amiloride analogues. J Biol Chem. 1994 Apr 1;269(13):9921-5. [PubMed Link Image]
Enzyme 3 Metabolite References
  1. 6790686;3085656
Enzyme 4 [top]
Enzyme 4 ID 5630
Enzyme 4 Name Membrane primary amine oxidase
Enzyme 4 Synonyms
  1. Copper amine oxidase
  2. HPAO
  3. Semicarbazide-sensitive amine oxidase
  4. SSAO
  5. Vascular adhesion protein 1
  6. VAP-1
Enzyme 4 Gene Name AOC3
Enzyme 4 Protein Sequence >Membrane primary amine oxidase
MNQKTILVLLILAVITIFALVCVLLVGRGGDGGEPSQLPHCPSVSPSAQPWTHPGQSQLF
ADLSREELTAVMRFLTQRLGPGLVDAAQARPSDNCVFSVELQLPPKAAALAHLDRGSPPP
AREALAIVFFGRQPQPNVSELVVGPLPHPSYMRDVTVERHGGPLPYHRRPVLFQEYLDID
QMIFNRELPQASGLLHHCCFYKHRGRNLVTMTTAPRGLQSGDRATWFGLYYNISGAGFFL
HHVGLELLVNHKALDPARWTIQKVFYQGRYYDSLAQLEAQFEAGLVNVVLIPDNGTGGSW
SLKSPVPPGPAPPLQFYPQGPRFSVQGSRVASSLWTFSFGLGAFSGPRIFDVRFQGERLV
YEISLQEALAIYGGNSPAAMTTRYVDGGFGMGKYTTPLTRGVDCPYLATYVDWHFLLESQ
APKTIRDAFCVFEQNQGLPLRRHHSDLYSHYFGGLAETVLVVRSMSTLLNYDYVWDTVFH
PSGAIEIRFYATGYISSAFLFGATGKYGNQVSEHTLGTVHTHSAHFKVDLDVAGLENWVW
AEDMVFVPMAVPWSPEHQLQRLQVTRKLLEMEEQAAFLVGSATPRYLYLASNHSNKWGHP
RGYRIQMLSFAGEPLPQNSSMARGFSWERYQLAVTQRKEEEPSSSSVFNQNDPWAPTVDF
SDFINNETIAGKDLVAWVTAGFLHIPHAEDIPNTVTVGNGVGFFLRPYNFFDEDPSFYSA
DSIYFRGDQDAGACEVNPLACLPQAAACAPDLPAFSHGGFSHN
Enzyme 4 Number of Residues 763
Enzyme 4 Molecular Weight 84621.3
Enzyme 4 Theoretical pI 6.51
Enzyme 4 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • cofactor binding
  • copper ion binding
  • ion binding
  • metal ion binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-NH2 group of donors
  • oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor
  • primary amine oxidase activity
  • quinone binding
  • transition metal ion binding
Process
  • amine metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • oxidation reduction
Component
Enzyme 4 General Function Involved in copper ion binding
Enzyme 4 Specific Function Cell adhesion protein that participates in lymphocyte recirculation by mediating the binding of lymphocytes to peripheral lymph node vascular endothelial cells in an L-selectin- independent fashion. Has a monoamine oxidase activity. May play a role in adipogenesis
Enzyme 4 Pathways
Enzyme 4 Reactions
  • RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2 [RN:R01853]
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • 6-26
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein Not Available
Enzyme 4 UniProtKB/Swiss-Prot ID Q16853 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name AOC3_HUMAN Link Image
Enzyme 4 PDB ID 1PU4 Link Image
Enzyme 4 PDB File Show
Enzyme 4 3D Structure
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >2292 bp
ATGAACCAGAAGACAATCCTCGTGCTCCTCATTCTGGCCGTCATCACCATCTTTGCCTTG
GTTTGTGTCCTGCTGGTGGGCAGGGGTGGAGATGGGGGTGAACCCAGCCAGCTTCCCCAT
TGCCCCTCTGTATCTCCCAGTGCCCAGCCTTGGACACACCCTGGCCAGAGCCAGCTGTTT
GCAGACCTGAGCCGAGAGGAGCTGACGGCTGTGATGCGCTTTCTGACCCAGCGGCTGGGG
CCAGGGCTGGTGGATGCAGCCCAGGCCCGGCCCTCGGACAACTGTGTCTTCTCAGTGGAG
TTGCAGCTGCCTCCCAAGGCTGCAGCCCTGGCTCACTTGGACAGGGGGAGCCCCCCACCT
GCCCGGGAGGCACTGGCCATCGTCTTCTTTGGCAGGCAACCCCAGCCCAACGTGAGTGAG
CTGGTGGTGGGGCCACTGCCTCACCCCTCCTACATGCGGGACGTGACTGTGGAGCGTCAT
GGAGGCCCCCTGCCCTATCACCGACGCCCCGTGCTGTTCCAAGAGTACCTGGACATAGAC
CAGATGATCTTCAACAGAGAGCTGCCCCAGGCTTCTGGGCTTCTCCACCACTGTTGCTTC
TACAAGCACCGGGGACGGAACCTGGTGACAATGACCACGGCTCCCCGTGGTCTGCAATCA
GGGGACCGGGCCACCTGGTTTGGCCTCTACTACAACATCTCGGGCGCTGGGTTCTTCCTG
CACCACGTGGGCTTGGAGCTGCTAGTGAACCACAAGGCCCTTGACCCTGCCCGCTGGACT
ATCCAGAAGGTGTTCTATCAAGGCCGCTACTACGACAGCCTGGCCCAGCTGGAGGCCCAG
TTTGAGGCCGGCCTGGTGAATGTGGTGCTGATCCCAGACAATGGCACAGGTGGGTCCTGG
TCCCTGAAGTCCCCTGTGCCCCCGGGTCCAGCTCCCCCTCTACAGTTCTATCCCCAAGGC
