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Human Metabolome Database Version 2.5

 

Showing metabocard for Tryptamine (HMDB00303)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2010-04-06 14:37:59
Accession Number HMDB00303
Secondary Accession Numbers Not Available
Common Name Tryptamine
Description Tryptamine is a monoamine compound that is common precursor molecule to many hormones and neurotransmitters. Biosynthesis generally proceeds from the amino acid tryptophan, with tryptamine in turn acting as a precursor for other compounds. Substitutions to the tryptamine molecule give rise to a group of compounds collectively known as tryptamines. The most well-known tryptamines are serotonin, an important neurotransmitter, and melatonin, a hormone involved in regulating the sleep-wake cycle.
Synonyms
  1. (3-Indolyl)ethylamine
  2. 1H-indole-3-ethanamine
  3. 2-(1H-Indol-3-yl)ethanamine
  4. 2-(1H-Indol-3-yl)ethylamine
  5. 2-(3-Indolyl)ethylamine
  6. 2-Indol-3-yl-aethylamin
  7. 2-indol-3-yl-ethylamine
  8. 3-(2-Aminoethyl)-1H-indole
  9. 3-(2-aminoethyl)indole
  10. 3-Indoleethanamine
  11. 3-Indoleethylamine
  12. Tryptamin
  13. Tryptamine
Chemical IUPAC Name 2-(1H-indol-3-yl)-ethylamine
Chemical Formula C10H12N2
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Amines
Class
  • Indoles and Indole Derivatives
Sub Class
  • Cyclic primary amines
Family
  • Mammalian Metabolite
Species
  • primary amine
  • primary aliphatic amine (alkylamine)
  • aromatic compound
  • heterocyclic compound
Biofunction
  • Component of Histidine metabolism
  • Component of Indole and ipecac alkaloid biosynthesis
  • Component of Phenylalanine metabolism
  • Component of Tryptophan metabolism
  • Component of Tyrosine metabolism
Application
Source
  • Endogenous
Average Molecular Weight 160.216
Monoisotopic Molecular Weight 160.100052
Isomeric SMILES NCCC1=CNC2=CC=CC=C12
Canonical SMILES NCCC1=CNC2=CC=CC=C12
KEGG Compound ID C00398 Link Image
BioCyc ID TRYPTAMINE Link Image
BiGG ID 34864 Link Image
Wikipedia Link Tryptamine Link Image
NuGOwiki Link HMDB00303 Link Image
Metagene Link HMDB00303 Link Image
METLIN ID 325 Link Image
PubChem Compound 1150 Link Image
PubChem Substance 11462248 Link Image
ChEBI ID 16765 Link Image
CAS Registry Number 61-54-1
InChI Identifier InChI=1/C10H12N2/c11-6-5-8-7-12-10-4-2-1-3-9(8)10/h1-4,7,12H,5-6,11H2
Synthesis Reference Abramovitch, R. A.; Shapiro, D. Tryptamines, carbolines, and related compounds. II. A convenient synthesis of tryptamines and b-carbolines. Journal of the Chemical Society (1956), 4589-92.
Melting Point (Experimental) 114 - 119 oC
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 33.0 mg/mL [MEYLAN,WM et al. (1996)]; 1.34 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 1
State Solid
Experimental LogP/Hydrophobicity 1.55 [HANSCH,C ET AL. (1995)] Source: PhysProp
Predicted LogP/Hydrophobicity 1.21 [Predicted by ALOGPS]; 1.4 [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 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 (Predicted from Solubility)
Biofluid Location
  • Urine
Tissue Location
Tissue References
Brain
Intestine
Nerve Cells
Neuron
Platelet
Concentrations (Normal)
Biofluid Urine
Value 0.098 (0.03-0.15) umol/mmol creatinine
Age Children:1-13 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 0.03 (0.01-0.049) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by Cornelius Lentner.
  • West Cadwell, N.J. : Medical education Div., Ciba-Geigy Corp.
  • Basel, Switzerland c1981-1992.
Biofluid Urine
Value 0.02 (0.02-0.03) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by Cornelius Lentner.
  • West Cadwell, N.J. : Medical education Div., Ciba-Geigy Corp.
  • Basel, Switzerland c1981-1992.
