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Human Metabolome Database Version 2.5

 

Showing metabocard for 5-Hydroxy-L-tryptophan (HMDB00472)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2010-06-07 11:37:11
Accession Number HMDB00472
Secondary Accession Numbers HMDB00504
Common Name 5-Hydroxy-L-tryptophan
Description 5-Hydroxy-L-tryptophan is an aromatic amino acid naturally produced by the body from the essential amino acid l-tryptophan. 5-Hydroxy-L-tryptophan is the immediate precursor of the neurotransmitter serotonin. The conversion to serotonin is catalyzed by the enzyme aromatic l-amino acid decarboxylase (EC 4.1.1.28, AADC1 also known as dopa decarboxylase), an essential enzyme in the metabolism of the monoamine neurotransmitters. An accumulation of 5-Hydroxy-L-tryptophan in cerebrospinal fluid occurs in Aromatic l-amino acid decarboxylase deficiency (OMIM 608643), accompanied by an increased excretion in the urine of the patients, which are indicative of the disorder but not specific 5-Hydroxy-L-tryptophan is also increased in other disorders such as in Parkinson's patients with severe postural instability and gait disorders. Confirmation of the diagnosis AADC deficiency is then required by enzyme activity measurement or genetic analysis. The amount of endogenous 5-Hydroxy-L-tryptophan available for serotonin synthesis depends on the availability of tryptophan and on the activity of various enzymes, especially tryptophan hydroxylase (EC 1.14.16.4), indoleamine 2,3-dioxygenase (EC 1.13.11.52), and tryptophan 2,3-dioxygenase. (EC 1.13.11.11, TDO). 5-Hydroxy-L-tryptophan has been used clinically for over 30 years. In addition to depression, the therapeutic administration of 5-Hydroxy-L-tryptophan has been shown to be effective in treating a wide variety of conditions, including fibromyalgia, insomnia, binge eating associated with obesity, cerebellar ataxia, and chronic headaches. 5-Hydroxy-L-tryptophan easily crosses the blood-brain barrier and effectively increases central nervous system (CNS) synthesis of serotonin. Supplementation with 5-Hydroxy-L-tryptophan is hypothesized to normalize serotonin synthesis, which is putatively related to its antidepressant properties. (PMID: 9295177, 17240182, 16023217)
Synonyms
  1. (+-)-5-Hydroxytryptophan
  2. (S)-5-Hydroxytryptophan
  3. 5-hydroxy-L-Tryptophan
  4. 5-Hydroxy-tryptophan
  5. 5-Hydroxyl-L-tryptophan
  6. 5-Hydroxytryptophan
  7. 5-Hydroxytryptophan L form
  8. 5-Hydroxytryptophan L-form
  9. Cincofarm
  10. Hydroxytryptophan
  11. Levothym
  12. Levotinine
  13. Oxitriptan
  14. Oxyfan
  15. Oxytryptophan
  16. Pretonine
  17. Quietim
  18. Serotonyl
  19. Telesol
  20. Triptene
  21. L-5-Hydroxytryptophan
Chemical IUPAC Name 2-amino-3-(5-hydroxy-1H-indol-3-yl)propanoic acid
Chemical Formula C11H12N2O3
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Amino acids and Amino Acid conjugates
Class
  • Amino Acids
  • Indoles and Indole Derivatives
Sub Class
  • NA
Family
  • Mammalian Metabolite
Species
  • phenol or hydroxyhetarene
  • primary amine
  • primary aliphatic amine (alkylamine)
  • carboxylic acid
  • aromatic compound
  • heterocyclic compound
  • alpha-aminoacid
Biofunction
  • Protein synthesis, amino acid biosynthesis
Application
—
Source
  • Endogenous
Average Molecular Weight 220.225
Monoisotopic Molecular Weight 220.084793
Isomeric SMILES NC(CC1=CNC2=C1C=C(O)C=C2)C(O)=O
Canonical SMILES NC(CC1=CNC2=C1C=C(O)C=C2)C(O)=O
KEGG Compound ID C00643 Link Image
BioCyc ID 5-HYDROXY-TRYPTOPHAN Link Image
BiGG ID 36630 Link Image
Wikipedia Link 5-HTP Link Image
NuGOwiki Link HMDB00472 Link Image
Metagene Link HMDB00472 Link Image
METLIN ID Not Available
PubChem Compound 144 Link Image
PubChem Substance 8150478 Link Image
ChEBI ID 17780 Link Image
CAS Registry Number 4350-09-8
InChI Identifier InChI=1/C11H12N2O3/c12-9(11(15)16)3-6-5-13-10-2-1-7(14)4-8(6)10/h1-2,4-5,9,13-14H,3,12H2,(H,15,16)
Synthesis Reference Boroda, E.; Rakowska, S.; Kanski, R.; Kanska, M. Enzymatic synthesis of L-tryptophan and 5'-hydroxy-L-tryptophan labeled with deuterium and tritium at the a-carbon position. Journal of Labelled Compounds & Radiopharmaceuticals (2003), 46(8), 691-698.
