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Human Metabolome Database Version 2.5

 

Showing metabocard for L-Tryptophan (HMDB00929)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2010-06-07 11:34:30
Accession Number HMDB00929
Secondary Accession Numbers Not Available
Common Name L-Tryptophan
Description Tryptophan is an essential amino acid which is the precursor of serotonin. Serotonin is a brain neurotransmitter, platelet clotting factor and neurohormone found in organs throughout the body. Metabolism of tryptophan to serotonin requires nutrients such as vitamin B6, niacin and glutathione. Niacin is an important metabolite of tryptophan. High corn or other tryptophan-deficient diets can cause pellagra, which is a niacin-tryptophan deficiency disease with symptoms of dermatitis, diarrhea and dementia. Inborn errors of tryptophan metabolism exist where a tumor (carcinoid) makes excess serotonin. Hartnup's disease is a disease where tryptophan and other amino acids are not absorbed properly. Tryptophan supplements may be useful in each condition, in carcinoid replacing the over-metabolized nutrient and in Hartnup's supplementing a malabsorbed nutrient. Some disorders of excess tryptophan in the blood may contribute to mental retardation. Assessment of tryptophan deficiency is done through studying excretion of tryptophan metabolites in the urine or blood. Blood may be the most sensitive test because the amino acid tryptophan is transported in a unique way. Increased urination of tryptophan fragments correlates with increased tryptophan degradation, which occurs with oral contraception, depression, mental retardation, hypertension and anxiety states. The requirement for tryptophan and protein decreases with age. Adults' minimum daily requirement is 3 mg/kg/day or about 200 mg a day. This may be an underestimation, for there are 400 mg of tryptophan in just a cup of wheat germ. A cup of low fat cottage cheese contains 300 mg of tryptophan and chicken and turkey contain up to 600 mg per pound. (http://www.dcnutrition.com)
Synonyms
  1. (-)-tryptophan
  2. (2S)-2-amino-3-(1H-indol-3-yl)propanoic acid
  3. (S)-1H-Indole-3-alanine
  4. (S)-2-Amino-3-(3-indolyl)propionic acid
  5. (S)-a-Amino-1H-indole-3-propanoate
  6. (S)-a-Amino-1H-indole-3-propanoic acid
  7. (S)-a-Aminoindole-3-propionate
  8. (S)-a-Aminoindole-3-propionic acid
  9. (S)-alpha-Amino-1H-indole-3-propanoic acid
  10. (S)-alpha-Amino-beta-(3-indolyl)-propionic acid
  11. (S)-alpha-Aminoindole-3-propionic acid
  12. (l)-tryptophan
  13. (s)-a-amino-b-indolepropionate
  14. (s)-a-amino-b-indolepropionic acid
  15. (s)-alpha-amino-beta-indolepropionic acid
  16. (s)-tryptophan
  17. 1-beta-3-Indolylalanine
  18. 1H-Indole-3-Alanine
  19. 1beta-3-Indolylalanine
  20. 2-Amino-3-indolylpropanoate
  21. 2-Amino-3-indolylpropanoic acid
  22. 3-Indol-3-ylalanine
  23. Ardeytropin
  24. H-TRP-oh
  25. Indole-3-alanine
  26. Kalma
  27. L-(-)-tryptophan
  28. L-Tryptophan
  29. 3-(1H-indol-3-yl)-L-Alanine
  30. L-alpha-amino-3-indolepropionic acid
  31. L-alpha-aminoindole-3-propionic acid
  32. L-beta-3-indolylalanine
  33. L-tryptofan
  34. L-tryptophane
  35. Lopac-T-0254
  36. Lyphan
  37. Optimax
  38. Pacitron
  39. Sedanoct
  40. Triptofano
  41. Trofan
  42. Tryptacin
  43. Tryptan
  44. Tryptophan
  45. Tryptophane
  46. Tryptophanum
  47. alpha'-Amino-3-indolepropionic acid
  48. alpha-Aminoindole-3-propionic acid
  49. l-b-3-Indolylalanine
  50. (S)-alpha-Amino-1H-indole-3-propanoate
  51. (S)-alpha-Aminoindole-3-propionate
  52. (s)-alpha-amino-beta-indolepropionate
  53. (2S)-2-amino-3-(1H-indol-3-yl)propanoate
Chemical IUPAC Name (2S)-2-amino-3-(1H-indol-3-yl)propanoic acid
Chemical Formula C11H12N2O2
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
  • primary amine
  • primary aliphatic amine (alkylamine)
  • carboxylic acid
  • aromatic compound
  • heterocyclic compound
  • alpha-aminoacid
Biofunction
  • Essential amino acid
  • Component of Aminoacyl-tRNA biosynthesis
  • 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
  • Exogenous
Average Molecular Weight 204.225
Monoisotopic Molecular Weight 204.089874
Isomeric SMILES N[C@@H](CC1=CNC2=CC=CC=C12)C(O)=O
Canonical SMILES NC(CC1=CNC2=CC=CC=C12)C(O)=O
KEGG Compound ID C00078 Link Image
BioCyc ID TRP Link Image
BiGG ID 33772 Link Image
Wikipedia Link Kalma Link Image
NuGOwiki Link HMDB00929 Link Image
Metagene Link HMDB00929 Link Image
METLIN ID 5879 Link Image
PubChem Compound 6305 Link Image
PubChem Substance 10322924 Link Image
ChEBI ID 27897 Link Image
CAS Registry Number 73-22-3
InChI Identifier InChI=1/C11H12N2O2/c12-9(11(14)15)5-7-6-13-10-4-2-1-3-8(7)10/h1-4,6,9,13H,5,12H2,(H,14,15)/t9-/m0/s1
Synthesis Reference Amir-Heidari, Bagher; Thirlway, Jenny; Micklefield, Jason. Stereochemical course of tryptophan dehydrogenation during biosynthesis of the calcium-dependent lipopeptide antibiotics. Organic Letters (2007), 9(8), 1513-1516.