Biofluid Urine
Value 0.026 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]
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Tryptophan Metabolism SMP00063 Link Image map00380 Link Image
General References
  1. Radulovacki P, Djuricic-Nedelson M, Chen EH, Radulovacki M: Human tryptamine metabolism decreases during night sleep. Brain Res Bull. 1983 Jan;10(1):43-5. [PubMed Link Image]
  2. Mathew RJ, Ho BT, Kralik P, Weinman M, Claghorn JL: Anxiety and platelet MAO levels after relaxation training. Am J Psychiatry. 1981 Mar;138(3):371-3. [PubMed Link Image]
  3. Gilboa-Garber N, Katz-Bergman Y, Pinsky A: Comparative study of the sensitivity of acetylcholinesterases and cholinesterases from animal and bacterial sources to inhibition by serotonin and its derivatives. Experientia. 1978 Aug 15;34(8):992-3. [PubMed Link Image]
  4. Tsuchiya H, Ohtani S, Yamada K, Tajima K, Sato M: Formation of tetrahydro-beta-carbolines in human saliva. Biochem Pharmacol. 1995 Dec 22;50(12):2109-12. [PubMed Link Image]
  5. Tam WY, Chan MY, Lee PH: The menstrual cycle and platelet 5-HT uptake. Psychosom Med. 1985 Jul-Aug;47(4):352-62. [PubMed Link Image]
  6. Friedl W, Kruger J, Propping P: Intraindividual stability and extent of genetic determination of platelet monoamine oxidase activity. Pharmacopsychiatria. 1981 May;14(3):83-6. [PubMed Link Image]
  7. Sullivan JP, McDonnell L, Hardiman OM, Farrell MA, Phillips JP, Tipton KF: The oxidation of tryptamine by the two forms of monoamine oxidase in human tissues. Biochem Pharmacol. 1986 Oct 1;35(19):3255-60. [PubMed Link Image]
  8. al Mardini H, Harrison EJ, Ince PG, Bartlett K, Record CO: Brain indoles in human hepatic encephalopathy. Hepatology. 1993 Jun;17(6):1033-40. [PubMed Link Image]
  9. Young SN, Gauthier S: Effect of tryptophan administration on tryptophan, 5-hydroxyindoleacetic acid and indoleacetic acid in human lumbar and cisternal cerebrospinal fluid. J Neurol Neurosurg Psychiatry. 1981 Apr;44(4):323-8. [PubMed Link Image]
  10. Siwers B, Ringberger VA, Tuck JR, Sjoqvist F: Initial clinical trial based on biochemical methodology of zimelidine (a serotonin uptake inhibitor) in depressed patients. Clin Pharmacol Ther. 1977 Feb;21(2):194-200. [PubMed Link Image]
  11. Sullivan JL, Coffey CE, Basuk B, Cavenar JO, Maltbie AA, Zung WW: Urinary tryptamine excretion in chronic schizophrenics with low platelet MAO activity. Biol Psychiatry. 1980 Feb;15(1):113-20. [PubMed Link Image]
  12. Tsuchiya H, Hayashi T, Tatsumi M, Hoshino Y, Ohtani S, Takagi N: High-performance liquid-chromatographic analysis for serotonin and tryptamine excreted in urine after oral loading with L-tryptophan. Clin Chem. 1989 Jan;35(1):43-7. [PubMed Link Image]
  13. Anderson GM, Gerner RH, Cohen DJ, Fairbanks L: Central tryptamine turnover in depression, schizophrenia, and anorexia: measurement of indoleacetic acid in cerebrospinal fluid. Biol Psychiatry. 1984 Oct;19(10):1427-35. [PubMed Link Image]
  14. Gaszner P, Miklya I: The use of the synthetic enhancer substances (-)-deprenyl and (-)-BPAP in major depression. Neuropsychopharmacol Hung. 2004 Dec;6(4):210-20. [PubMed Link Image]
  15. Dolusic E, Kowalczyk M, Magnus V, Sandberg G, Normanly J: Biotinylated indoles as probes for indole-binding proteins. Bioconjug Chem. 2001 Mar-Apr;12(2):152-62. [PubMed Link Image]
  16. Demisch L, von der Muhlen H, Bochnik HJ, Seiler N: Substrate-typic changes of platelet monoamine oxidase activity in sub-types of schizophrenia. Arch Psychiatr Nervenkr. 1977 Dec 28;224(4):319-29. [PubMed Link Image]