CCCCGCTTCAGTGTCCAGGGAAGTCGAGTGGCCTCCTCACTGTGGACTTTCTCCTTTGGC
CTCGGAGCATTCAGTGGCCCAAGGATCTTTGACGTTCGCTTCCAAGGAGAAAGACTAGTT
TATGAGATAAGCCTCCAAGAGGCCTTGGCCATCTATGGTGGAAATTCCCCAGCAGCAATG
ACGACCCGCTATGTGGATGGAGGCTTTGGCATGGGCAAGTACACCACGCCCCTGACCCGT
GGGGTGGACTGCCCCTACTTGGCCACCTACGTGGACTGGCACTTCCTTTTGGAGTCCCAG
GCCCCCAAGACAATACGTGATGCCTTTTGTGTGTTTGAACAGAACCAGGGCCTCCCCCTG
CGGCGACACCACTCAGATCTCTACTCGCACTACTTTGGGGGTCTTGCGGAAACGGTGCTG
GTCGTCAGATCTATGTCCACCTTGCTCAACTATGACTATGTGTGGGATACGGTCTTCCAC
CCCAGTGGGGCCATAGAAATACGATTCTATGCCACGGGCTACATCAGCTCGGCATTCCTC
TTTGGTGCTACTGGGAAGTACGGGAACCAAGTGTCAGAGCACACCCTGGGCACGGTCCAC
ACCCACAGCGCCCACTTCAAGGTGGATCTGGATGTAGCAGGACTGGAGAACTGGGTCTGG
GCCGAGGATATGGTCTTTGTCCCCATGGCTGTGCCCTGGAGCCCTGAGCACCAGCTGCAG
AGGCTGCAGGTGACCCGGAAGCTGCTGGAGATGGAGGAGCAGGCCGCCTTCCTCGTGGGA
AGCGCCACCCCTCGCTACCTGTACCTGGCCAGCAACCACAGCAACAAGTGGGGTCACCCC
CGGGGCTACCGCATCCAGATGCTCAGCTTTGCTGGAGAGCCGCTGCCCCAAAACAGCTCC
ATGGCGAGAGGCTTCAGCTGGGAGAGGTACCAGCTGGCTGTGACCCAGCGGAAGGAGGAG
GAGCCCAGTAGCAGCAGCGTTTTCAATCAGAATGACCCTTGGGCCCCCACTGTGGATTTC
AGTGACTTCATCAACAATGAGACCATTGCTGGAAAGGATTTGGTGGCCTGGGTGACAGCT
GGTTTTCTGCATATCCCACATGCAGAGGACATTCCTAACACAGTGACTGTGGGGAACGGC
GTGGGCTTCTTCCTCCGACCCTATAACTTCTTTGACGAAGACCCCTCCTTCTACTCTGCC
GACTCCATCTACTTCCGAGGGGACCAGGATGCTGGGGCCTGCGAGGTCAACCCCCTAGCT
TGCCTGCCCCAGGCTGCTGCCTGTGCCCCCGACCTCCCTGCCTTCTCCCACGGGGGCTTC
TCTCACAACTAG
Enzyme 4 GenBank Gene ID U39447 Link Image
Enzyme 4 GeneCard ID AOC3 Link Image
Enzyme 4 GenAtlas ID AOC3 Link Image
Enzyme 4 HGNC ID HGNC:550 Link Image
Enzyme 4 Chromosome Location 1
Enzyme 4 Locus 17q21
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Zhang X, McIntire WS: Cloning and sequencing of a copper-containing, topa quinone-containing monoamine oxidase from human placenta. Gene. 1996 Nov 14;179(2):279-86. [PubMed Link Image]
  2. Smith DJ, Salmi M, Bono P, Hellman J, Leu T, Jalkanen S: Cloning of vascular adhesion protein 1 reveals a novel multifunctional adhesion molecule. J Exp Med. 1998 Jul 6;188(1):17-27. [PubMed Link Image]
  3. Zhang Q, Mashima Y, Noda S, Imamura Y, Kudoh J, Shimizu N, Nishiyama T, Umeda S, Oguchi Y, Tanaka Y, Iwata T: Characterization of AOC2 gene encoding a copper-binding amine oxidase expressed specifically in retina. Gene. 2003 Oct 30;318:45-53. [PubMed Link Image]
  4. 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 Link Image]
  5. 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 Link Image]
  6. Aboulaich N, Vainonen JP, Stralfors P, Vener AV: Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes. Biochem J. 2004 Oct 15;383(Pt 2):237-48. [PubMed Link Image]
  7. Liu T, Qian WJ, Gritsenko MA, Camp DG 2nd, Monroe ME, Moore RJ, Smith RD: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res. 2005 Nov-Dec;4(6):2070-80. [PubMed Link Image]
  8. Bour S, Daviaud D, Gres S, Lefort C, Prevot D, Zorzano A, Wabitsch M, Saulnier-Blache JS, Valet P, Carpene C: Adipogenesis-related increase of semicarbazide-sensitive amine oxidase and monoamine oxidase in human adipocytes. Biochimie. 2007 Aug;89(8):916-25. Epub 2007 Feb 24. [PubMed Link Image]
  9. Kaitaniemi S, Elovaara H, Gron K, Kidron H, Liukkonen J, Salminen T, Salmi M, Jalkanen S, Elima K: The unique substrate specificity of human AOC2, a semicarbazide-sensitive amine oxidase. Cell Mol Life Sci. 2009 Aug;66(16):2743-57. Epub 2009 Jul 9. [PubMed Link Image]
  10. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed Link Image]
  11. Airenne TT, Nymalm Y, Kidron H, Smith DJ, Pihlavisto M, Salmi M, Jalkanen S, Johnson MS, Salminen TA: Crystal structure of the human vascular adhesion protein-1: unique structural features with functional implications. Protein Sci. 2005 Aug;14(8):1964-74. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5631