Melting Point (Experimental) 230 oC
Experimental Water Solubility 13.4 mg/mL at 25 oC [YALKOWSKY,SH & DANNENFELSER,RM (1992)]; 23.5 mg/mL [HMP experimental] Source: PhysProp
Predicted Water Solubility 1.36 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity -1.06 [HANSCH,C ET AL. (1995)] Source: PhysProp
Predicted LogP/Hydrophobicity -1.10 [Predicted by ALOGPS]; -1.3 [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 1GC3 Link Image
Experimental PDB File Show
Experimental PDB Structure
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Varian)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
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 LogP)
  • Extracellular
Biofluid Location
  • Blood
  • Cerebrospinal Fluid
  • Saliva
  • Urine
Tissue Location
Tissue References
Fibroblasts —
Nerve Cells —
Concentrations (Normal)
Biofluid Blood
Value 44.0 (37.0-51.0) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Cynober LA: Plasma amino acid levels with a note on membrane transport: characteristics, regulation, and metabolic significance. Nutrition. 2002 Sep;18(9):761-6. [PubMed Link Image]
Biofluid Blood
Value 48.7 +/- 11.6 uM
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 85-100. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid Blood
Value 101.5 +/- 27.2 uM
Age Newborn:0-30 days old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 85-100. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid Blood
Value 45.0 +/- 9.0 uM
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 85-100. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid CSF
Value 1.3 +/- 0.4 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid CSF
Value 2.32 +/- 0.09 uM
Age Adult:>18 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Heyes MP, Saito K, Crowley JS, Davis LE, Demitrack MA, Der M, Dilling LA, Elia J, Kruesi MJ, Lackner A, et al.: Quinolinic acid and kynurenine pathway metabolism in inflammatory and non-inflammatory neurological disease. Brain. 1992 Oct;115 ( Pt 5):1249-73. [PubMed Link Image]
Biofluid CSF
Value 20.4 +/- 8.2 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Peng CT, Wu KH, Lan SJ, Tsai JJ, Tsai FJ, Tsai CH: Amino acid concentrations in cerebrospinal fluid in children with acute lymphoblastic leukemia undergoing chemotherapy. Eur J Cancer. 2005 May;41(8):1158-63. Epub 2005 Apr 14. [PubMed Link Image]
Biofluid CSF
Value 2.0 +/- 0.53 uM
Age Adult:>18 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Botez MI, Young SN: Biogenic amine metabolites and thiamine in cerebrospinal fluid in heredo-degenerative ataxias. Can J Neurol Sci. 2001 May;28(2):134-40. [PubMed Link Image]
Biofluid CSF
Value 2.0 (1.2-2.5) uM
Age Adult:>18 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Koskiniemi M, Laakso J, Kuurne T, Laipio M, Harkonen M: Indole levels in human lumbar and ventricular cerebrospinal fluid and the effect of L-tryptophan administration. Acta Neurol Scand. 1985 Feb;71(2):127-32. [PubMed Link Image]
Biofluid CSF
Value 5 +/- 3 uM
Age N/A
Sex Both
Patient information Normal
Comments Not Available
References
  • Wishart DS, Lewis MJ, Morrissey JA, Flegel MD, Jeroncic K, Xiong Y, Cheng D, Eisner R, Gautam B, Tzur D, Sawhney S, Bamforth F, Greiner R, Li L: The human cerebrospinal fluid metabolome. J Chromatogr B Analyt Technol Biomed Life Sci. 2008 Aug 15;871(2):164-173. Epub 2008 May 8. [PubMed Link Image]
Biofluid CSF
Value 2.64 +/- 0.52 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Do KQ, Lauer CJ, Schreiber W, Zollinger M, Gutteck-Amsler U, Cuenod M, Holsboer F: gamma-Glutamylglutamine and taurine concentrations are decreased in the cerebrospinal fluid of drug-naive patients with schizophrenic disorders. J Neurochem. 1995 Dec;65(6):2652-62. [PubMed Link Image]
Biofluid Saliva
Value 0.5 +/- 0.5 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Buczko W, Cylwik D, Stokowska W: [Metabolism of tryptophan via the kynurenine pathway in saliva] Postepy Hig Med Dosw (Online). 2005;59:283-9. [PubMed Link Image]
Biofluid Urine
Value 13.52 +/- 7.37 umol/mmol creatinine
Age Infant:0-1 yr old
Sex Both
Patient information Normal
Comments Not Available
References
  • Shoemaker JD, Elliott WH: Automated screening of urine samples for carbohydrates, organic and amino acids after treatment with urease. J Chromatogr. 1991 Jan 2;562(1-2):125-38. [PubMed Link Image]
Biofluid Urine
Value 7.84 +/- 8.63 umol/mmol creatinine
Age Adult:>18 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
Biofluid Urine
Value 5.263 (1.316-9.211) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Doctor's Data
Biofluid Urine
Value 7.8 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 44 +/- 29 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Shaykhutdinov RA, MacInnis GD, Dowlatabadi R, Weljie AM, Vogel HJ. Quantitative analysis of metabolite concentrations in human urine samples using 13C{1H} NMR spectroscopy. Metabolomics. 2009
Concentrations (Abnormal)
Biofluid Blood
Value 31.6 (29.6-33.6) uM
Age Adult:>18 yrs old
Sex Both
Condition Epilepsy
Comments Acute seizures
References
  • Rainesalo S, Keranen T, Palmio J, Peltola J, Oja SS, Saransaari P: Plasma and cerebrospinal fluid amino acids in epileptic patients. Neurochem Res. 2004 Jan;29(1):319-24. [PubMed Link Image]
Biofluid Blood
Value 37.2 (34.3-40.1) uM
Age Adult:>18 yrs old
Sex Both
Condition Epilepsy
Comments Juvenile myoclonic epilepsy (JME)