  17. Gaszner P, Miklya I: Major depression and the synthetic enhancer substances, (-)-deprenyl and R-(-)-1-(benzofuran-2-yl)-2-propylaminopentane. Prog Neuropsychopharmacol Biol Psychiatry. 2006 Jan;30(1):5-14. Epub 2005 Jul 14. [PubMed Link Image]
  18. Mousseau DD, Layrargues GP, Butterworth RF: Region-selective decreases in densities of [3H]tryptamine binding sites in autopsied brain tissue from cirrhotic patients with hepatic encephalopathy. J Neurochem. 1994 Feb;62(2):621-5. [PubMed Link Image]
  19. Anthenelli RM, Tipp J, Li TK, Magnes L, Schuckit MA, Rice J, Daw W, Nurnberger JI Jr: Platelet monoamine oxidase activity in subgroups of alcoholics and controls: results from the Collaborative Study on the Genetics of Alcoholism. Alcohol Clin Exp Res. 1998 May;22(3):598-604. [PubMed Link Image]
  20. Wikipedia Link Image
Metabolic Enzymes
  1. Serotonin N-acetyltransferase
  2. Amine oxidase [flavin-containing] A
  3. Aromatic-L-amino-acid decarboxylase
  4. Amiloride-sensitive amine oxidase [copper-containing] precursor
  5. Indolethylamine N-methyltransferase
  6. cDNA, FLJ93072, Homo sapiens monoamine oxidase B (MAOB), nuclear gene encoding mitochondrial protein, mRNA (Monoamine oxidase B, isoform CRA_a)
  7. Serotonin N-acetyltransferase
Enzyme 1 [top]
Enzyme 1 ID 5259
Enzyme 1 Name Serotonin N-acetyltransferase
Enzyme 1 Synonyms
  1. Aralkylamine N- acetyltransferase
  2. AA-NAT
  3. Serotonin acetylase
Enzyme 1 Gene Name AANAT
Enzyme 1 Protein Sequence >Serotonin N-acetyltransferase
MSTQSTHPLKPEAPRLPPGIPESPSCQRRHTLPASEFRCLTPEDAVSAFEIEREAFISVL
GVCPLYLDEIRHFLTLCPELSLGWFEEGCLVAFIIGSLWDKERLMQESLTLHRSGGHIAH
LHVLAVHRAFRQQGRGPILLWRYLHHLGSQPAVRRAALMCEDALVPFYERFSFHAVGPCA
ITVGSLTFMELHCSLRGHPFLRRNSGC
Enzyme 1 Number of Residues 207
Enzyme 1 Molecular Weight 23344
Enzyme 1 Theoretical pI 7.57
Enzyme 1 GO Classification
Function
  • N-acetyltransferase activity
  • acetyltransferase activity
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
Component
Enzyme 1 General Function Not Available
Enzyme 1 Specific Function Catalyzes the N-acetylation of serotonin into N- acetylserotonin
Enzyme 1 Pathways
Enzyme 1 Reactions
  • acetyl-CoA + an aralkylamine = CoA + an N-acetylaralkylamine
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 1389594 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q16613 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name SNAT_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >624 bp
ATGTCCACGCAGAGCACCCACCCCCTGAAACCTGAGGCCCCACGTCTGCCACCTGGGATC
CCCGAGTCCCCGAGCTGTCAGCGGCGCCACACACTCCCTGCCAGTGAGTTTCGCTGCCTC
ACCCCGGAGGACGCTGTCAGCGCCTTTGAGATCGAGCGTGAAGCCTTCATCTCCGTCTTG
GGCGTCTGCCCCCTGTACCTGGATGAGATCCGGCACTTCCTGACCCTATGTCCAGAGCTG
TCCCTGGGCTGGTTCGAGGAGGGCTGCCTTGTGGCCTTCATCATCGGCTCGCTCTGGGAC
AAGGAGAGACTCATGCAGGAGTCACTGACGCTGCACAGGTCTGGGGGCCACATAGCCCAC
CTGCATGTGCTGGCCGTGCACCGCGCCTTCCGGCAGCAGGGCAGGGGCCCCATCCTGCTG
TGGCGCTACCTGCACCACCTGGGCAGCCAGCCGGCCGTGCGCCGGGCCGCGCTCATGTGC
GAGGACGCGCTGGTACCCTTCTATGAGAGGTTCAGCTTCCACGCCGTGGGCCCCTGCGCC
ATCACCGTGGGCTCCCTCACCTTCATGGAGCTCCACTGCTCCCTGCGGGGCCACCCCTTC
CTGCGCAGGAACAGCGGCTGCTGA
Enzyme 1 GenBank Gene ID U40391 Link Image
Enzyme 1 GeneCard ID AANAT Link Image
Enzyme 1 GenAtlas ID AANAT Link Image
Enzyme 1 HGNC ID HGNC:19 Link Image
Enzyme 1 Chromosome Location 17
Enzyme 1 Locus 17q25