Melting Point (Experimental) 293-298 oC
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 3.63 mg/mL [Predicted by ALOGPS]; 31.5 mg/mL at 25 oC [MEYLAN,WM et al. (1996)] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity -2.051 Source: PhysProp
Predicted LogP/Hydrophobicity -1.7 [Predicted by PubChem via XLOGP]; -1.70 [MEYLAN,WM & HOWARD,PH (1995)]; -1.56 [Predicted by ALOGPS] 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 Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm
Biofluid Location
  • Blood
  • Cerebrospinal Fluid
  • Urine
Tissue Location Not Available
Concentrations (Normal)
Biofluid Blood
Value 0.018 +/- 0.0027 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Gijsman HJ, van Gerven JM, de Kam ML, Schoemaker RC, Pieters MS, Weemaes M, de Rijk R, van der Post J, Cohen AF: Placebo-controlled comparison of three dose-regimens of 5-hydroxytryptophan challenge test in healthy volunteers. J Clin Psychopharmacol. 2002 Apr;22(2):183-9. [PubMed Link Image]
Biofluid CSF
Value 0.005 (0.00-0.010) uM
Age Infant:0-1 yr old
Sex Both
Patient information Normal
Comments Not Available
References
  • Spaapen LJ, Bakker JA, Velter C, Loots W, Rubio-Gozalbo ME, Forget PP, Dorland L, De Koning TJ, Poll-The BT, Ploos van Amstel HK, Bekhof J, Blau N, Duran M: Tetrahydrobiopterin-responsive phenylalanine hydroxylase deficiency in Dutch neonates. J Inherit Metab Dis. 2001 Jun;24(3):352-8. [PubMed Link Image]
Biofluid Urine
Value 0.0078 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. Magnussen I, Van Woert MH: Human pharmacokinetics of long term 5-hydroxytryptophan combined with decarboxylase inhibitors. Eur J Clin Pharmacol. 1982;23(1):81-6. [PubMed Link Image]
  2. Li Kam Wa TC, Freestone S, Samson RR, Johnson NR, Lee MR: A comparison of the renal and neuroendocrine effects of two 5-hydroxytryptamine renal prodrugs in normal man. Clin Sci (Lond). 1993 Nov;85(5):607-14. [PubMed Link Image]
  3. Li Kam Wa TC, Freestone S, Samson RR, Johnston NR, Lee MR: Renal metabolism and effects of the glutamyl derivatives of L-dopa and 5-hydroxytryptophan in man. Clin Sci (Lond). 1996 Aug;91(2):177-85. [PubMed Link Image]
  4. Iacono RP, Kuniyoshi SM, Ahlman JR, Zimmerman GJ, Maeda G, Pearlstein RD: Concentrations of indoleamine metabolic intermediates in the ventricular cerebrospinal fluid of advanced Parkinson's patients with severe postural instability and gait disorders. J Neural Transm. 1997;104(4-5):451-9. [PubMed Link Image]
  5. Verbeek MM, Geurtz PB, Willemsen MA, Wevers RA: Aromatic L-amino acid decarboxylase enzyme activity in deficient patients and heterozygotes. Mol Genet Metab. 2007 Apr;90(4):363-9. Epub 2007 Jan 19. [PubMed Link Image]