Enzyme 5 Name Retina-specific copper amine oxidase
Enzyme 5 Synonyms
  1. RAO
  2. Amine oxidase [copper-containing]
  3. Semicarbazide-sensitive amine oxidase
  4. SSAO
Enzyme 5 Gene Name AOC2
Enzyme 5 Protein Sequence >Retina-specific copper amine oxidase
MHLKIVLAFLALSLITIFALAYVLLTSPGGSSQPPHCPSVSHRAQPWPHPGQSQLFADLS
REELTAVMRFLTQRLGPGLVDAAQAQPSDNCIFSVELQLPPKAAALAHLDRGSPPPAREA
LAIVLFGGQPQPNVSELVVGPLPHPSYMRDVTVERHGGPLPYHRRPVLRAEFTQMWRHLK
EVELPKAPIFLSSTFNYNGSTLAAVHATPRGLRSGDRATWMALYHNISGVGLFLHPVGLE
LLLDHRALDPAHWTVQQVFYLGHYYADLGQLEREFKSGRLEVVRVPLPPPNGASSLRSRN
SPGPLPPLQFSPQGSQYSVQGNLVVSSLWSFTFGHGVFSGLRIFDVRFQGERIAYEVSVQ
ECVSIYGADSPKTMLTRYLDSSFGLGRNSRGLVRGVDCPYQATMVDIHILVGKGAVQLLP
GAVCVFEEAQGLPLRRHHNYLQNHFYGGLASSALVVRSVSSVGNYDYIWDFVLYPNGALE
GRVHATGYINTAFLKGGEEGLLFGNRVGERVLGTVHTHAFHFKLDLDVAGLKNWVVAEDV
VFKPVAAPWNPEHWLQRPQLTRQVLGKEDLTAFSLGSPLPRYLYLASNQTNAWGHQRGYR
IQIHSPLGIHIPLESDMERALSWGRYQLVVTQRKEEESQSSSIYHQNDIWTPTVTFADFI
NNETLLGEDLVAWVTASFLHIPHAEDIPNTVTLGNRVGFLLRPYNFFDEDPSIFSPGSVY
FEKGQDAGLCSINPVACLPDLAACVPDLPPFSYHGF
Enzyme 5 Number of Residues 756
Enzyme 5 Molecular Weight 83672.7
Enzyme 5 Theoretical pI 7.03
Enzyme 5 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • cofactor binding
  • copper ion binding
  • ion binding
  • metal ion binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-NH2 group of donors
  • oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor
  • primary amine oxidase activity
  • quinone binding
  • transition metal ion binding
Process
  • amine metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • oxidation reduction
Component
Enzyme 5 General Function Involved in copper ion binding
Enzyme 5 Specific Function Has a monoamine oxidase activity with substrate specificity for 2-phenylethylamine and tryptamine. May play a role in adipogenesis. May be a critical modulator of signal transmission in retina
Enzyme 5 Pathways
Enzyme 5 Reactions
  • RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2 [RN:R01853]
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • 1-32
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 3510335 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID O75106 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name AOC2_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >2271 bp
ATGCATCTCAAGATAGTCCTGGCGTTCCTGGCACTGTCCCTCATTACCATCTTTGCCCTG
GCCTATGTTTTGCTGACCAGCCCAGGTGGTTCCAGCCAGCCTCCCCACTGCCCCTCTGTA
TCCCATAGGGCCCAGCCCTGGCCACACCCTGGCCAGAGCCAGCTGTTTGCAGACCTGAGC
CGAGAGGAGTTGACAGCTGTGATGCGCTTTCTGACCCAGCGGCTGGGGCCAGGGCTGGTG
GACGCAGCCCAGGCTCAGCCCTCGGACAACTGCATCTTCTCAGTGGAGCTGCAGCTGCCC
CCCAAGGCTGCAGCCCTGGCCCACCTGGACAGGGGGAGCCCCCCACCTGCCCGGGAGGCA
CTGGCCATCGTCCTCTTTGGTGGACAACCCCAACCCAATGTGAGTGAGCTGGTGGTGGGG
CCGCTGCCTCACCCCTCGTACATGCGGGATGTGACTGTGGAGCGTCACGGCGGGCCCCTG
CCCTATCACCGTCGCCCGGTGCTGAGAGCTGAGTTTACACAGATGTGGAGGCATCTGAAA
GATGTGGAGCTACCCAAGGCACCCATCTTCCTGTCGTCCACCTTCAACTACAATGGCTCT
ACCCTGGCAGCTGTGCATGCCACCCCTCGGGGCTTGCGCTCAAGGGAACGAACTACCTGG
ATGGCCCTCTACCATAACATCTCAGGGGTTGGTCTTTTCCTTCACCCCGTGGGGCTGGAG
CTACTACTGGACCACAGGGCCCTGGACCCTGCCCACTGGACTGTCCAGCAGGTCTTCTAC
CTTGGGCACTACTATGCAGACTTGGGCCAGTTGGAACGGGAGTTTAAGTCTGGCCGGTTG
GAAGTGGTTAGAGTCCCTCTACCTCCACCAAATGGAGCTTCATCCCTGAGGTCTCGGAAC
TCTCCAGGTCCTCTTCCCCCTCTTCAGTTCTCGCCCCAGGGTTCCCAGTACAGTGTGCAA
GGAAACCTGGTGGTATCCTCCCTCTGGTCATTTACCTTTGGCCATGGGGTGTTCAGCGGC
CTGAGGATTTTTGATGTTCGGTTCCAGGGTGAGCGAATAGCCTATGAAGTCAGTGTCCAG
GAGTGTGTATCTATCTATGGTGCCGATTCACCCAAGACGATGCTGACTCGCTATTTGGAT