References
  • Rainesalo S, Keranen T, Palmio J, Peltola J, Oja SS, Saransaari P: Plasma and cerebrospinal fluid amino acids in epileptic patients. Neurochem Res. 2004 Jan;29(1):319-24. [PubMed Link Image]
Biofluid Blood
Value 53.3 (50.3-56.3) uM
Age Adult:>18 yrs old
Sex Both
Condition Epilepsy
Comments Refractory localization-related epilepsy (RLE)
References
  • Rainesalo S, Keranen T, Palmio J, Peltola J, Oja SS, Saransaari P: Plasma and cerebrospinal fluid amino acids in epileptic patients. Neurochem Res. 2004 Jan;29(1):319-24. [PubMed Link Image]
Biofluid Blood
Value 83.3 +/- 26.0 uM
Age Adult:>18 yrs old
Sex Male
Condition Schizophrenia
Comments Not Available
References
  • Alfredsson G, Wiesel FA: Monoamine metabolites and amino acids in serum from schizophrenic patients before and during sulpiride treatment. Psychopharmacology (Berl). 1989;99(3):322-7. [PubMed Link Image]
Biofluid Blood
Value 80.2 +/- 22.0 uM
Age Adult:>18 yrs old
Sex Female
Condition Schizophrenia
Comments Not Available
References
  • Alfredsson G, Wiesel FA: Monoamine metabolites and amino acids in serum from schizophrenic patients before and during sulpiride treatment. Psychopharmacology (Berl). 1989;99(3):322-7. [PubMed Link Image]
Biofluid Blood
Value 33.06 +/- 8.99 uM
Age Adult:>18 yrs old
Sex Both
Condition Alzheimer's disease
Comments Not Available
References
  • Fonteh AN, Harrington RJ, Tsai A, Liao P, Harrington MG: Free amino acid and dipeptide changes in the body fluids from Alzheimer's disease subjects. Amino Acids. 2007 Feb;32(2):213-24. Epub 2006 Oct 10. [PubMed Link Image]
Biofluid CSF
Value 1.0 +/- 0.2 uM
Age Children:1-13 yrs old
Sex Both
Condition Hartnup disease
Comments Not Available
References
  • Jonas AJ, Butler IJ: Circumvention of defective neutral amino acid transport in Hartnup disease using tryptophan ethyl ester. J Clin Invest. 1989 Jul;84(1):200-4. [PubMed Link Image]
Biofluid CSF
Value 1.7 +/- 0.27 uM
Age Adult:>18 yrs old
Sex Both
Condition Epilepsy
Comments Not Available
References
  • Botez MI, Young SN: Effects of anticonvulsant treatment and low levels of folate and thiamine on amine metabolites in cerebrospinal fluid. Brain. 1991 Feb;114 ( Pt 1A):333-48. [PubMed Link Image]
Biofluid CSF
Value 1.6+/- 0.57 uM
Age Adult:>18 yrs old
Sex Both
Condition Epilepsy
Comments Not Available
References
  • Botez MI, Young SN: Effects of anticonvulsant treatment and low levels of folate and thiamine on amine metabolites in cerebrospinal fluid. Brain. 1991 Feb;114 ( Pt 1A):333-48. [PubMed Link Image]
Biofluid CSF
Value 1.7 +/- 0.4 uM
Age Adult:>18 yrs old
Sex N/A
Condition Epilepsy
Comments Not Available
References
  • Botez MI, Young SN: Effects of anticonvulsant treatment and low levels of folate and thiamine on amine metabolites in cerebrospinal fluid. Brain. 1991 Feb;114 ( Pt 1A):333-48. [PubMed Link Image]
Biofluid CSF
Value 1.68 +/- 0.52 uM
Age Adult:>18 yrs old
Sex Both
Condition Epilepsy
Comments Not Available
References
  • Botez MI, Young SN: Effects of anticonvulsant treatment and low levels of folate and thiamine on amine metabolites in cerebrospinal fluid. Brain. 1991 Feb;114 ( Pt 1A):333-48. [PubMed Link Image]
Biofluid CSF
Value 14.3 +/- 12.5 uM
Age Adult:>18 yrs old
Sex N/A
Condition Epilepsy
Comments Not Available
References
  • Botez MI, Young SN: Effects of anticonvulsant treatment and low levels of folate and thiamine on amine metabolites in cerebrospinal fluid. Brain. 1991 Feb;114 ( Pt 1A):333-48. [PubMed Link Image]
Biofluid CSF
Value 11.5 +/- 8.2 uM
Age Adult:>18 yrs old
Sex N/A
Condition Epilepsy
Comments Not Available
References
  • Botez MI, Young SN: Effects of anticonvulsant treatment and low levels of folate and thiamine on amine metabolites in cerebrospinal fluid. Brain. 1991 Feb;114 ( Pt 1A):333-48. [PubMed Link Image]
Biofluid CSF
Value 13.0 +/- 5.2 uM
Age Children:1-13 yrs old
Sex N/A
Condition Leukemia
Comments Not Available
References
  • Peng CT, Wu KH, Lan SJ, Tsai JJ, Tsai FJ, Tsai CH: Amino acid concentrations in cerebrospinal fluid in children with acute lymphoblastic leukemia undergoing chemotherapy. Eur J Cancer. 2005 May;41(8):1158-63. Epub 2005 Apr 14. [PubMed Link Image]
Biofluid CSF
Value 12.8 +/- 3.5 uM
Age Children:1-13 yrs old
Sex N/A
Condition Leukemia
Comments Acute Lymphoblastic Leukemia (ALL) with Central Nervous System (CNS) disease
References
  • Peng CT, Wu KH, Lan SJ, Tsai JJ, Tsai FJ, Tsai CH: Amino acid concentrations in cerebrospinal fluid in children with acute lymphoblastic leukemia undergoing chemotherapy. Eur J Cancer. 2005 May;41(8):1158-63. Epub 2005 Apr 14. [PubMed Link Image]
Biofluid CSF
Value 2.42 +/- 0.14 uM
Age Adult:>18 yrs old
Sex N/A
Condition Olivopontocerebral atrophy
Comments Not Available
References
  • Botez MI, Young SN: Biogenic amine metabolites and thiamine in cerebrospinal fluid in heredo-degenerative ataxias. Can J Neurol Sci. 2001 May;28(2):134-40. [PubMed Link Image]
Biofluid CSF
Value 1.80 +/- 0.2 uM
Age Adult:>18 yrs old
Sex N/A
Condition Hereditary spastic paraplegia
Comments Not Available
References
  • Botez MI, Young SN: Biogenic amine metabolites and thiamine in cerebrospinal fluid in heredo-degenerative ataxias. Can J Neurol Sci. 2001 May;28(2):134-40. [PubMed Link Image]
Biofluid CSF
Value 1.8 +/- 0.3 uM
Age Adult:>18 yrs old
Sex N/A
Condition Hypothyroidism
Comments Not Available
References