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Coon SL, Mazuruk K, Bernard M, Roseboom PH, Klein DC, Rodriguez IR: The human serotonin N-acetyltransferase (EC 2.3.1.87) gene (AANAT): structure, chromosomal localization, and tissue expression. Genomics. 1996 May 15;34(1):76-84. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5401
Enzyme 2 Name Amine oxidase [flavin-containing] A
Enzyme 2 Synonyms
  1. Monoamine oxidase type A
  2. 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 59682
Enzyme 2 Theoretical pI 7.96
Enzyme 2 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
Enzyme 2 General Function Amino acid transport and metabolism
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
  • RCH2NH2 + H2O + O2 = RCHO + ammonia + H2O2
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • 498-518
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 187353 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P21397 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name AOFA_HUMAN Link Image
Enzyme 2 PDB ID 1O5W Link Image
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
ATTCACTTCAGACCAGAGCTTCCAGCAGAGAGAAACCAGTTAATTCAGCGGCTTCCAATG
GGAGCTGTCATTAAGTGCATGATGTATTACAAGGAGGCCTTCTGGAAGAAGAAGGATTAC
TGTGGCTGCATGATCATTGAAGATGAAGATGCTCCAATTTCAATAACCTTGGATGACACC
AAGCCTGATGGGTCACTGCCTGCCATCATGGGCTTCATTCTTGCCCGGAAAGCTGATCGA
CTTGCTAAGCTACATAAGGAAATAAGGAAGAAGAAAATCTGTGAGCTCTATGCCAAAGTG
CTGGGATCCCAAGAAGCTTTACATCCAGTGCATTATGAAGAGAAGAACTGGTGTGAGGAG
CAGTACTCTGGGGGCTGCTACACGGCCTACTTCCCTCCTGGGATCATGACTCAATATGGA
AGGGTGATTCGTCAACCCGTGGGCAGGATTTTCTTTGCGGGCACAGAGACTGCCACAAAG
TGGAGCGGCTACATGGAAGGGGCAGTTGAGGCTGGAGAACGAGCAGCTAGGGAGGTCTTA
AATGGTCTCGGGAAGGTGACCGAGAAAGATATCTGGGTACAAGAACCTGAATCAAAGGAC
GTTCCAGCGGTAGAAATCACCCACACCTTCTGGGAAAGGAACCTGCCCTCTGTTTCTGGC
CTGCTGAAGATCATTGGATTTTCCACATCAGTAACTGCCCTGGGGTTTGTGCTGTACAAA
TACAAGCTCCTGCCACGGTCTTGA
Enzyme 2 GenBank Gene ID M68840 Link Image
Enzyme 2 GeneCard ID MAOA Link Image
Enzyme 2 GenAtlas ID MAOA Link Image
Enzyme 2 HGNC ID HGNC:6833 Link Image
Enzyme 2 Chromosome Location X
Enzyme 2 Locus Xp11.3
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
  4. Denney RM: The promoter of the human monoamine oxidase A gene. Prog Brain Res. 1995;106:57-66. [PubMed Link Image]
  5. 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 Link Image]
  6. 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 Link Image]
  7. 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 Link Image]
  8. 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 Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5510
Enzyme 3 Name Aromatic-L-amino-acid decarboxylase
Enzyme 3 Synonyms
  1. AADC
  2. DOPA decarboxylase
  3. DDC
Enzyme 3 Gene Name DDC
Enzyme 3 Protein Sequence >Aromatic-L-amino-acid decarboxylase
MNASEFRRRGKEMVDYVANYMEGIEGRQVYPDVEPGYLRPLIPAAAPQEPDTFEDIINDV
EKIIMPGVTHWHSPYFFAYFPTASSYPAMLADMLCGAIGCIGFSWAASPACTELETVMMD
WLGKMLELPKAFLNEKAGEGGGVIQGSASEATLVALLAARTKVIHRLQAASPELTQAAIM
EKLVAYSSDQAHSSVERAGLIGGVKLKAIPSDGNFAMRASALQEALERDKAAGLIPFFMV
ATLGTTTCCSFDNLLEVGPICNKEDIWLHVDAAYAGSAFICPEFRHLLNGVEFADSFNFN
PHKWLLVNFDCSAMWVKKRTDLTGAFRLDPTYLKHSHQDSGLITDYRHWQIPLGRRFRSL
KMWFVFRMYGVKGLQAYIRKHVQLSHEFESLVRQDPRFEICVEVILGLVCFRLKGSNKVN
EALLQRINSAKKIHLVPCHLRDKFVLRFAICSRTVESAHVQRAWEHIKELAADVLRAERE
Enzyme 3 Number of Residues 480
Enzyme 3 Molecular Weight 53895
Enzyme 3 Theoretical pI 7.21
Enzyme 3 GO Classification
Function
  • carbon-carbon lyase activity
  • carboxy-lyase activity
  • catalytic activity
  • lyase activity
Process
  • amino acid and derivative metabolism
  • amino acid metabolism
  • cellular metabolism
  • metabolism
  • physiological process