AGCAGCTTTGGACTCGGCCGTAACAGCCGAGGCTTGGTGCGGGGAGTGGACTGCCCCTAT
CAAGCCACGATGGTGGACATCCATATATTAGTGGGCAAAGGGGCAGTCCAGCTGCTTCCA
GGGGCTGTGTGTGTATTTGAGGAAGCCCAGGGACTGCCCCTTCGAAGGCACCACAATTAC
CTTCAAAATCATTTCTATGGTGGTTTGGCCAGCTCAGCCCTTGTGGTCAGGTCTGTGTCA
TCTGTGGGCAACTATGACTACATTTGGGACTTTGTGTTGTACCCAAATGGGGCACTTGAA
GGGCGGGTCCATGCCACGGGTTATATCAACACAGCTTTCCTGAAAGGGGGAGAGGAGGGC
CTCCTCTTTGGGAACCGTGTGGGGGAAAGAGTGCTGGGAACGGTGCACACACATGCCTTC
CACTTCAAGCTGGACCTGGATGTGGCAGGGCTGAAAAACTGGGTGGTAGCTGAAGACGTG
GTGTTTAAACCTGTGGCTGCCCCCTGGAACCCGGAGCACTGGCTACAGCGCCCACAGCTG
ACTCGGCAGGTCCTGGGAAAGGAGGACCTGACAGCTTTTTCCTTGGGAAGCCCCCTACCC
CGCTACCTCTACCTGGCTAGCAACCAGACTAATGCGTGGGGTCACCAGCGCGGGTACCGA
ATCCAGATCCACAGCCCCCTTGGCATACAAATACCCCTGGAGAGTGACATGGAGAGGGCC
CTCAGCTGGGGGAGATACCAGCTTGTGGTGACCCAGAGAAAGGAGGAGGAGTCACAGAGC
AGTAGCATCTATCACCAGAATGACATCTGGACACCCACAGTTACCTTTGCTGACTTCATC
AACAATGAAACCCTCTTAGGAGAGGATCTGGTGGCTTGGGTCACAGCCAGCTTCCTGCAC
ATTCCCCATGCCGAGGACATCCCAAACACAGTGACTCTGGGGAACAGAGTTGGCTTCTTG
CTCCGACCCTATAACTTCTTTGATGAGGACCCCTCCATCTTCTCCCCTGGCAGTGTGTAC
TTTGAGAAGGGCCAGGATGCTGGGCTCTGCAGCATCAATCCTGTGGCCTGCCTCCCCGAC
CTGGCAGCCTGTGTCCCGGACTTACCCCCTTTCTCTTACCACGGCTTCTAG
Enzyme 5 GenBank Gene ID AB012943 Link Image
Enzyme 5 GeneCard ID AOC2 Link Image
Enzyme 5 GenAtlas ID AOC2 Link Image
Enzyme 5 HGNC ID HGNC:549 Link Image
Enzyme 5 Chromosome Location 1
Enzyme 5 Locus 17q21
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Imamura Y, Kubota R, Wang Y, Asakawa S, Kudoh J, Mashima Y, Oguchi Y, Shimizu N: Human retina-specific amine oxidase (RAO): cDNA cloning, tissue expression, and chromosomal mapping. Genomics. 1997 Mar 1;40(2):277-83. [PubMed Link Image]
  2. Imamura Y, Noda S, Mashima Y, Kudoh J, Oguchi Y, Shimizu N: Human retina-specific amine oxidase: genomic structure of the gene (AOC2), alternatively spliced variant, and mRNA expression in retina. Genomics. 1998 Jul 15;51(2):293-8. [PubMed Link Image]
  3. Zody MC, Garber M, Adams DJ, Sharpe T, Harrow J, Lupski JR, Nicholson C, Searle SM, Wilming L, Young SK, Abouelleil A, Allen NR, Bi W, Bloom T, Borowsky ML, Bugalter BE, Butler J, Chang JL, Chen CK, Cook A, Corum B, Cuomo CA, de Jong PJ, DeCaprio D, Dewar K, FitzGerald M, Gilbert J, Gibson R, Gnerre S, Goldstein S, Grafham DV, Grocock R, Hafez N, Hagopian DS, Hart E, Norman CH, Humphray S, Jaffe DB, Jones M, Kamal M, Khodiyar VK, LaButti K, Laird G, Lehoczky J, Liu X, Lokyitsang T, Loveland J, Lui A, Macdonald P, Major JE, Matthews L, Mauceli E, McCarroll SA, Mihalev AH, Mudge J, Nguyen C, Nicol R, O'Leary SB, Osoegawa K, Schwartz DC, Shaw-Smith C, Stankiewicz P, Steward C, Swarbreck D, Venkataraman V, Whittaker CA, Yang X, Zimmer AR, Bradley A, Hubbard T, Birren BW, Rogers J, Lander ES, Nusbaum C: DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage. Nature. 2006 Apr 20;440(7087):1045-9. [PubMed Link Image]
  4. 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 Link Image]
  5. Heniquez A, Meissonnier G, Visentin V, Prevot D, Carpene C: High expression of semicarbazide-sensitive amine oxidase genes AOC2 and AOC3, but not the diamine oxidase gene AOC1 in human adipocytes. Inflamm Res. 2003 Apr;52 Suppl 1:S74-5. [PubMed Link Image]
  6. Bour S, Daviaud D, Gres S, Lefort C, Prevot D, Zorzano A, Wabitsch M, Saulnier-Blache JS, Valet P, Carpene C: Adipogenesis-related increase of semicarbazide-sensitive amine oxidase and monoamine oxidase in human adipocytes. Biochimie. 2007 Aug;89(8):916-25. Epub 2007 Feb 24. [PubMed Link Image]