  • Sjoberg S, Eriksson M, Nordin C: L-thyroxine treatment and neurotransmitter levels in the cerebrospinal fluid of hypothyroid patients: a pilot study. Eur J Endocrinol. 1998 Nov;139(5):493-7. [PubMed Link Image]
Biofluid CSF
Value 2.4 +/- 0.13 uM
Age N/A
Sex N/A
Condition Friedreich's ataxia
Comments Not Available
References
  • Botez MI, Young SN: Biogenic amine metabolites and thiamine in cerebrospinal fluid in heredo-degenerative ataxias. Can J Neurol Sci. 2001 May;28(2):134-40. [PubMed Link Image]
Biofluid CSF
Value 0.0018 +/- 0.0003 uM
Age Adult:>18 yrs old
Sex Both
Condition Hypothyroidism
Comments Not Available
References
  • Sjoberg S, Eriksson M, Nordin C: L-thyroxine treatment and neurotransmitter levels in the cerebrospinal fluid of hypothyroid patients: a pilot study. Eur J Endocrinol. 1998 Nov;139(5):493-7. [PubMed Link Image]
Biofluid CSF
Value 1.6 +/- 0.3 uM
Age Adult:>18 yrs old
Sex Both
Condition Hypothyroidism
Comments Not Available
References
  • Sjoberg S, Eriksson M, Nordin C: L-thyroxine treatment and neurotransmitter levels in the cerebrospinal fluid of hypothyroid patients: a pilot study. Eur J Endocrinol. 1998 Nov;139(5):493-7. [PubMed Link Image]
Biofluid CSF
Value 2.67 +/- 0.6 uM
Age Adult:>18 yrs old
Sex Both
Condition Schizophrenia
Comments Not Available
References
  • Do KQ, Lauer CJ, Schreiber W, Zollinger M, Gutteck-Amsler U, Cuenod M, Holsboer F: gamma-Glutamylglutamine and taurine concentrations are decreased in the cerebrospinal fluid of drug-naive patients with schizophrenic disorders. J Neurochem. 1995 Dec;65(6):2652-62. [PubMed Link Image]
Biofluid CSF
Value 1.3 +/- 0.32 uM
Age Adult:>18 yrs old
Sex Both
Condition Alzheimer's disease
Comments Not Available
References
  • Fonteh AN, Harrington RJ, Tsai A, Liao P, Harrington MG: Free amino acid and dipeptide changes in the body fluids from Alzheimer's disease subjects. Amino Acids. 2007 Feb;32(2):213-24. Epub 2006 Oct 10. [PubMed Link Image]
Biofluid Urine
Value 7.83 +/- 7.48 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Condition Cachexia
Comments Not Available
References
Biofluid Urine
Value 1.19 +/- 0.23 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Condition Alzheimer's disease
Comments Not Available
References
  • Fonteh AN, Harrington RJ, Tsai A, Liao P, Harrington MG: Free amino acid and dipeptide changes in the body fluids from Alzheimer's disease subjects. Amino Acids. 2007 Feb;32(2):213-24. Epub 2006 Oct 10. [PubMed Link Image]
Associated Disorders
Condition References
Alzheimer's disease
  • Fonteh AN, Harrington RJ, Tsai A, Liao P, Harrington MG: Free amino acid and dipeptide changes in the body fluids from Alzheimer's disease subjects. Amino Acids. 2007 Feb;32(2):213-24. Epub 2006 Oct 10. [PubMed Link Image]
Cachexia —
Epilepsy
Friedreich's ataxia
  • Botez MI, Young SN: Biogenic amine metabolites and thiamine in cerebrospinal fluid in heredo-degenerative ataxias. Can J Neurol Sci. 2001 May;28(2):134-40. [PubMed Link Image]
Hartnup disease
  • Jonas AJ, Butler IJ: Circumvention of defective neutral amino acid transport in Hartnup disease using tryptophan ethyl ester. J Clin Invest. 1989 Jul;84(1):200-4. [PubMed Link Image]
Hereditary spastic paraplegia
  • Botez MI, Young SN: Biogenic amine metabolites and thiamine in cerebrospinal fluid in heredo-degenerative ataxias. Can J Neurol Sci. 2001 May;28(2):134-40. [PubMed Link Image]
Hypothyroidism
  • Sjoberg S, Eriksson M, Nordin C: L-thyroxine treatment and neurotransmitter levels in the cerebrospinal fluid of hypothyroid patients: a pilot study. Eur J Endocrinol. 1998 Nov;139(5):493-7. [PubMed Link Image]
Leukemia
  • Peng CT, Wu KH, Lan SJ, Tsai JJ, Tsai FJ, Tsai CH: Amino acid concentrations in cerebrospinal fluid in children with acute lymphoblastic leukemia undergoing chemotherapy. Eur J Cancer. 2005 May;41(8):1158-63. Epub 2005 Apr 14. [PubMed Link Image]
Olivopontocerebral atrophy
  • Botez MI, Young SN: Biogenic amine metabolites and thiamine in cerebrospinal fluid in heredo-degenerative ataxias. Can J Neurol Sci. 2001 May;28(2):134-40. [PubMed Link Image]
Schizophrenia
OMIM ID
Pathways
Name SMPDB Link KEGG Link
Transcription/Translation SMP00019 Link Image
Tryptophan Metabolism SMP00063 Link Image map00380 Link Image
General References
  1. Jonas AJ, Butler IJ: Circumvention of defective neutral amino acid transport in Hartnup disease using tryptophan ethyl ester. J Clin Invest. 1989 Jul;84(1):200-4. [PubMed Link Image]
  2. Peng CT, Wu KH, Lan SJ, Tsai JJ, Tsai FJ, Tsai CH: Amino acid concentrations in cerebrospinal fluid in children with acute lymphoblastic leukemia undergoing chemotherapy. Eur J Cancer. 2005 May;41(8):1158-63. Epub 2005 Apr 14. [PubMed Link Image]
  3. Cynober LA: Plasma amino acid levels with a note on membrane transport: characteristics, regulation, and metabolic significance. Nutrition. 2002 Sep;18(9):761-6. [PubMed Link Image]
  4. Rainesalo S, Keranen T, Palmio J, Peltola J, Oja SS, Saransaari P: Plasma and cerebrospinal fluid amino acids in epileptic patients. Neurochem Res. 2004 Jan;29(1):319-24. [PubMed Link Image]
  5. Guchhait RB, Janson C, Price WH: Validity of plasma factor in schizophrenia as measured by tryptophan uptake. Biol Psychiatry. 1975 Jun;10(3):303-14. [PubMed Link Image]
  6. Sjoberg S, Eriksson M, Nordin C: L-thyroxine treatment and neurotransmitter levels in the cerebrospinal fluid of hypothyroid patients: a pilot study. Eur J Endocrinol. 1998 Nov;139(5):493-7. [PubMed Link Image]