Component
Enzyme 3 General Function Amino acid transport and metabolism
Enzyme 3 Specific Function Catalyzes the decarboxylation of L-3,4- dihydroxyphenylalanine (DOPA) to dopamine, L-5-hydroxytryptophan to serotonin and L-tryptophan to tryptamine
Enzyme 3 Pathways
Enzyme 3 Reactions
  • L-tryptophan = tryptamine + CO2
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 181521 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P20711 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name DDC_HUMAN Link Image
Enzyme 3 PDB ID 1JS3 Link Image
Enzyme 3 PDB File Show
Enzyme 3 3D Structure
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1443 bp
ATGAACGCAAGTGAATTCCGAAGGAGAGGGAAGGAGATGGTGGATTACGTGGCCAACTAC
ATGGAAGGCATTGAGGGACGCCAGGTCTACCCTGACGTGGAGCCCGGGTACCTGCGGCCG
CTGATCCCTGCCGCTGCCCCTCAGGAGCCAGACACGTTTGAGGACATCATCAACGACGTT
GAGAAGATAATCATGCCTGGGGTGACGCACTGGCACAGCCCCTACTTCTTCGCCTACTTC
CCCACTGCCAGCTCGTACCCGGCCATGCTTGCGGACATGCTGTGCGGGGCCATTGGCTGC
ATCGGCTTCTCCTGGGCGGCAAGCCCAGCATGCACAGAGCTGGAGACTGTGATGATGGAC
TGGCTCGGGAAGATGCTGGAACTACCAAAGGCATTTTTGAATGAGAAAGCTGGAGAAGGG
GGAGGAGTGATCCAGGGAAGTGCCAGTGAAGCCACCCTGGTGGCCCTGCTGGCCGCTCGG
ACCAAAGTGATCCATCGGCTGCAGGCAGCGTCCCCAGAGCTCACACAGGCCGCTATCATG
GAGAAGCTGGTGGCTTACTCATCCGATCAGGCACACTCCTCAGTGGAAAGAGCTGGGTTA
ATTGGTGGAGTGAAATTAAAAGCCATCCCCTCAGATGGCAACTTCGCCATGCGTGCGTCT
GCCCTGCAGGAAGCCCTGGAGAGAGACAAAGCGGCTGGCCTGATTCCTTTCTTTATGGTT
GCCACCCTGGGGACCACAACATGCTGCTCCTTTGACAATCTCTTAGAAGTCGGTCCTATC
TGCAACAAGGAAGACATATGGCTGCACGTTGATGCAGCCTACGCAGGCAGTGCATTCATC
TGCCCTGAGTTCCGGCACCTTCTGAATGGAGTGGAGTTTGCAGATTCATTCAACTTTAAT
CCCCACAAATGGCTATTGGTGAATTTTGACTGTTCTGCCATGTGGGTGAAAAAGAGAACA
GACTTAACGGGAGCCTTTAGACTGGACCCCACTTACCTGAAGCACAGCCATCAGGATTCA
GGGCTTATCACTGACTACCGGCATTGGCAGATACCACTGGGCAGAAGATTTCGCTCTTTG
AAAATGTGGTTTGTATTTAGGATGTATGGAGTCAAAGGACTGCAGGCTTATATCCGCAAG
CATGTCCAGCTGTCCCATGAGTTTGAGTCACTGGTGCGCCAGGATCCCCGCTTTGAAATC
TGTGTGGAAGTCATTCTGGGGCTTGTCTGCTTTCGGCTAAAGGGTTCCAACAAAGTGAAT
GAAGCTCTTCTGCAAAGAATAAACAGTGCCAAAAAAATCCACTTGGTTCCATGTCACCTC
AGGGACAAGTTTGTCCTGCGCTTTGCCATCTGTTCTCGCACGGTGGAATCTGCCCATGTG
CAGCGGGCCTGGGAACACATCAAAGAGCTGGCGGCCGACGTGCTGCGAGCAGAGAGGGAG
TAG
Enzyme 3 GenBank Gene ID M76180 Link Image
Enzyme 3 GeneCard ID DDC Link Image
Enzyme 3 GenAtlas ID DDC Link Image
Enzyme 3 HGNC ID HGNC:2719 Link Image
Enzyme 3 Chromosome Location 7
Enzyme 3 Locus 7p11
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Ichinose H, Kurosawa Y, Titani K, Fujita K, Nagatsu T: Isolation and characterization of a cDNA clone encoding human aromatic L-amino acid decarboxylase. Biochem Biophys Res Commun. 1989 Nov 15;164(3):1024-30. [PubMed Link Image]
  2. Scherer LJ, McPherson JD, Wasmuth JJ, Marsh JL: Human dopa decarboxylase: localization to human chromosome 7p11 and characterization of hepatic cDNAs. Genomics. 1992 Jun;13(2):469-71. [PubMed Link Image]
  3. Sumi-Ichinose C, Ichinose H, Takahashi E, Hori T, Nagatsu T: Molecular cloning of genomic DNA and chromosomal assignment of the gene for human aromatic L-amino acid decarboxylase, the enzyme for catecholamine and serotonin biosynthesis. Biochemistry. 1992 Mar 3;31(8):2229-38. [PubMed Link Image]
  4. Le Van Thai A, Coste E, Allen JM, Palmiter RD, Weber MJ: Identification of a neuron-specific promoter of human aromatic L-amino acid decarboxylase gene. Brain Res Mol Brain Res. 1993 Mar;17(3-4):227-38. [PubMed Link Image]
  5. Craig SP, Thai AL, Weber M, Craig IW: Localisation of the gene for human aromatic L-amino acid decarboxylase (DDC) to chromosome 7p13-->p11 by in situ hybridisation. Cytogenet Cell Genet. 1992;61(2):114-6. [PubMed Link Image]