  6. Turner EH, Loftis JM, Blackwell AD: Serotonin a la carte: supplementation with the serotonin precursor 5-hydroxytryptophan. Pharmacol Ther. 2006 Mar;109(3):325-38. Epub 2005 Jul 14. [PubMed Link Image]
  7. Wikipedia Link Image
Metabolic Enzymes
  1. Aromatic-L-amino-acid decarboxylase
  2. Indoleamine 2,3-dioxygenase
  3. Tryptophan 5-hydroxylase 1
  4. Tryptophan 5-hydroxylase 2
  5. Indoleamine 2,3-dioxygenase-like protein 1
Enzyme 1 [top]
Enzyme 1 ID 5510
Enzyme 1 Name Aromatic-L-amino-acid decarboxylase
Enzyme 1 Synonyms
  1. AADC
  2. DOPA decarboxylase
  3. DDC
Enzyme 1 Gene Name DDC
Enzyme 1 Protein Sequence >Aromatic-L-amino-acid decarboxylase 
MNASEFRRRGKEMVDYVANYMEGIEGRQVYPDVEPGYLRPLIPAAAPQEPDTFEDIINDV
EKIIMPGVTHWHSPYFFAYFPTASSYPAMLADMLCGAIGCIGFSWAASPACTELETVMMD
WLGKMLELPKAFLNEKAGEGGGVIQGSASEATLVALLAARTKVIHRLQAASPELTQAAIM
EKLVAYSSDQAHSSVERAGLIGGVKLKAIPSDGNFAMRASALQEALERDKAAGLIPFFMV
ATLGTTTCCSFDNLLEVGPICNKEDIWLHVDAAYAGSAFICPEFRHLLNGVEFADSFNFN
PHKWLLVNFDCSAMWVKKRTDLTGAFRLDPTYLKHSHQDSGLITDYRHWQIPLGRRFRSL
KMWFVFRMYGVKGLQAYIRKHVQLSHEFESLVRQDPRFEICVEVILGLVCFRLKGSNKVN
EALLQRINSAKKIHLVPCHLRDKFVLRFAICSRTVESAHVQRAWEHIKELAADVLRAERE
Enzyme 1 Number of Residues 480
Enzyme 1 Molecular Weight 53895
Enzyme 1 Theoretical pI 7.21
Enzyme 1 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 1 General Function Amino acid transport and metabolism
Enzyme 1 Specific Function Catalyzes the decarboxylation of L-3,4- dihydroxyphenylalanine (DOPA) to dopamine, L-5-hydroxytryptophan to serotonin and L-tryptophan to tryptamine
Enzyme 1 Pathways
Enzyme 1 Reactions
  • L-tryptophan = tryptamine + CO2
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 181521 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P20711 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name DDC_HUMAN Link Image
Enzyme 1 PDB ID 1JS3 Link Image
Enzyme 1 PDB File Show
Enzyme 1 3D Structure
Enzyme 1 Cellular Location Not Available
Enzyme 1 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 1 GenBank Gene ID M76180 Link Image
Enzyme 1 GeneCard ID DDC Link Image
Enzyme 1 GenAtlas ID DDC Link Image
Enzyme 1 HGNC ID HGNC:2719 Link Image
Enzyme 1 Chromosome Location 7
Enzyme 1 Locus 7p11
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 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 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5674
Enzyme 2 Name Indoleamine 2,3-dioxygenase
Enzyme 2 Synonyms
  1. IDO
  2. Indoleamine-pyrrole 2,3-dioxygenase
Enzyme 2 Gene Name INDO
Enzyme 2 Protein Sequence >Indoleamine 2,3-dioxygenase 
MAHAMENSWTISKEYHIDEEVGFALPNPQENLPDFYNDWMFIAKHLPDLIESGQLRERVE