  7. Koskiniemi M, Laakso J, Kuurne T, Laipio M, Harkonen M: Indole levels in human lumbar and ventricular cerebrospinal fluid and the effect of L-tryptophan administration. Acta Neurol Scand. 1985 Feb;71(2):127-32. [PubMed Link Image]
  8. Kennedy JS, Gwirtsman HE, Schmidt DE, Johnson BW, Fielstein E, Salomon RM, Shiavi RG, Ebert MH, Parris WC, Loosen PT: Serial cerebrospinal fluid tryptophan and 5-hydroxy indoleacetic acid concentrations in healthy human subjects. Life Sci. 2002 Aug 23;71(14):1703-15. [PubMed Link Image]
  9. Bender KI, Lutsevich NF, Lutsevich AN, Kupchikov VV: [Endogenous metabolites as modulators of the transport of drugs by serum albumin] Farmakol Toksikol. 1990 May-Jun;53(3):72-80. [PubMed Link Image]
  10. Eklundh T, Eriksson M, Sjoberg S, Nordin C: Monoamine precursors, transmitters and metabolites in cerebrospinal fluid: a prospective study in healthy male subjects. J Psychiatr Res. 1996 May-Jun;30(3):201-8. [PubMed Link Image]
  11. Heiman-Patterson TD, Bird SJ, Parry GJ, Varga J, Shy ME, Culligan NW, Edelsohn L, Tatarian GT, Heyes MP, Garcia CA, et al.: Peripheral neuropathy associated with eosinophilia-myalgia syndrome. Ann Neurol. 1990 Oct;28(4):522-8. [PubMed Link Image]
  12. Talbert AM, Tranter GE, Holmes E, Francis PL: Determination of drug-plasma protein binding kinetics and equilibria by chromatographic profiling: exemplification of the method using L-tryptophan and albumin. Anal Chem. 2002 Jan 15;74(2):446-52. [PubMed Link Image]
  13. Dunner DL, Heiber S, Perel JM: The effect of L-tryptophan administration on the concentration of probenecid in plasma and cerebrospinal fluid in patients. Psychopharmacology (Berl). 1977 Aug 16;53(3):305-8. [PubMed Link Image]
  14. Heyes MP, Saito K, Crowley JS, Davis LE, Demitrack MA, Der M, Dilling LA, Elia J, Kruesi MJ, Lackner A, et al.: Quinolinic acid and kynurenine pathway metabolism in inflammatory and non-inflammatory neurological disease. Brain. 1992 Oct;115 ( Pt 5):1249-73. [PubMed Link Image]
  15. George CF, Millar TW, Hanly PJ, Kryger MH: The effect of L-tryptophan on daytime sleep latency in normals: correlation with blood levels. Sleep. 1989 Aug;12(4):345-53. [PubMed Link Image]
  16. Buczko W, Cylwik D, Stokowska W: [Metabolism of tryptophan via the kynurenine pathway in saliva] Postepy Hig Med Dosw (Online). 2005;59:283-9. [PubMed Link Image]
  17. Gutsche B, Grun C, Scheutzow D, Herderich M: Tryptophan glycoconjugates in food and human urine. Biochem J. 1999 Oct 1;343 Pt 1:11-9. [PubMed Link Image]
  18. Wikipedia Link Image
Metabolic Enzymes
  1. Aromatic-L-amino-acid decarboxylase
  2. Indoleamine 2,3-dioxygenase
  3. Tryptophan 2,3-dioxygenase
  4. Tryptophan 5-hydroxylase 1
  5. Tryptophan 5-hydroxylase 2
  6. Tryptophanyl-tRNA synthetase, cytoplasmic
  7. Tryptophanyl-tRNA synthetase, mitochondrial precursor
  8. Indoleamine 2,3-dioxygenase-like protein 1
  9. cDNA FLJ75236, highly similar to Human tryptophan oxygenase
  10. cDNA, FLJ94340, Homo sapiens tryptophanyl tRNA synthetase 2 (mitochondrial)(WARS2), nuclear gene encoding mitochondrial protein, mRNA (Tryptophanyl tRNA synthetase 2 (Mitochondrial), isoform CRA_a)
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 5675
Enzyme 3 Name Tryptophan 2,3-dioxygenase
Enzyme 3 Synonyms
  1. TO
  2. Tryptophan pyrrolase
  3. Tryptophanase
  4. Tryptophan oxygenase
  5. Tryptamin 2,3-dioxygenase
  6. TRPO
Enzyme 3 Gene Name TDO2
Enzyme 3 Protein Sequence >Tryptophan 2,3-dioxygenase 
MSGCPFLGNNFGYTFKKLPVEGSEEDKSQTGVNRASKGGLIYGNYLHLEKVLNAQELQSE
TKGNKIHDEHLFIITHQAYELWFKQILWELDSVREIFQNGHVRDERNMLKVVSRMHRVSV
ILKLLVQQFSILETMTALDFNDFREYLSPASGFQSLQFRLLENKIGVLQNMRVPYNRRHY
RDNFKGEENELLLKSEQEKTLLELVEAWLERTPGLEPHGFNFWGKLEKNITRGLEEEFIR
IQAKEESEEKEEQVAEFQKQKEVLLSLFDEKRHEHLLSKGERRLSYRALQGALMIYFYRE
EPRFQVPFQLLTSLMDIDSLMTKWRYNHVCMVHRMLGSKAGTGGSSGYHYLRSTVSDRYK
VFVDLFNLSTYLIPRHWIPKMNPTIHKFLYTAEYCDSSYFSSDESD
Enzyme 3 Number of Residues 406
Enzyme 3 Molecular Weight 47872
Enzyme 3 Theoretical pI 6.93
Enzyme 3 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on single donors with incorporation of molecular oxygen
  • oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
  • tryptophan 2,3-dioxygenase activity
Process
  • amino acid and derivative metabolism
  • amino acid derivative metabolism
  • biogenic amine metabolism
  • cellular metabolism
  • indolalkylamine metabolism
  • metabolism
  • physiological process
  • tryptophan metabolism
Component
—
Enzyme 3 General Function Amino acid transport and metabolism
Enzyme 3 Specific Function Incorporates oxygen into the indole moiety of tryptophan. Has a broad specificity towards tryptamine and derivatives including D- and L-tryptophan, 5-hydroxytryptophan and serotonin
Enzyme 3 Pathways
Enzyme 3 Reactions
  • L-tryptophan + O2 = L-formylkynurenine
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 993046 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P48775 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name T23O_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1221 bp 
ATGAGTGGGTGCCCATTTTTAGGAAACAACTTTGGATATACTTTTAAAAAACTCCCCGTA
GAAGGCAGCGAAGAAGACAAATCACAAACTGGTGTGAATAGAGCCAGCAAAGGAGGTCTT
ATCTATGGGAACTACCTGCATTTGGAAAAAGTTTTGAATGCACAAGAACTGCAAAGTGAA
ACAAAAGGAAATAAAATCCATGATGAACATCTTTTTATCATAACTCATCAAGCTTATGAA
CTCTGGTTTAAGCAAATCCTCTGGGAGTTGGATTCTGTTCGAGAGATCTTTCAGAATGGC