  7. Kaitaniemi S, Elovaara H, Gron K, Kidron H, Liukkonen J, Salminen T, Salmi M, Jalkanen S, Elima K: The unique substrate specificity of human AOC2, a semicarbazide-sensitive amine oxidase. Cell Mol Life Sci. 2009 Aug;66(16):2743-57. Epub 2009 Jul 9. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5657
Enzyme 6 Name S-adenosylmethionine decarboxylase proenzyme
Enzyme 6 Synonyms
  1. AdoMetDC
  2. SAMDC
  3. S-adenosylmethionine decarboxylase alpha chain
  4. S-adenosylmethionine decarboxylase beta chain
Enzyme 6 Gene Name AMD1
Enzyme 6 Protein Sequence >S-adenosylmethionine decarboxylase proenzyme
MEAAHFFEGTEKLLEVWFSRQQPDANQGSGDLRTIPRSEWDILLKDVQCSIISVTKTDKQ
EAYVLSESSMFVSKRRFILKTCGTTLLLKALVPLLKLARDYSGFDSIQSFFYSRKNFMKP
SHQGYPHRNFQEEIEFLNAIFPNGAAYCMGRMNSDCWYLYTLDFPESRVISQPDQTLEIL
MSELDPAVMDQFYMKDGVTAKDVTRESGIRDLIPGSVIDATMFNPCGYSMNGMKSDGTYW
TIHITPEPEFSYVSFETNLSQTSYDDLIRKVVEVFKPGKFVTTLFVNQSSKCRTVLASPQ
KIEGFKRLDCQSAMFNDYNFVFTSFAKKQQQQQS
Enzyme 6 Number of Residues 334
Enzyme 6 Molecular Weight 38339.3
Enzyme 6 Theoretical pI 5.78
Enzyme 6 GO Classification
Function
  • adenosylmethionine decarboxylase activity
  • carbon-carbon lyase activity
  • carboxy-lyase activity
  • catalytic activity
  • lyase activity
Process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid derivative metabolic process
  • cellular biogenic amine metabolic process
  • cellular metabolic process
  • metabolic process
  • polyamine biosynthetic process
  • polyamine metabolic process
  • spermidine biosynthetic process
  • spermine biosynthetic process
Component
Enzyme 6 General Function Involved in adenosylmethionine decarboxylase activity
Enzyme 6 Specific Function S-adenosyl-L-methionine = (5-deoxy-5- adenosyl)(3-aminopropyl)-methylsulfonium salt + CO(2)
Enzyme 6 Pathways
Enzyme 6 Reactions
  • S-adenosyl-L-methionine = (5-deoxy-5-adenosyl)(3-aminopropyl)methylsulfonium salt + CO2 [RN:R00178]
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 55664717 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID P17707 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name DCAM_HUMAN Link Image
Enzyme 6 PDB ID 1MSV Link Image
Enzyme 6 PDB File Show
Enzyme 6 3D Structure
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >1005 bp
ATGGAAGCTGCACATTTTTTCGAAGGGACCGAGAAGCTGCTGGAGGTTTGGTTCTCCCGG
CAGCAGCCCGACGCAAACCAAGGATCTGGGGATCTTCGCACTATCCCAAGATCTGAGTGG
GACATACTTTTGAAGGATGTGCAATGTTCAATCATAAGTGTGACAAAAACTGACAAGCAG
GAAGCTTATGTACTCAGTGAGAGTAGCATGTTTGTCTCCAAGAGACGTTTCATTTTGAAG
ACATGTGGTACCACCCTCTTGCTGAAAGCACTGGTTCCCCTGTTGAAGCTTGCTAGGGAT
TACAGTGGGTTTGACTCAATTCAAAGCTTCTTTTATTCTCGTAAGAATTTCATGAAGCCT
TCTCACCAAGGGTACCCACACCGGAATTTCCAGGAAGAAATAGAGTTTCTTAATGCAATT
TTCCCAAATGGAGCAGCATATTGTATGGGACGTATGAATTCTGACTGTTGGTACTTATAT
ACTCTGGATTTCCCAGAGAGTCGGGTAATCAGTCAGCCAGATCAAACCTTGGAAATTCTG
ATGAGTGAGCTTGACCCAGCAGTTATGGACCAGTTCTACATGAAAGATGGTGTTACTGCA
AAGGATGTCACTCGTGAGAGTGGAATTCGTGACCTGATACCAGGTTCTGTCATTGATGCC
ACAATGTTCAATCCTTGTGGGTATTCGATGAATGGAATGAAATCGGATGGAACTTATTGG
ACTATTCACATCACTCCAGAACCAGAATTTTCTTATGTTAGCTTTGAAACAAACTTAAGT
CAGACCTCCTATGATGACCTGATCAGGAAAGTTGTAGAAGTCTTCAAGCCAGGAAAATTT
GTGACCACCTTGTTTGTTAATCAGAGTTCTAAATGTCGCACAGTGCTTGCTTCGCCCCAG
AAGATTGAAGGTTTTAAGCGTCTTGATTGCCAGAGTGCTATGTTCAATGATTACAATTTT
GTTTTTACCAGTTTTGCTAAGAAGCAGCAACAACAGCAGAGTTGA
Enzyme 6 GenBank Gene ID AL357515 Link Image
Enzyme 6 GeneCard ID AMD1 Link Image
Enzyme 6 GenAtlas ID AMD1 Link Image
Enzyme 6 HGNC ID HGNC:457 Link Image
Enzyme 6 Chromosome Location 6
Enzyme 6 Locus 6q21
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Pajunen A, Crozat A, Janne OA, Ihalainen R, Laitinen PH, Stanley B, Madhubala R, Pegg AE: Structure and regulation of mammalian S-adenosylmethionine decarboxylase. J Biol Chem. 1988 Nov 15;263(32):17040-9. [PubMed Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