KLNMLSIDHLTDHKSQRLARLVLGCITMAYVWGKGHGDVRKVLPRNIAVPYCQLSKKLEL
PPILVYADCVLANWKKKDPNKPLTYENMDVLFSFRDGDCSKGFFLVSLLVEIAAASAIKV
IPTVFKAMQMQERDTLLKALLEIASCLEKALQVFHQIHDHVNPKAFFSVLRIYLSGWKGN
PQLSDGLVYEGFWEDPKEFAGGSAGQSSVFQCFDVLLGIQQTAGGGHAAQFLQDMRRYMP
PAHRNFLCSLESNPSVREFVLSKGDAGLREAYDACVKALVSLRSYHLQIVTKYILIPASQ
QPKENKTSEDPSKLEAKGTGGTDLMNFLKTVRSTTEKSLLKEG
Enzyme 2 Number of Residues 403
Enzyme 2 Molecular Weight 45327
Enzyme 2 Theoretical pI 7.33
Enzyme 2 GO Classification
Function
  • binding
  • heme binding
  • tetrapyrrole binding
Process
—
Component
—
Enzyme 2 General Function Not Available
Enzyme 2 Specific Function Catalyzes the cleavage of the pyrrol ring of tryptophan and incorporates both atoms of a molecule of oxygen
Enzyme 2 Pathways Not Available
Enzyme 2 Reactions Not Available
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 306956 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P14902 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name I23O_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1212 bp 
ATGGCACACGCTATGGAAAACTCCTGGACAATCAGTAAAGAGTACCATATTGATGAAGAA
GTGGGCTTTGCTCTGCCAAATCCACAGGAAAATCTACCTGATTTTTATAATGACTGGATG
TTCATTGCTAAACATCTGCCTGATCTCATAGAGTCTGGCCAGCTTCGAGAAAGAGTTGAG
AAGTTAAACATGCTCAGCATTGATCATCTCACAGACCACAAGTCACAGCGCCTTGCACGT
CTAGTTCTGGGATGCATCACCATGGCATATGTGTGGGGCAAAGGTCATGGAGATGTCCGT
AAGGTCTTGCCAAGAAATATTGCTGTTCCTTACTGCCAACTCTCCAAGAAACTGGAACTG
CCTCCTATTTTGGTTTATGCAGACTGTGTCTTGGCAAACTGGAAGAAAAAGGATCCTAAT
AAGCCCCTGACTTATGAGAACATGGACGTTTTGTTCTCATTTCGTGATGGAGACTGCAGT
AAAGGATTCTTCCTGGTCTCTCTATTGGTGGAAATAGCAGCTGCTTCTGCAATCAAAGTA
ATTCCTACTGTATTCAAGGCAATGCAAATGCAAGAACGGGACACTTTGCTAAAGGCGCTG
TTGGAAATAGCTTCTTGCTTGGAGAAAGCCCTTCAAGTGTTTCACCAAATCCACGATCAT
GTGAACCCAAAAGCATTTTTCAGTGTTCTTCGCATATATTTGTCTGGCTGGAAAGGCAAC
CCCCAGCTATCAGACGGTCTGGTGTATGAAGGGTTCTGGGAAGACCCAAAGGAGTTTGCA
GGGGGCAGTGCAGGCCAAAGCAGCGTCTTTCAGTGCTTTGACGTCCTGCTGGGCATCCAG
CAGACTGCTGGTGGAGGACATGCTGCTCAGTTCCTCCAGGACATGAGAAGATATATGCCA
CCAGCTCACAGGAACTTCCTGTGCTCATTAGAGTCAAATCCCTCAGTCCGTGAGTTTGTC
CTTTCAAAAGGTGATGCTGGCCTGCGGGAAGCTTATGACGCCTGTGTGAAAGCTCTGGTC
TCCCTGAGGAGCTACCATCTGCAAATCGTGACTAAGTACATCCTGATTCCTGCAAGCCAG
CAGCCAAAGGAGAATAAGACCTCTGAAGACCCTTCAAAACTGGAAGCCAAAGGAACTGGA
GGCACTGATTTAATGAATTTCCTGAAGACTGTGAGAAGTACAACTGAGAAATCCCTTTTG
AAGGAAGGTTAA
Enzyme 2 GenBank Gene ID M34455 Link Image
Enzyme 2 GeneCard ID INDO Link Image
Enzyme 2 GenAtlas ID INDO Link Image
Enzyme 2 HGNC ID HGNC:6059 Link Image
Enzyme 2 Chromosome Location 8
Enzyme 2 Locus 8p12-p11
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Dai W, Gupta SL: Molecular cloning, sequencing and expression of human interferon-gamma-inducible indoleamine 2,3-dioxygenase cDNA. Biochem Biophys Res Commun. 1990 Apr 16;168(1):1-8. [PubMed Link Image]