CATGTCAGAGATGAAAGGAACATGCTTAAGGTTGTTTCTCGGATGCACCGAGTGTCAGTG
ATCCTGAAACTGCTGGTGCAGCAGTTTTCCATTCTGGAGACGATGACAGCCTTGGACTTC
AATGACTTCAGAGAGTACTTATCTCCAGCATCAGGCTTCCAGAGTTTGCAATTCCGACTA
TTAGAAAACAAGATAGGTGTTCTTCAGAACATGAGAGTCCCTTATAACAGAAGACATTAT
CGTGATAACTTCAAAGGAGAAGAAAATGAACTGCTACTTAAATCTGAGCAGGAAAAGACA
CTTCTGGAATTAGTGGAGGCATGGCTGGAAAGAACTCCAGGTTTAGAGCCACATGGATTT
AACTTCTGGGGAAAGCTTGAAAAAAATATCACCAGAGGCCTGGAAGAGGAATTCATAAGG
ATTCAGGCTAAAGAAGAGTCTGAAGAAAAAGAGGAACAGGTGGCTGAATTTCAGAAGCAA
AAAGAGGTGCTACTGTCCTTATTTGATGAGAAACGTCATGAACATCTCCTTAGTAAAGGT
GAAAGACGGCTGTCATACAGAGCACTTCAGGGAGCATTGATGATATATTTTTACAGGGAA
GAGCCTAGGTTCCAGGTGCCTTTTCAGTTGCTGACTTCTCTTATGGACATAGATTCACTG
ATGACCAAATGGAGATATAACCATGTGTGCATGGTGCACAGAATGCTGGGCAGCAAAGCT
GGCACCGGTGGTTCCTCAGGCTATCACTACCTGCGATCAACTGTGAGTGATAGGTACAAG
GTATTTGTAGATTTATTTAATCTTTCAACATACCTGATTCCCCGACACTGGATACCGAAG
ATGAACCCAACCATTCACAAATTTCTATATACAGCAGAATACTGTGATAGCTCCTACTTC
AGCAGTGATGAATCAGATTAA
Enzyme 3 GenBank Gene ID U32989 Link Image
Enzyme 3 GeneCard ID TDO2 Link Image
Enzyme 3 GenAtlas ID TDO2 Link Image
Enzyme 3 HGNC ID HGNC:11708 Link Image
Enzyme 3 Chromosome Location 4
Enzyme 3 Locus 4q31-q32
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Comings DE, Muhleman D, Dietz G, Sherman M, Forest GL: Sequence of human tryptophan 2,3-dioxygenase (TDO2): presence of a glucocorticoid response-like element composed of a GTT repeat and an intronic CCCCT repeat. Genomics. 1995 Sep 20;29(2):390-6. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5709
Enzyme 4 Name Tryptophan 5-hydroxylase 1
Enzyme 4 Synonyms
  1. Tryptophan 5-monooxygenase 1
Enzyme 4 Gene Name TPH1
Enzyme 4 Protein Sequence >Tryptophan 5-hydroxylase 1 
MIEDNKENKDHSLERGRASLIFSLKNEVGGLIKALKIFQEKHVNLLHIESRKSKRRNSEF
EIFVDCDINREQLNDIFHLLKSHTNVLSVNLPDNFTLKEDGMETVPWFPKKISDLDHCAN
RVLMYGSELDADHPGFKDNVYRKRRKYFADLAMNYKHGDPIPKVEFTEEEIKTWGTVFQE
LNKLYPTHACREYLKNLPLLSKYCGYREDNIPQLEDVSNFLKERTGFSIRPVAGYLSPRD
FLSGLAFRVFHCTQYVRHSSDPFYTPEPDTCHELLGHVPLLAEPSFAQFSQEIGLASLGA
SEEAVQKLATCYFFTVEFGLCKQDGQLRVFGAGLLSSISELKHALSGHAKVKPFDPKITC
KQECLITTFQDVYFVSESFEDAKEKMREFTKTIKRPFGVKYNPYTRSIQILKDTKSITSA
MNELQHDLDVVSDALAKVSRKPSI
Enzyme 4 Number of Residues 444
Enzyme 4 Molecular Weight 50986
Enzyme 4 Theoretical pI 7.23
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 37955 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID P17752 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name TPH1_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 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 4 GenBank Gene ID X52836 Link Image
Enzyme 4 GeneCard ID TPH1 Link Image
Enzyme 4 GenAtlas ID TPH1 Link Image
Enzyme 4 HGNC ID HGNC:12008 Link Image
Enzyme 4 Chromosome Location 11
Enzyme 4 Locus 11p15.3-p14
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 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 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5711
Enzyme 5 Name Tryptophan 5-hydroxylase 2
Enzyme 5 Synonyms
  1. Tryptophan 5-monooxygenase 2
  2. Neuronal tryptophan hydroxylase
Enzyme 5 Gene Name TPH2
Enzyme 5 Protein Sequence >Tryptophan 5-hydroxylase 2 
MQPAMMMFSSKYWARRGFSLDSAVPEEHQLLGSSTLNKPNSGKNDDKGNKGSSKREAATE
SGKTAVVFSLKNEVGGLVKALRLFQEKRVNMVHIESRKSRRRSSEVEIFVDCECGKTEFN
ELIQLLKFQTTIVTLNPPENIWTEEEELEDVPWFPRKISELDKCSHRVLMYGSELDADHP
GFKDNVYRQRRKYFVDVAMGYKYGQPIPRVEYTEEETKTWGVVFRELSKLYPTHACREYL
KNFPLLTKYCGYREDNVPQLEDVSMFLKERSGFTVRPVAGYLSPRDFLAGLAYRVFHCTQ
YIRHGSDPLYTPEPDTCHELLGHVPLLADPKFAQFSQEIGLASLGASDEDVQKLATCYFF
TIEFGLCKQEGQLRAYGAGLLSSIGELKHALSDKACVKAFDPKTTCLQECLITTFQEAYF
VSESFEEAKEKMRDFAKSITRPFSVYFNPYTQSIEILKDTRSIENVVQDLRSDLNTVCDA
LNKMNQYLGI
Enzyme 5 Number of Residues 490
Enzyme 5 Molecular Weight 56057
Enzyme 5 Theoretical pI 6.36
Enzyme 5 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 5 General Function Amino acid transport and metabolism
Enzyme 5 Specific Function L-tryptophan + tetrahydrobiopterin + O(2) = 5- hydroxy-L-tryptophan + 4a-hydroxytetrahydrobiopterin
Enzyme 5 Pathways
Enzyme 5 Reactions
  • L-tryptophan + tetrahydrobiopterin + O2 = 5-hydroxy-L-tryptophan + 4a-hydroxytetrahydrobiopterin
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 27497159 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID Q8IWU9 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name TPH2_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 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 5 GenBank Gene ID AY098914 Link Image
Enzyme 5 GeneCard ID TPH2 Link Image
Enzyme 5 GenAtlas ID TPH2 Link Image
Enzyme 5 HGNC ID HGNC:20692 Link Image
Enzyme 5 Chromosome Location 12
Enzyme 5 Locus 12q21.1
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 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 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5846
Enzyme 6 Name Tryptophanyl-tRNA synthetase, cytoplasmic
Enzyme 6 Synonyms
  1. Tryptophan-- tRNA ligase
  2. TrpRS
  3. IFP53
  4. hWRS
Enzyme 6 Gene Name WARS
Enzyme 6 Protein Sequence >Tryptophanyl-tRNA synthetase, cytoplasmic 
MPNSEPASLLELFNSIATQGELVRSLKAGNASKDEIDSAVKMLVSLKMSYKAAAGEDYKA
DCPPGNPAPTSNHGPDATEAEEDFVDPWTVQTSSAKGIDYDKLIVRFGSSKIDKELINRI
ERATGQRPHHFLRRGIFFSHRDMNQVLDAYENKKPFYLYTGRGPSSEAMHVGHLIPFIFT
KWLQDVFNVPLVIQMTDDEKYLWKDLTLDQAYSYAVENAKDIIACGFDINKTFIFSDLDY
MGMSSGFYKNVVKIQKHVTFNQVKGIFGFTDSDCIGKISFPAIQAAPSFSNSFPQIFRDR
TDIQCLIPCAIDQDPYFRMTRDVAPRIGYPKPALLHSTFFPALQGAQTKMSASDPNSSIF
LTDTAKQIKTKVNKHAFSGGRDTIEEHRQFGGNCDVDVSFMYLTFFLEDDDKLEQIRKDY