  6. 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 Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5627
Enzyme 4 Name Amiloride-sensitive amine oxidase [copper-containing] precursor
Enzyme 4 Synonyms
  1. Diamine oxidase
  2. DAO
  3. Amiloride-binding protein
  4. ABP
  5. Histaminase
  6. Kidney amine oxidase
  7. KAO
Enzyme 4 Gene Name ABP1
Enzyme 4 Protein Sequence >Amiloride-sensitive amine oxidase [copper-containing] precursor
MPALGWAVAAILMLQTAMAEPSPGTLPRKAGVFSDLSNQELKAVHSFLWSKKELRLQPSS
TTTMAKNTVFLIEMLLPKKYHVLRFLDKGERHPVREARAVIFFGDQEHPNVTEFAVGPLP
GPCYMRALSPRPGYQSSWASRPISTAEYALLYHTLQEATKPLHQFFLNTTGFSFQDCHDR
CLAFTDVAPRGVASGQRRSWLIIQRYVEGYFLHPTGLELLVDHGSTDAGHWAVEQVWYNG
KFYGSPEELARKYADGEVDVVVLEDPLPGGKGHDSTEEPPLFSSHKPRGDFPSPIHVSGP
RLVQPHGPRFRLEGNAVLYGGWSFAFRLRSSSGLQVLNVHFGGERIAYEVSVQEAVALYG
GHTPAGMQTKYLDVGWGLGSVTHELAPGIDCPETATFLDTFHYYDADDPVHYPRALCLFE
MPTGVPLRRHFNSNFKGGFNFYAGLKGQVLVLRTTSTVYNYDYIWDFIFYPNGVMEAKMH
ATGYVHATFYTPEGLRHGTRLHTHLIGNIHTHLVHYRVDLDVAGTKNSFQTLQMKLENIT
NPWSPRHRVVQPTLEQTQYSWERQAAFRFKRKLPKYLLFTSPQENPWGHKRSYRLQIHSM
ADQVLPPGWQEEQAITWARYPLAVTKYRESELCSSSIYHQNDPWDPPVVFEQFLHNNENI
ENEDLVAWVTVGFLHIPHSEDIPNTATPGNSVGFLLRPFNFFPEDPSLASRDTVIVWPRD
NGPNYVQRWIPEDRDCSMPPPFSYNGTYRPV
Enzyme 4 Number of Residues 751
Enzyme 4 Molecular Weight 85342
Enzyme 4 Theoretical pI 7.01
Enzyme 4 GO Classification
Function
  • binding
  • cation binding
  • copper ion binding
  • ion binding
  • transition metal ion binding
Process
Component
Enzyme 4 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 4 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 4 Pathways
Enzyme 4 Reactions
  • RCH2NH2 + H2O + O2 = RCHO + ammonia + H2O2
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • 1-19
Enzyme 4 Transmembrane Regions Not Available
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 177960 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID P19801 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name ABP1_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >2142 bp
ATGCCGGCCCTGGGCTGGGCCGTGGCTGCCATCCTGATGCTGCAGACGGCCATGGCGGAG
CCCTCCCCGGGGACTCTGCCCAGGAAGGCAGGGGTGTTTTCAGACCTAAGCAACCAAGAG
CTGAAGGCAGTGCACAGCTTCCTCTGGTCCAAGAAGGAGCTGAGGCTGCAGCCCTCCAGT
ACCACCACCATGGCCAAGAACACCGTGTTTCTCATCGAGATGCTGCTGCCCAAGAAGTAC
CATGTGCTGAGGTTTCTGGATAAAGGTGAAAGGCATCCTGTGCGGGAAGCCCGTGCCGTC
ATCTTCTTTGGTGACCAGGAGCATCCCAATGTCACCGAGTTTGCTGTGGGGCCCCTGCCA
GGGCCCTGCTACATGCGAGCACTGTCCCCCAGGCCTGGGTACCAGTCCTCCTGGGCATCG
AGGCCCATCTCCACAGCAGAGTATGCCCTCCTCTACCACACCCTGCAGGAAGCCACCAAG
CCCCTGCATCAGTTCTTCCTCAATACCACAGGCTTCTCATTCCAAGACTGCCATGACAGA
TGCCTGGCCTTCACCGATGTGGCCCCCCGGGGTGTGGCTTCTGGCCAGCGCCGCAGTTGG
CTTATCATACAGCGCTATGTAGAAGGCTACTTTCTGCACCCCACTGGGCTGGAGCTCCTC
GTGGATCATGGGAGCACAGATGCTGGGCACTGGGCCGTGGAGCAGGTGTGGTACAACGGG
AAGTTCTATGGGAGCCCAGAGGAACTGGCACGGAAGTATGCAGATGGAGAGGTGGACGTG
GTGGTCCTGGAGGACCGCTGCCTGGGGGCAAGGGGCATGACAGCACAGAGGAGCCGGCCC
TCTTCTCCTCCACAAGCCCCGCGGGACTTTCCCCAGCCCCATCCATGTGAGCGGCCCCCG
CTTGGTCCAGCCCCACGGCCCTCGCTTCAGGCTGGAGGGCAACGCTGTGCTCTACGGCGG
CTGGAGCTTTGCCTTCCGGTGCGCTCCTCCTCCGGGCTGCAGGTCCTGAACGTGCACTTC
GGCGGAGAGCGCATTGCCTATGAGGTCAGCGTGCAAGAGGCAGTGGCGCTGTATGGAGGA
CACACACCTGCAGGCATGCAGACCAAGTACCTCGATGTCGGCTGGGGCCTGGGCAGCGTC
ACTCATGAGTTAGCCCCCGGCATCGACTGCCCGGAGACCGCCACCTTCCTGGACACTTTC
CACTACTATGATGCCGATGACCCGGTCCATTATCCCCGAGCCCTCTGCCTCTTTGAAATG
CCCACAGGGGTGCCCCTTCGGCGGCACTTTAATTCCAACTTTAAAGGTGGCTTCAACTTC
TATGCAGGGCTGAAGGGCCAGGTGCTGGTGCTGCGGACAACTTCAACTGTCTACAATTAT