  4. Stanley BA, Pegg AE: Amino acid residues necessary for putrescine stimulation of human S-adenosylmethionine decarboxylase proenzyme processing and catalytic activity. J Biol Chem. 1991 Oct 5;266(28):18502-6. [PubMed Link Image]
  5. Xiong H, Pegg AE: Mechanistic studies of the processing of human S-adenosylmethionine decarboxylase proenzyme. Isolation of an ester intermediate. J Biol Chem. 1999 Dec 3;274(49):35059-66. [PubMed Link Image]
  6. Xiong H, Stanley BA, Pegg AE: Role of cysteine-82 in the catalytic mechanism of human S-adenosylmethionine decarboxylase. Biochemistry. 1999 Feb 23;38(8):2462-70. [PubMed Link Image]
  7. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  8. Ekstrom JL, Mathews II, Stanley BA, Pegg AE, Ealick SE: The crystal structure of human S-adenosylmethionine decarboxylase at 2.25 A resolution reveals a novel fold. Structure. 1999 May;7(5):583-95. [PubMed Link Image]
  9. Tolbert WD, Ekstrom JL, Mathews II, Secrist JA 3rd, Kapoor P, Pegg AE, Ealick SE: The structural basis for substrate specificity and inhibition of human S-adenosylmethionine decarboxylase. Biochemistry. 2001 Aug 14;40(32):9484-94. [PubMed Link Image]
Enzyme 6 Metabolite References
  1. Pegg AE, Shuttleworth K, Hibasami H: Specificity of mammalian spermidine synthase and spermine synthase. Biochem J. 1981 Aug 1;197(2):315-20. [PubMed Link Image]
Enzyme 7 [top]
Enzyme 7 ID 6322
Enzyme 7 Name Ornithine decarboxylase
Enzyme 7 Synonyms
  1. ODC
Enzyme 7 Gene Name ODC1
Enzyme 7 Protein Sequence >Ornithine decarboxylase
MNNFGNEEFDCHFLDEGFTAKDILDQKINEVSSSDDKDAFYVADLGDILKKHLRWLKALP
RVTPFYAVKCNDSKAIVKTLAATGTGFDCASKTEIQLVQSLGVPPERIIYANPCKQVSQI
KYAANNGVQMMTFDSEVELMKVARAHPKAKLVLRIATDDSKAVCRLSVKFGATLRTSRLL
LERAKELNIDVVGVSFHVGSGCTDPETFVQAISDARCVFDMGAEVGFSMYLLDIGGGFPG
SEDVKLKFEEITGVINPALDKYFPSDSGVRIIAEPGRYYVASAFTLAVNIIAKKIVLKEQ
TGSDDEDESSEQTFMYYVNDGVYGSFNCILYDHAHVKPLLQKRPKPDEKYYSSSIWGPTC
DGLDRIVERCDLPEMHVGDWMLFENMGAYTVAAASTFNGFQRPTIYYVMSGPAWQLMQQF
QNPDFPPEVEEQDASTLPVSCAWESGMKRHRAACASASINV
Enzyme 7 Number of Residues 461
Enzyme 7 Molecular Weight 51147.7
Enzyme 7 Theoretical pI 4.88
Enzyme 7 GO Classification
Function
  • catalytic activity
Process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid derivative metabolic process
  • cellular biogenic amine metabolic process
  • cellular metabolic process
  • metabolic process
  • polyamine biosynthetic process
  • polyamine metabolic process
Component
Enzyme 7 General Function Involved in catalytic activity
Enzyme 7 Specific Function L-ornithine = putrescine + CO(2)
Enzyme 7 Pathways
Enzyme 7 Reactions
  • L-ornithine = putrescine + CO2 [RN:R00670]
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 29893806 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID P11926 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name DCOR_HUMAN Link Image
Enzyme 7 PDB ID 1D7K Link Image
Enzyme 7 PDB File Show
Enzyme 7 3D Structure
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >1386 bp
ATGAACAACTTTGGTAATGAAGAGTTTGACTGCCACTTCCTCGATGAAGGTTTTACTGCC
AAGGACATTCTGGACCAGAAAATTAATGAAGTTTCTTCTTCTGATGATAAGGATGCCTTC
TATGTGGCAGACCTGGGAGACATTCTAAAGAAACATCTGAGGTGGTTAAAAGCTCTCCCT
CGTGTCACCCCCTTTTATGCAGTCAAATGTAATGATAGCAAAGCCATCGTGAAGACCCTT
GCTGCTACCGGGACAGGATTTGACTGTGCTAGCAAGACTGAAATACAGTTGGTGCAGAGT
CTGGGGGTGCCTCCAGAGAGGATTATCTATGCAAATCCTTGTAAACAAGTATCTCAAATT
AAGTATGCTGCTAATAATGGAGTCCAGATGATGACTTTTGATAGTGAAGTTGAGTTGATG
AAAGTTGCCAGAGCACATCCCAAAGCAAAGTTGGTTTTGCGGATTGCCACTGATGATTCC
AAAGCAGTCTGTCGTCTCAGTGTGAAATTCGGTGCCACGCTCAGAACCAGCAGGCTCCTT