TSGAMLTGELKKALIEVLQPLIAEHQARRKEVTDEIVKEFMTPRKLSFDFQ
Enzyme 6 Number of Residues 471
Enzyme 6 Molecular Weight 53166
Enzyme 6 Theoretical pI 6.15
Enzyme 6 GO Classification
Function
  • ATP binding
  • RNA ligase activity
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • ligase activity
  • ligase activity, forming phosphoric ester bonds
  • nucleotide binding
  • purine nucleotide binding
  • tRNA ligase activity
  • tryptophan-tRNA ligase activity
Process
  • RNA metabolism
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
  • tRNA aminoacylation
  • tRNA aminoacylation for protein translation
  • tRNA metabolism
  • tryptophanyl-tRNA aminoacylation
Component
—
Enzyme 6 General Function Translation, ribosomal structure and biogenesis
Enzyme 6 Specific Function ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + L-tryptophyl-tRNA(Trp)
Enzyme 6 Pathways
Enzyme 6 Reactions
  • ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + L-tryptophyl-tRNA(Trp)
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 184657 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID P23381 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name SYWC_HUMAN Link Image
Enzyme 6 PDB ID 1R6T Link Image
Enzyme 6 PDB File Show
Enzyme 6 3D Structure
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >1416 bp 
ATGCCCAACAGTGAGCCCGCATCTCTGCTGGAGCTGTTCAACAGCATCGCCACACAAGGG
GAGCTCGTAAGGTCCCTCAAAGCGGGAAATGCGTCAAAGGATGAAATTGATTCTGCAGTA
AAGATGTTGGTGTCATTAAAAATGAGCTACAAAGCTGCCGCGGGGGAGGATTACAAGGCT
GACTGTCCTCCAGGGAACCCAGCACCTACCAGTAATCATGGCCCAGATGCCACAGAAGCT
GAAGAGGATTTTGTGGACCCATGGACAGTACAGACAAGCAGTGCAAAAGGCATAGACTAC
GATAAGCTCATTGTTCGGTTTGGAAGTAGTAAAATTGACAAAGAGCTAATAAACCGAATA
GAGAGAGCCACCGGCCAAAGACCACACCACTTCCTGCGCAGAGGCATCTTCTTCTCACAC
AGAGATATGAATCAGGTTCTTGATGCCTATGAAAATAAGAAGCCATTTTATCTGTACACG
GGCCGGGGCCCCTCTTCTGAAGCAATGCATGTAGGTCACCTCATTCCATTTATTTTCACA
AAGTGGCTCCAGGATGTATTTAACGTGCCCTTGGTGATCCAGATGACGGATGACGAGAAG
TATCTGTGGAAGGACCTGACCCTGGACCAGGCCTATAGCTATGCTGTGGAGAATGCCAAG
GACATCATCGCCTGTGGCTTTGACATCAACAAGACTTTCATATTCTCTGACCTGGACTAC
ATGGGGATGAGCTCAGGTTTCTACAAAAATGTGGTGAAGATTCAAAAGCATGTTACCTTC
AACCAAGTGAAAGGCATTTTCGGCTTCACTGACAGCGACTGCATTGGGAAGATCAGTTTT
CCTGCCATCCAGGCTGCTCCCTCCTTCAGCAACTCATTCCCACAGATCTTCCGAGACAGG
ACGGATATCCAGTGCCTTATCCCATGTGCCATTGACCAGGATCCTTACTTTAGAATGACA
AGGGACGTCGCCCCCAGGATCGGCTATCCTAAACCAGCCCTGTTGCACTCCACCTTCTTC
CCAGCCCTGCAGGGCGCCCAGACCAAAATGAGTGCCAGCGACCCCAACTCCTCCATCTTC
CTCACCGACACGGCCAAGCAGATCAAAACCAAGGTCAATAAGCATGCGTTTTCTGGAGGG
AGAGACACCATCGAGGAGCACAGGCAGTTTGGGGGCAACTGTGATGTGGACGTGTCTTTC
ATGTACCTGACCTTCTTCCTCGAGGACGACGACAAGCTCGAGCAGATCAGGAAGGATTAC
ACCAGCGGAGCCATGCTCACCGGTGAGCTCAAGAAGGCACTCATAGAGGTTCTGCAGCCC
TTGATCGCAGAGCACCAGGCCCGGCGCAAGGAGGTCACGGATGAGATAGTGAAAGAGTTC
ATGACTCCCCGGAAGCTGTCCTTCGACTTTCAGTAG
Enzyme 6 GenBank Gene ID M77804 Link Image
Enzyme 6 GeneCard ID WARS Link Image
Enzyme 6 GenAtlas ID WARS Link Image
Enzyme 6 HGNC ID HGNC:12729 Link Image
Enzyme 6 Chromosome Location 14
Enzyme 6 Locus 14q32.31
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Rubin BY, Anderson SL, Xing L, Powell RJ, Tate WP: Interferon induces tryptophanyl-tRNA synthetase expression in human fibroblasts. J Biol Chem. 1991 Dec 25;266(36):24245-8. [PubMed Link Image]
  2. Fleckner J, Rasmussen HH, Justesen J: Human interferon gamma potently induces the synthesis of a 55-kDa protein (gamma 2) highly homologous to rabbit peptide chain release factor and bovine tryptophanyl-tRNA synthetase. Proc Natl Acad Sci U S A. 1991 Dec 15;88(24):11520-4. [PubMed Link Image]
  3. Frolova LYu, Sudomoina MA, Grigorieva AYu, Zinovieva OL, Kisselev LL: Cloning and nucleotide sequence of the structural gene encoding for human tryptophanyl-tRNA synthetase. Gene. 1991 Dec 30;109(2):291-6. [PubMed Link Image]
  4. Buwitt U, Flohr T, Bottger EC: Molecular cloning and characterization of an interferon induced human cDNA with sequence homology to a mammalian peptide chain release factor. EMBO J. 1992 Feb;11(2):489-96. [PubMed Link Image]
  5. Sokolova IV, Narovlianskii AN, Amchenkova AM, Turpaev KT: [Alternative splicing of 5'-terminal exons of the human tryptophanyl-tRNA synthetase gene] Mol Biol (Mosk). 1996 Mar-Apr;30(2):319-29. [PubMed Link Image]
  6. Frolova LY, Grigorieva AY, Sudomoina MA, Kisselev LL: The human gene encoding tryptophanyl-tRNA synthetase: interferon-response elements and exon-intron organization. Gene. 1993 Jun 30;128(2):237-45. [PubMed Link Image]
  7. Rasmussen HH, van Damme J, Puype M, Gesser B, Celis JE, Vandekerckhove J: Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes. Electrophoresis. 1992 Dec;13(12):960-9. [PubMed Link Image]
  8. Bange FC, Flohr T, Buwitt U, Bottger EC: An interferon-induced protein with release factor activity is a tryptophanyl-tRNA synthetase. FEBS Lett. 1992 Mar 30;300(2):162-6. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 5898
Enzyme 7 Name Tryptophanyl-tRNA synthetase, mitochondrial precursor
Enzyme 7 Synonyms
  1. Tryptophan--tRNA ligase
  2. TrpRS
  3. (MtTrpRS
Enzyme 7 Gene Name WARS2
Enzyme 7 Protein Sequence >Tryptophanyl-tRNA synthetase, mitochondrial precursor 
MALHSMRKARERWSFIRALHKGSAAAPALQKDSKKRVFSGIQPTGILHLGNYLGAIESWV
RLQDEYDSVLYSIVDLHSITVPQDPAVLRQSILDMTAVLLACGINPEKSILFQQSQVSEH
TQLSWILSCMVRLPRLQHLHQWKAKTTKQKHDGTVGLLTYPVLQAADILLYKSTHVPVGE
DQVQHMELVQDLAQGFNKKYGEFFPVPESILTSMKKVKSLRDPSAKMSKSDPDKLATVRI
TDSPEEIVQKFRKAVTDFTSEVTYDPAGRAGVSNIVAVHAAVTGLSVEEVVRRSAGMNTA