GATTACATTTGGGACTTTATCTTCTACCCCAACGGGGTGATGGAGGCCAAGATGCATGCC
ACTGGCTACGTCCACGCCACCTTCTACACCCCCGAGGGCTGCGCACGGCACTCGCCTGCA
CACCCACCTGATTGGCAACATACACACTCACTTGTGCACTACCGCGTAGACCTGGATGTG
GCAGGCACCAAGAACAGCTTCCAGACACTGCAGATGAAGCTAGAAAACATCACCAACCCC
TGGAGCCCGAGACACCGCGTGGTCCAGCCAACTCTGGAGCAGACGCAGTACTCCTGGGAG
CGCCAGGCGGCCTTCCGCTTCAAAAGGAGGCTGCCCAAGTACCTGCTCTTTACCAGCCCC
CAGGAGAACCCCTGGGGCCACAAGCGCAGCTACCGCCTGCAGATCCACTCCATGGCCGAC
CAGGTGCTGCCCCCAGGCTGGCAGGAGGAGCAGGCCATCACCTGGGCAAGGTACCCCCTG
GCAGTGACCAAGTACCGGGAGTCAGAGCTGTGCAGCAGCAGCATCTACCACCAGAACGAC
CCCTGGGACCCGCCCGTGGTCTTTGAGCAGTTTCTTCACAACAACGAGAACATTGAAAAT
GAGGACCTGGTGGCCTGGGTGACGGTGGGCTTCCTGCACATCCCCCACTCAGAGGACATT
CCCAACACAGCCACACCTGGGAACTCCGTGGGCTTCCTGCTCCGGCCATTCAACTTCTTC
CCAGAGGACCCCTCCCCTCCCTGGCATCCAGAGACACTGTGA
Enzyme 4 GenBank Gene ID M55602 Link Image
Enzyme 4 GeneCard ID ABP1 Link Image
Enzyme 4 GenAtlas ID ABP1 Link Image
Enzyme 4 HGNC ID HGNC:80 Link Image
Enzyme 4 Chromosome Location 7
Enzyme 4 Locus 7q34-q36
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 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. 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 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5652
Enzyme 5 Name Indolethylamine N-methyltransferase
Enzyme 5 Synonyms
  1. Aromatic alkylamine N-methyltransferase
  2. Indolamine N-methyltransferase
  3. Arylamine N- methyltransferase
  4. Amine N-methyltransferase
Enzyme 5 Gene Name INMT
Enzyme 5 Protein Sequence >Indolethylamine N-methyltransferase
MKGGFTGGDEYQKHFLPRDYLATYYSFDGSPSPEAEMLKFNLECLHKTFGPGGLQGDTLI
DIGSGPTIYQVLAACDSFQDITLSDFTDRNREELEKWLKKEPGAYDWTPAVKFACELEGN
SGRWEEKEEKLRAAVKRVLKCDVHLGNPLAPAVLPLADCVLTLLAMECACCSLDAYRAAL
CNLASLLKPGGHLVTTVTLRLPSYVVGKREFSCVALEKEEVEQAVLDAGFDIEQLLHSPQ
SYSVTNAANNGVCCIVARKKPGP
Enzyme 5 Number of Residues 263
Enzyme 5 Molecular Weight 28815
Enzyme 5 Theoretical pI 4.92
Enzyme 5 GO Classification
Function
  • catalytic activity
  • methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
Component
Enzyme 5 General Function Not Available
Enzyme 5 Specific Function Catalyzes the N-methylation of tryptamine and structurally related compounds (Potential)
Enzyme 5 Pathways
Enzyme 5 Reactions
  • S-adenosyl-L-methionine + an amine = S-adenosyl-L-homocysteine + a methylated amine
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 6580815 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID O95050 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name INMT_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >792 bp
ATGAAGGGTGGCTTCACTGGGGGTGATGAGTACCAGAAGCACTTCCTGCCCAGGGACTAC
TTGGCTACTTACTACAGCTTCGATGGCAGCCCCTCACCCGAGGCCGAGATGCTGAAGTTT
AACTTGGAATGTCTCCACAAGACCTTCGGCCCTGGAGGCCTCCAAGGGGACACGCTGATT
GACATTGGCTCAGGTCCTACCATCTACCAAGTTCTTGCTGCCTGTGATTCCTTCCAAGAC
ATCACTCTCTCCGACTTTACCGACCGCAACCGGGAGGAGCTGGAAAAGTGGCTGAAGAAG
GAGCCGGGGGCCTATGACTGGACCCCAGCGGTGAAATTCGCCTGTGAGCTGGAAGGAAAC
AGCGGCCGATGGGAGGAGAAGGAGGAGAAGCTGCGGGCAGCGGTGAAGCGGGTGCTCAAG
TGCGATGTCCACCTGGGCAACCCGCTGGCCCCGGCTGTGTTGCCTCTCGCCGACTGTGTG
CTCACCCTGCTGGCCATGGAGTGTGCCTGCTGTAGCCTTGATGCCTACCGCGCTGCCCTG
TGCAACCTTGCCTCACTGCTCAAGCCGGGTGGCCACCTGGTGACCACTGTCACGCTTCGG
CTCCCGTCCTACGTGGTGGGGAAGCGTGAATTTTCCTGCGTGGCCCTGGAGAAAGAGGAG
GTGGAGCAGGCTGTCCTGGATGCTGGCTTTGACATTGAACAGCTCCTACACAGTCCCCAG
AGCTACTCTGTCACCAATGCTGCCAACAATGGGGTCTGCTGCATTGTGGCTCGCAAGAAG
CCTGGGCCCTGA
Enzyme 5 GenBank Gene ID AF128846 Link Image
Enzyme 5 GeneCard ID INMT Link Image
Enzyme 5 GenAtlas ID INMT Link Image
Enzyme 5 HGNC ID HGNC:6069 Link Image