TTGGAACGGGCGAAAGAGCTAAATATCGATGTTGTTGGTGTCAGCTTCCATGTAGGAAGC
GGCTGTACCGATCCTGAGACCTTCGTGCAGGCAATCTCTGATGCCCGCTGTGTTTTTGAC
ATGGGGGCTGAGGTTGGTTTCAGCATGTATCTGCTTGATATTGGCGGTGGCTTTCCTGGA
TCTGAGGATGTGAAACTTAAATTTGAAGAGATCACCGGCGTAATCAACCCAGCGTTGGAC
AAATACTTTCCGTCAGACTCTGGAGTGAGAATCATAGCTGAGCCCGGCAGATACTATGTT
GCATCAGCTTTCACGCTTGCAGTTAATATCATTGCCAAGAAAATTGTATTAAAGGAACAG
ACGGGCTCTGATGACGAAGATGAGTCGAGTGAGCAGACCTTTATGTATTATGTGAATGAT
GGCGTCTATGGATCATTTAATTGCATACTCTATGACCACGCACATGTAAAGCCCCTTCTG
CAAAAGAGACCTAAACCAGATGAGAAGTATTATTCATCCAGCATATGGGGACCAACATGT
GATGGCCTCGATCGGATTGTTGAGCGCTGTGACCTGCCTGAAATGCATGTGGGTGATTGG
ATGCTCTTTGAAAACATGGGCGCTTACACTGTTGCTGCTGCCTCTACGTTCAATGGCTTC
CAGAGGCCGACGATCTACTATGTGATGTCAGGGCCTGCGTGGCAACTCATGCAGCAATTC
CAGAACCCCGACTTCCCACCCGAAGTAGAGGAACAGGATGCCAGCACCCTGCCTGTGTCT
TGTGCCTGGGAGAGTGGGATGAAACGCCACAGAGCAGCCTGTGCTTCGGCTAGTATTAAT
GTGTAG
Enzyme 7 GenBank Gene ID M16650 Link Image
Enzyme 7 GeneCard ID ODC1 Link Image
Enzyme 7 GenAtlas ID ODC1 Link Image
Enzyme 7 HGNC ID HGNC:8109 Link Image
Enzyme 7 Chromosome Location 2
Enzyme 7 Locus 2p25
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Hickok NJ, Seppanen PJ, Gunsalus GL, Janne OA: Complete amino acid sequence of human ornithine decarboxylase deduced from complementary DNA. DNA. 1987 Jun;6(3):179-87. [PubMed Link Image]
  2. Fitzgerald MC, Flanagan MA: Characterization and sequence analysis of the human ornithine decarboxylase gene. DNA. 1989 Nov;8(9):623-34. [PubMed Link Image]
  3. van Steeg H, van Oostrom CT, Martens JW, van Kreyl C, Schepens J, Wieringa B: Nucleotide sequence of the human ornithine decarboxylase gene. Nucleic Acids Res. 1989 Nov 11;17(21):8855-6. [PubMed Link Image]
  4. Hickok NJ, Wahlfors J, Crozat A, Halmekyto M, Alhonen L, Janne J, Janne OA: Human ornithine decarboxylase-encoding loci: nucleotide sequence of the expressed gene and characterization of a pseudogene. Gene. 1990 Sep 14;93(2):257-63. [PubMed Link Image]
  5. Moshier JA, Gilbert JD, Skunca M, Dosescu J, Almodovar KM, Luk GD: Isolation and expression of a human ornithine decarboxylase gene. J Biol Chem. 1990 Mar 25;265(9):4884-92. [PubMed Link Image]
  6. Moshier JA, Osborne DL, Skunca M, Dosescu J, Gilbert JD, Fitzgerald MC, Polidori G, Wagner RL, Friezner Degen SJ, Luk GD, et al.: Multiple promoter elements govern expression of the human ornithine decarboxylase gene in colon carcinoma cells. Nucleic Acids Res. 1992 May 25;20(10):2581-90. [PubMed Link Image]
  7. Wright PS, Cooper JR, Cross-Doersen DE, Miller JA, Chmielewski PA, Wagner RL, Streng KA, Flanagan MA: Regulation of ornithine decarboxylase mRNA levels in human breast cancer cells: pattern of expression and involvement of core enhancer promoter element. Cell Growth Differ. 1995 Sep;6(9):1097-102. [PubMed Link Image]
  8. 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 Link Image]
  9. Hsieh JT, Denning MF, Heidel SM, Verma AK: Expression of human chromosome 2 ornithine decarboxylase gene in ornithine decarboxylase-deficient Chinese hamster ovary cells. Cancer Res. 1990 Apr 15;50(8):2239-44. [PubMed Link Image]
  10. Kaczmarek L, Calabretta B, Ferrari S, de Riel JK: Cell-cycle-dependent expression of human ornithine decarboxylase. J Cell Physiol. 1987 Sep;132(3):545-51. [PubMed Link Image]
  11. Bauer PM, Fukuto JM, Buga GM, Pegg AE, Ignarro LJ: Nitric oxide inhibits ornithine decarboxylase by S-nitrosylation. Biochem Biophys Res Commun. 1999 Aug 27;262(2):355-8. [PubMed Link Image]
  12. Bauer PM, Buga GM, Fukuto JM, Pegg AE, Ignarro LJ: Nitric oxide inhibits ornithine decarboxylase via S-nitrosylation of cysteine 360 in the active site of the enzyme. J Biol Chem. 2001 Sep 14;276(37):34458-64. Epub 2001 Jul 18. [PubMed Link Image]