  2. Tone S, Takikawa O, Habara-Ohkubo A, Kadoya A, Yoshida R, Kido R: Primary structure of human indoleamine 2,3-dioxygenase deduced from the nucleotide sequence of its cDNA. Nucleic Acids Res. 1990 Jan 25;18(2):367. [PubMed Link Image]
  3. Kadoya A, Tone S, Maeda H, Minatogawa Y, Kido R: Gene structure of human indoleamine 2,3-dioxygenase. Biochem Biophys Res Commun. 1992 Nov 30;189(1):530-6. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5709
Enzyme 3 Name Tryptophan 5-hydroxylase 1
Enzyme 3 Synonyms
  1. Tryptophan 5-monooxygenase 1
Enzyme 3 Gene Name TPH1
Enzyme 3 Protein Sequence >Tryptophan 5-hydroxylase 1 
MIEDNKENKDHSLERGRASLIFSLKNEVGGLIKALKIFQEKHVNLLHIESRKSKRRNSEF
EIFVDCDINREQLNDIFHLLKSHTNVLSVNLPDNFTLKEDGMETVPWFPKKISDLDHCAN
RVLMYGSELDADHPGFKDNVYRKRRKYFADLAMNYKHGDPIPKVEFTEEEIKTWGTVFQE
LNKLYPTHACREYLKNLPLLSKYCGYREDNIPQLEDVSNFLKERTGFSIRPVAGYLSPRD
FLSGLAFRVFHCTQYVRHSSDPFYTPEPDTCHELLGHVPLLAEPSFAQFSQEIGLASLGA
SEEAVQKLATCYFFTVEFGLCKQDGQLRVFGAGLLSSISELKHALSGHAKVKPFDPKITC
KQECLITTFQDVYFVSESFEDAKEKMREFTKTIKRPFGVKYNPYTRSIQILKDTKSITSA
MNELQHDLDVVSDALAKVSRKPSI
Enzyme 3 Number of Residues 444
Enzyme 3 Molecular Weight 50986
Enzyme 3 Theoretical pI 7.23
Enzyme 3 GO Classification
Function
  • amine binding
  • amino acid binding
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • iron ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced pteridine as one donor, and incorporation of one atom of oxygen
  • transition metal ion binding
  • tryptophan 5-monooxygenase activity
Process
  • amino acid and derivative metabolism
  • amino acid metabolism
  • aromatic amino acid family metabolism
  • cellular metabolism
  • metabolism
  • neurotransmitter biosynthesis
  • neurotransmitter metabolism
  • physiological process
  • serotonin biosynthesis
Component
—
Enzyme 3 General Function Amino acid transport and metabolism
Enzyme 3 Specific Function L-tryptophan + tetrahydrobiopterin + O(2) = 5- hydroxy-L-tryptophan + 4a-hydroxytetrahydrobiopterin
Enzyme 3 Pathways
Enzyme 3 Reactions
  • L-tryptophan + tetrahydrobiopterin + O2 = 5-hydroxy-L-tryptophan + 4a-hydroxytetrahydrobiopterin
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 37955 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P17752 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name TPH1_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1335 bp 
ATGATTGAAGACAATAAGGAGAACAAAGACCATTCCTTAGAAAGGGGAAGAGCAAGTCTC
ATTTTTTCCTTAAAGAATGAAGTTGGAGGACTTATAAAAGCCCTGAAAATCTTTCAGGAG
AAGCATGTGAATCTGTTACATATCGAGTCCCGAAAATCAAAAAGAAGAAACTCAGAATTT