Enzyme 5 Chromosome Location Not Available
Enzyme 5 Locus Not Available
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Thompson MA, Moon E, Kim UJ, Xu J, Siciliano MJ, Weinshilboum RM: Human indolethylamine N-methyltransferase: cDNA cloning and expression, gene cloning, and chromosomal localization. Genomics. 1999 Nov 1;61(3):285-97. [PubMed Link Image]
  2. 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]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 16425
Enzyme 6 Name cDNA, FLJ93072, Homo sapiens monoamine oxidase B (MAOB), nuclear gene encoding mitochondrial protein, mRNA (Monoamine oxidase B, isoform CRA_a)
Enzyme 6 Synonyms Not Available
Enzyme 6 Gene Name MAOB
Enzyme 6 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 6 Number of Residues 520
Enzyme 6 Molecular Weight 58764
Enzyme 6 Theoretical pI 7.55
Enzyme 6 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
Enzyme 6 General Function Amino acid transport and metabolism
Enzyme 6 Specific Function Not Available
Enzyme 6 Pathways Not Available
Enzyme 6 Reactions Not Available
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein Not Available
Enzyme 6 UniProtKB/Swiss-Prot ID B2R6R3 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name B2R6R3_HUMAN Link Image
Enzyme 6 PDB ID 2BK3 Link Image
Enzyme 6 PDB File Show
Enzyme 6 3D Structure
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence Not Available
Enzyme 6 GenBank Gene ID AK312679 Link Image
Enzyme 6 GeneCard ID B2R6R3 Link Image
Enzyme 6 GenAtlas ID Not Available
Enzyme 6 HGNC ID Not Available
Enzyme 6 Chromosome Location Not Available
Enzyme 6 Locus Not Available
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References Not Available
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 17340
Enzyme 7 Name Serotonin N-acetyltransferase
Enzyme 7 Synonyms
  1. Serotonin acetylase
  2. Aralkylamine N-acetyltransferase
  3. AA-NAT
Enzyme 7 Gene Name AANAT
Enzyme 7 Protein Sequence >Serotonin N-acetyltransferase
MSMQSTHPPKPEAPRLPPGIPESPSCQRRHTLPASEFRCLTPEDAVSAFEIEREAFISVL
GVCPLDLDEIRHFLTLCPELSLGWFEEGCLVAFIIGSLWDKERLMQESLTLHRSGGHIAH
LHVLAVHRAFRQQGRGPILLWRYLHHLGSQPAVRRAALMCEDALVPFYERFSFHAVGPCA
ITVGSLTFTELHCSLRDHPFLRRNSGC
Enzyme 7 Number of Residues 207
Enzyme 7 Molecular Weight 23337.7
Enzyme 7 Theoretical pI 7.14
Enzyme 7 GO Classification
Function
  • N-acetyltransferase activity
  • acetyltransferase activity
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
Component
Enzyme 7 General Function Involved in aralkylamine N-acetyltransferase activity
Enzyme 7 Specific Function Catalyzes the N-acetylation of serotonin into N- acetylserotonin
Enzyme 7 Pathways Not Available
Enzyme 7 Reactions Not Available
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 57635273 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID Q5IS55 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name SNAT_PANTR Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence Not Available
Enzyme 7 GenBank Gene ID AY665273 Link Image
Enzyme 7 GeneCard ID AANAT Link Image
Enzyme 7 GenAtlas ID Not Available
Enzyme 7 HGNC ID Not Available
Enzyme 7 Chromosome Location 1
Enzyme 7 Locus 17q25
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Dorus S, Vallender EJ, Evans PD, Anderson JR, Gilbert SL, Mahowald M, Wyckoff GJ, Malcom CM, Lahn BT: Accelerated evolution of nervous system genes in the origin of Homo sapiens. Cell. 2004 Dec 29;119(7):1027-40. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available