  13. Leong WF, Chow VT: Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal differential cellular gene expression in response to enterovirus 71 infection. Cell Microbiol. 2006 Apr;8(4):565-80. [PubMed Link Image]
  14. Almrud JJ, Oliveira MA, Kern AD, Grishin NV, Phillips MA, Hackert ML: Crystal structure of human ornithine decarboxylase at 2.1 A resolution: structural insights to antizyme binding. J Mol Biol. 2000 Jan 7;295(1):7-16. [PubMed Link Image]
Enzyme 7 Metabolite References
  1. 497233;14707
Enzyme 8 [top]
Enzyme 8 ID 15055
Enzyme 8 Name cDNA FLJ75710, highly similar to Homo sapiens deoxyhypusine synthase (DHPS), transcript variant 1, mRNA (Deoxyhypusine synthase, isoform CRA_b)
Enzyme 8 Synonyms Not Available
Enzyme 8 Gene Name DHPS
Enzyme 8 Protein Sequence >cDNA FLJ75710, highly similar to Homo sapiens deoxyhypusine synthase (DHPS), transcript variant 1, mRNA (Deoxyhypusine synthase, isoform CRA_b)
MEGSLEREAPAGALAAVLKHSSTLPPESTQVRGYDFNRGVNYRALLEAFGTTGFQATNFG
RAVQQVNAMIEKKLEPLSQDEDQHADLTQSRRPLTSCTIFLGYTSNLISSGIRETIRYLV
QHNMVDVLVTTAGGVEEDLIKCLAPTYLGEFSLRGKELRENGINRIGNLLVPNENYCKFE
DWLMPILDQMVMEQNTEGVKWTPSKMIARLGKEINNPESVYYWAQKNHIPVFSPALTDGS
LGDMIFFHSYKNPGLVLDIVEDLRLINTQAIFAKCTGMIILGGGVVKHHIANANLMRNGA
DYAVYINTAQEFDGSDSGARPDEAVSWGKIRVDAQPVKVYADASLVFPLLVAETFAQKMD
AFMHEKNED
Enzyme 8 Number of Residues 369
Enzyme 8 Molecular Weight 40971
Enzyme 8 Theoretical pI 5.02
Enzyme 8 GO Classification Not Available
Enzyme 8 General Function Posttranslational modification, protein turnover, chaperones
Enzyme 8 Specific Function Not Available
Enzyme 8 Pathways Not Available
Enzyme 8 Reactions Not Available
Enzyme 8 Pfam Domain Function Not Available
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 158256538 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID A8K688 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name A8K688_HUMAN Link Image
Enzyme 8 PDB ID 1RQD Link Image
Enzyme 8 PDB File Show
Enzyme 8 3D Structure
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >1110 bp
ATGGAAGGTTCCCTGGAACGGGAGGCGCCAGCGGGGGCGCTGGCCGCCGTGCTAAAGCAC
AGCTCGACGTTGCCGCCCGAAAGCACCCAGGTCCGGGGCTACGACTTCAACCGCGGTGTG
AATTACCGCGCACTGCTGGAGGCCTTCGGCACCACCGGCTTCCAAGCAACCAACTTCGGG
CGCGCTGTACAGCAAGTCAATGCCATGATCGAGAAGAAGCTGGAACCACTGTCACAGGAT
GAAGACCAGCACGCGGACCTGACCCAGAGCCGCCGCCCACTTACCAGCTGCACCATTTTC
CTGGGATATACATCCAACCTCATCAGTTCAGGCATCCGTGAGACCATTCGCTACCTTGTG
CAGCACAACATGGTGGACGTATTGGTGACCACAGCTGGCGGCGTGGAGGAAGACCTCATC
AAGTGCCTGGCGCCCACATACTTGGGCGAGTTTAGCCTCAGGGGGAAGGAGCTCCGGGAG
AACGGGATCAATAGGATCGGAAACCTGCTGGTGCCCAATGAGAATTACTGCAAGTTTGAG
GACTGGCTGATGCCCATTCTGGACCAGATGGTGATGGAGCAGAACACAGAGGGTGTAAAG
TGGACGCCTTCTAAGATGATCGCCCGGCTGGGCAAGGAGATCAACAACCCAGAGTCCGTG
TATTACTGGGCCCAGAAGAACCACATCCCTGTGTTTAGTCCCGCACTTACAGACGGCTCG
CTGGGCGACATGATCTTCTTCCATTCCTACAAGAACCCGGGCCTGGTCCTGGACATCGTT
GAGGACCTGAGGCTCATCAACACACAGGCCATCTTTGCCAAGTGCACTGGGATGATCATT
CTGGGCGGGGGCGTGGTCAAGCACCACATTGCCAATGCCAACCTCATGCGGAACGGGGCC
GACTACGCTGTTTACATCAACACAGCCCAGGAGTTTGATGGCTCTGACTCAGGTGCCCGA
CCAGACGAGGCTGTCTCCTGGGGCAAGATCCGGGTGGATGCACAGCCCGTCAAGGTCTAT
GCTGACGCCTCCCTGGTCTTCCCCCTGCTTGTGGCTGAAACCTTTGCCCAGAAGATGGAT
GCCTTCATGCATGAGAAGAACGAGGACTGA
Enzyme 8 GenBank Gene ID AK291553 Link Image
Enzyme 8 GeneCard ID A8K688 Link Image
Enzyme 8 GenAtlas ID Not Available
Enzyme 8 HGNC ID Not Available
Enzyme 8 Chromosome Location 19
Enzyme 8 Locus 19p13.2-p13.1
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References Not Available
Enzyme 8 Metabolite References Not Available