GAGATTTTTGTTGACTGTGACATCAACAGAGAACAATTGAATGATATTTTTCATCTGCTG
AAGTCTCATACCAATGTTCTCTCTGTGAATCTACCAGATAATTTTACTTTGAAGGAAGAT
GGTATGGAAACTGTTCCTTGGTTTCCAAAGAAGATTTCTGACCTGGACCATTGTGCCAAC
AGAGTTCTGATGTATGGATCTGAACTAGATGCAGACCATCCTGGCTTCAAAGACAATGTC
TACCGTAAACGTCGAAAGTATTTTGCGGACTTGGCTATGAACTATAAACATGGAGACCCC
ATTCCAAAGGTTGAATTCACTGAAGAGGAGATTAAGACCTGGGGAACCGTATTCCAAGAG
CTCAACAAACTCTACCCAACCCATGCTTGCAGAGAGTATCTCAAAAACTTACCTTTGCTT
TCTAAATATTGTGGATATCGGGAGGATAATATCCCACAATTGGAAGATGTCTCCAACTTT
TTAAAAGAGCGTACAGGTTTTTCCATCCGTCCTGTGGCTGGTTACTTATCACCAAGAGAT
TTCTTATCAGGTTTAGCCTTTCGAGTTTTTCACTGCACTCAATATGTGAGACACAGTTCA
GATCCCTTCTATACCCCAGAGCCAGATACCTGCCATGAACTCTTAGGTCATGTCCCGCTT
TTGGCTGAACCTAGTTTTGCCCAATTCTCCCAAGAAATTGGCTTGGCTTCTCTTGGCGCT
TCAGAGGAGGCTGTTCAAAAACTGGCAACGTGCTACTTTTTCACTGTGGAGTTTGGTCTA
TGTAAACAAGATGGACAGCTAAGAGTCTTTGGTGCTGGCTTACTTTCTTCTATCAGTGAA
CTCAAACATGCACTTTCTGGACATGCCAAAGTAAAGCCCTTTGATCCCAAGATTACCTGC
AAACAGGAATGTCTTATCACAACTTTTCAAGATGTCTACTTTGTATCTGAAAGTTTTGAA
GATGCAAAGGAGAAGATGAGAGAATTTACCAAAACAATTAAGCGTCCATTTGGAGTGAAG
TATAATCCATATACACGGAGTATTCAGATCCTGAAAGACACCAAGAGCATAACCAGTGCC
ATGAATGAGCTGCAGCATGATCTCGATGTTGTCAGTGATGCCCTTGCTAAGGTCAGCAGG
AAGCCGAGTATCTAA
Enzyme 3 GenBank Gene ID X52836 Link Image
Enzyme 3 GeneCard ID TPH1 Link Image
Enzyme 3 GenAtlas ID TPH1 Link Image
Enzyme 3 HGNC ID HGNC:12008 Link Image
Enzyme 3 Chromosome Location 11
Enzyme 3 Locus 11p15.3-p14
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Boularand S, Darmon MC, Ganem Y, Launay JM, Mallet J: Complete coding sequence of human tryptophan hydroxylase. Nucleic Acids Res. 1990 Jul 25;18(14):4257. [PubMed Link Image]
  2. Tipper JP, Citron BA, Ribeiro P, Kaufman S: Cloning and expression of rabbit and human brain tryptophan hydroxylase cDNA in Escherichia coli. Arch Biochem Biophys. 1994 Dec;315(2):445-53. [PubMed Link Image]
  3. Wang GA, Coon SL, Kaufman S: Alternative splicing at the 3'-cDNA of human tryptophan hydroxylase. J Neurochem. 1998 Oct;71(4):1769-72. [PubMed Link Image]
  4. Wang L, Erlandsen H, Haavik J, Knappskog PM, Stevens RC: Three-dimensional structure of human tryptophan hydroxylase and its implications for the biosynthesis of the neurotransmitters serotonin and melatonin. Biochemistry. 2002 Oct 22;41(42):12569-74. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5711
Enzyme 4 Name Tryptophan 5-hydroxylase 2
Enzyme 4 Synonyms
  1. Tryptophan 5-monooxygenase 2
  2. Neuronal tryptophan hydroxylase
Enzyme 4 Gene Name TPH2
Enzyme 4 Protein Sequence >Tryptophan 5-hydroxylase 2 
MQPAMMMFSSKYWARRGFSLDSAVPEEHQLLGSSTLNKPNSGKNDDKGNKGSSKREAATE
SGKTAVVFSLKNEVGGLVKALRLFQEKRVNMVHIESRKSRRRSSEVEIFVDCECGKTEFN
ELIQLLKFQTTIVTLNPPENIWTEEEELEDVPWFPRKISELDKCSHRVLMYGSELDADHP
GFKDNVYRQRRKYFVDVAMGYKYGQPIPRVEYTEEETKTWGVVFRELSKLYPTHACREYL
KNFPLLTKYCGYREDNVPQLEDVSMFLKERSGFTVRPVAGYLSPRDFLAGLAYRVFHCTQ
YIRHGSDPLYTPEPDTCHELLGHVPLLADPKFAQFSQEIGLASLGASDEDVQKLATCYFF
TIEFGLCKQEGQLRAYGAGLLSSIGELKHALSDKACVKAFDPKTTCLQECLITTFQEAYF
VSESFEEAKEKMRDFAKSITRPFSVYFNPYTQSIEILKDTRSIENVVQDLRSDLNTVCDA
LNKMNQYLGI
Enzyme 4 Number of Residues 490
Enzyme 4 Molecular Weight 56057
Enzyme 4 Theoretical pI 6.36
Enzyme 4 GO Classification
Function
  • amine binding
  • amino acid binding
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • iron ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced pteridine as one donor, and incorporation of one atom of oxygen
  • transition metal ion binding
  • tryptophan 5-monooxygenase activity
Process
  • amino acid and derivative metabolism
  • amino acid metabolism
  • aromatic amino acid family metabolism
  • cellular metabolism
  • metabolism
  • neurotransmitter biosynthesis
  • neurotransmitter metabolism
  • physiological process
  • serotonin biosynthesis
Component
—
Enzyme 4 General Function Amino acid transport and metabolism
Enzyme 4 Specific Function L-tryptophan + tetrahydrobiopterin + O(2) = 5- hydroxy-L-tryptophan + 4a-hydroxytetrahydrobiopterin
Enzyme 4 Pathways
Enzyme 4 Reactions
  • L-tryptophan + tetrahydrobiopterin + O2 = 5-hydroxy-L-tryptophan + 4a-hydroxytetrahydrobiopterin
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 27497159 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q8IWU9 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name TPH2_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1473 bp 
ATGCAGCCAGCAATGATGATGTTTTCCAGTAAATACTGGGCACGGAGAGGGTTTTCCCTG
GATTCAGCAGTGCCCGAAGAGCATCAGCTACTTGGCAGCTCAACACTAAATAAACCTAAC
TCTGGCAAAAATGACGACAAAGGCAACAAGGGAAGCAGCAAACGTGAAGCTGCTACCGAA
AGTGGCAAGACAGCAGTTGTTTTCTCCTTGAAGAATGAAGTTGGTGGATTGGTAAAAGCA
CTGAGGCTCTTTCAGGAAAAACGTGTCAACATGGTTCATATTGAATCCAGGAAATCTCGG
CGAAGAAGTTCTGAGGTTGAAATCTTTGTGGACTGTGAGTGTGGGAAAACAGAATTCAAT
GAGCTCATTCAGTTGCTGAAATTTCAAACCACTATTGTGACGCTGAATCCTCCAGAGAAC
ATTTGGACAGAGGAAGAAGAGCTAGAGGATGTGCCCTGGTTCCCTCGGAAGATCTCTGAG
TTAGACAAATGCTCTCACAGAGTTCTCATGTATGGTTCTGAGCTTGATGCTGACCACCCA
GGATTTAAGGACAATGTCTATCGACAGAGAAGAAAGTATTTTGTGGATGTGGCCATGGGT
TATAAATATGGTCAGCCCATTCCCAGGGTGGAGTATACTGAAGAAGAAACTAAAACTTGG
GGTGTTGTATTCCGGGAGCTCTCCAAACTCTATCCCACTCATGCTTGCCGAGAGTATTTG
AAAAACTTCCCTCTGCTGACTAAATACTGTGGCTACAGAGAGGACAATGTGCCTCAACTC
GAAGATGTCTCCATGTTTCTGAAAGAAAGGTCTGGCTTCACGGTGAGGCCGGTGGCTGGA
TACCTGAGCCCACGAGACTTTCTGGCAGGACTGGCCTACAGAGTGTTCCACTGTACCCAG
TACATCCGGCATGGCTCAGATCCCCTCTACACCCCAGAACCAGACACATGCCATGAACTC
TTGGGACATGTTCCACTACTTGCGGATCCTAAGTTTGCTCAGTTTTCACAAGAAATAGGT
CTGGCGTCTCTGGGAGCATCAGATGAAGATGTTCAGAAACTAGCCACGTGCTATTTCTTC
ACAATCGAGTTTGGCCTTTGCAAGCAAGAAGGGCAACTGCGGGCATATGGAGCAGGACTC
CTTTCCTCCATTGGAGAATTAAAGCACGCCCTTTCTGACAAGGCATGTGTGAAAGCCTTT
GACCCAAAGACAACTTGCTTACAGGAATGCCTTATCACCACCTTCCAGGAAGCCTACTTT
GTTTCAGAAAGTTTTGAAGAAGCCAAAGAAAAGATGAGGGACTTTGCAAAGTCAATTACC
CGTCCCTTCTCAGTATACTTCAATCCCTACACACAGAGTATTGAAATTCTGAAAGACACC
AGAAGTATTGAAAATGTGGTGCAGGACCTTCGCAGCGACTTGAATACAGTGTGTGATGCT
TTAAACAAAATGAACCAATATCTGGGGATTTGA
Enzyme 4 GenBank Gene ID AY098914 Link Image
Enzyme 4 GeneCard ID TPH2 Link Image
Enzyme 4 GenAtlas ID TPH2 Link Image
Enzyme 4 HGNC ID HGNC:20692 Link Image
Enzyme 4 Chromosome Location 12
Enzyme 4 Locus 12q21.1
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Walther DJ, Peter JU, Bashammakh S, Hortnagl H, Voits M, Fink H, Bader M: Synthesis of serotonin by a second tryptophan hydroxylase isoform. Science. 2003 Jan 3;299(5603):76. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 13115
Enzyme 5 Name Indoleamine 2,3-dioxygenase-like protein 1
Enzyme 5 Synonyms
  1. Indoleamine-pyrrole 2,3-dioxygenase-like protein 1
Enzyme 5 Gene Name INDOL1
Enzyme 5 Protein Sequence >Indoleamine 2,3-dioxygenase-like protein 1 
MEPHRPNVKTAVPLSLESYHISEEYGFLLPDSLKELPDHYRPWMEIANKLPQLIDAHQLQ
AHVDKMPLLSCQFLKGHREQRLAHLVLSFLTMGYVWQEGEAQPAEVLPRNLALPFVEVSR
NLGLPPILVHSDLVLTNWTKKDPDGNLETIISFPGGESLHGFILVTALVEKEAVPGIKAL
VQATNAILQPNQEALLQALQRLRLSIQDITKTLGQMHDYVDPDIFYAGIRIFLSGWKDNP
AMPAGLMYEGVSQEPLKYSGGSAAQSTVLHAFDEFLGIRHSKESGDFLYRMRDYMPPSHK
AFIEDIHSAPSLRDYILSSGQDHLLTAYNQCVQALAELRSYHITMVTKYLITAAAKAKHG
KPNHLPGPPQALKDRGTGGTAVMSFLKSVRDKTLESILHPRG
Enzyme 5 Number of Residues 402
Enzyme 5 Molecular Weight 44865
Enzyme 5 Theoretical pI 6.94
Enzyme 5 GO Classification
Function
  • binding
  • heme binding
  • tetrapyrrole binding
Process
—
Component
—
Enzyme 5 General Function Not Available
Enzyme 5 Specific Function Not Available
Enzyme 5 Pathways Not Available
Enzyme 5 Reactions Not Available
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 34536196 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID Q6ZQW0 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name I23OL_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence Not Available
Enzyme 5 GenBank Gene ID AK128691 Link Image
Enzyme 5 GeneCard ID Q6ZQW0 Link Image
Enzyme 5 GenAtlas ID INDOL1 Link Image
Enzyme 5 HGNC ID HGNC:27269 Link Image
Enzyme 5 Chromosome Location Not Available
Enzyme 5 Locus Not Available
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References Not Available
Enzyme 5 Metabolite References Not Available