RYKLAVADAVIEKFAPIKREIEKLKLDKDHLEKVLQIGSAKAKELAYTVCQEVKKLVGFL
Enzyme 7 Number of Residues 360
Enzyme 7 Molecular Weight 40147
Enzyme 7 Theoretical pI 9.82
Enzyme 7 GO Classification
Function
  • ATP binding
  • RNA ligase activity
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • ligase activity
  • ligase activity, forming phosphoric ester bonds
  • nucleotide binding
  • purine nucleotide binding
  • tRNA ligase activity
  • tryptophan-tRNA ligase activity
Process
  • RNA metabolism
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
  • tRNA aminoacylation
  • tRNA aminoacylation for protein translation
  • tRNA metabolism
  • tryptophanyl-tRNA aminoacylation
Component
—
Enzyme 7 General Function Translation, ribosomal structure and biogenesis
Enzyme 7 Specific Function ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + L-tryptophyl-tRNA(Trp)
Enzyme 7 Pathways
Enzyme 7 Reactions
  • ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + L-tryptophyl-tRNA(Trp)
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 6572289 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID Q9UGM6 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name SYWM_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >1083 bp 
ATGGCGCTGCACTCAATGCGGAAAGCGCGTGAGCGCTGGAGCTTCATCCGGGCACTTCAT
AAGGGATCCGCAGCTGCTCCCGCTCTCCAGAAAGACAGCAAGAAGCGAGTATTTTCCGGC
ATTCAACCTACAGGAATCCTCCACCTGGGCAATTACCTGGGAGCCATTGAGAGCTGGGTG
AGGTTACAGGATGAATATGACTCTGTATTATACAGCATTGTTGACCTCCACTCCATTACT
GTCCCCCAAGACCCAGCTGTCCTTCGGCAGAGCATCCTGGACATGACTGCTGTTCTTCTT
GCCTGTGGCATAAACCCGGAAAAAAGCATCCTTTTCCAACAATCTCAGGTGTCTGAACAC
ACACAATTAAGTTGGATCCTTTCCTGCATGGTCAGACTACCTCGATTACAACATTTACAT
CAGTGGAAGGCAAAGACTACCAAGCAGAAGCACGATGGCACGGTGGGCCTGCTCACATAC
CCAGTACTCCAGGCAGCCGACATTCTGTTGTACAAGTCCACACACGTTCCTGTTGGGGAG
GATCAAGTCCAGCACATGGAACTAGTTCAGGATCTAGCACAAGGTTTCAACAAGAAGTAT
GGGGAGTTCTTTCCAGTGCCCGAGTCCATTCTCACATCCATGAAGAAGGTAAAATCCCTA
CGTGATCCTTCTGCCAAAATGTCGAAATCAGACCCTGACAAACTGGCCACCGTCCGAATA
ACAGACAGCCCAGAGGAGATAGTGCAGAAATTCCGCAAGGCTGTGACAGACTTCACCTCG
GAGGTCACCTATGACCCGGCTGGCCGCGCTGGCGTGTCCAACATAGTGGCGGTGCATGCC
GCGGTGACGGGGCTCTCCGTGGAGGAAGTGGTGCGCCGCAGCGCGGGCATGAACACTGCT
CGCTACAAGCTGGCCGTGGCAGATGCTGTGATTGAGAAGTTTGCCCCAATTAAGCGTGAA
ATTGAAAAACTGAAGCTGGACAAGGACCATTTAGAGAAGGTTTTACAAATTGGATCAGCA
AAAGCCAAAGAATTAGCATACACTGTGTGCCAGGAGGTGAAGAAATTGGTGGGTTTTCTA
TAG
Enzyme 7 GenBank Gene ID AJ242739 Link Image
Enzyme 7 GeneCard ID WARS2 Link Image
Enzyme 7 GenAtlas ID WARS2 Link Image
Enzyme 7 HGNC ID HGNC:12730 Link Image
Enzyme 7 Chromosome Location Not Available
Enzyme 7 Locus Not Available
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Jorgensen R, Sogaard TM, Rossing AB, Martensen PM, Justesen J: Identification and characterization of human mitochondrial tryptophanyl-tRNA synthetase. J Biol Chem. 2000 Jun 2;275(22):16820-6. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 13115
Enzyme 8 Name Indoleamine 2,3-dioxygenase-like protein 1
Enzyme 8 Synonyms
  1. Indoleamine-pyrrole 2,3-dioxygenase-like protein 1
Enzyme 8 Gene Name INDOL1
Enzyme 8 Protein Sequence >Indoleamine 2,3-dioxygenase-like protein 1 
MEPHRPNVKTAVPLSLESYHISEEYGFLLPDSLKELPDHYRPWMEIANKLPQLIDAHQLQ
AHVDKMPLLSCQFLKGHREQRLAHLVLSFLTMGYVWQEGEAQPAEVLPRNLALPFVEVSR
NLGLPPILVHSDLVLTNWTKKDPDGNLETIISFPGGESLHGFILVTALVEKEAVPGIKAL
VQATNAILQPNQEALLQALQRLRLSIQDITKTLGQMHDYVDPDIFYAGIRIFLSGWKDNP
AMPAGLMYEGVSQEPLKYSGGSAAQSTVLHAFDEFLGIRHSKESGDFLYRMRDYMPPSHK
AFIEDIHSAPSLRDYILSSGQDHLLTAYNQCVQALAELRSYHITMVTKYLITAAAKAKHG
KPNHLPGPPQALKDRGTGGTAVMSFLKSVRDKTLESILHPRG
Enzyme 8 Number of Residues 402
Enzyme 8 Molecular Weight 44865
Enzyme 8 Theoretical pI 6.94
Enzyme 8 GO Classification
Function
  • binding
  • heme binding
  • tetrapyrrole binding
Process
—
Component
—
Enzyme 8 General Function Not Available
Enzyme 8 Specific Function Not Available
Enzyme 8 Pathways Not Available
Enzyme 8 Reactions Not Available
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 34536196 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID Q6ZQW0 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name I23OL_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence Not Available
Enzyme 8 GenBank Gene ID AK128691 Link Image
Enzyme 8 GeneCard ID Q6ZQW0 Link Image
Enzyme 8 GenAtlas ID INDOL1 Link Image
Enzyme 8 HGNC ID HGNC:27269 Link Image
Enzyme 8 Chromosome Location Not Available
Enzyme 8 Locus Not Available
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References Not Available
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 13117
Enzyme 9 Name cDNA FLJ75236, highly similar to Human tryptophan oxygenase
Enzyme 9 Synonyms
  1. TDOmRNA
  2. Tryptophan 2,3-dioxygenase, isoform CRA_b
Enzyme 9 Gene Name TDO2
Enzyme 9 Protein Sequence >cDNA FLJ75236, highly similar to Human tryptophan oxygenase 
MSGCPFLGNNFGYTFKKLPVEGSEEDKSQTGVNRASKGGLIYGNYLHLEKVLNAQELQSE
TKGNKIHDEHLFIITHQAYELWFKQILWELDSVREIFQNGHVRDERNMLKVVSRMHRVSV
ILKLLVQQFSILETMTALDFNDFREYLSPASGFQSLQFRLLENKIGVLQNMRVPYNRRHY
RDNFKGEENELLLKSEQEKTLLELVEAWLERTPGLEPHGFNFWGKLEKNITRGLEEEFIR
IQAKEESEEKEEQVAEFQKQKEVLLSLFDEKRHEHLLSKGERRLSYRALQGALMIYFYRE
EPRFQVPFQLLTSLMDIDSLMTKWRYNHVCMVHRMLGSKAGTGGSSGYHYLRSTVSDRYK
VFVDLFNLSTYLIPRHWIPKMNPTIHKFLYTAEYCDSSYFSSDESD
Enzyme 9 Number of Residues 406
Enzyme 9 Molecular Weight 47872
Enzyme 9 Theoretical pI 6.93
Enzyme 9 GO Classification Not Available
Enzyme 9 General Function Amino acid transport and metabolism
Enzyme 9 Specific Function Not Available
Enzyme 9 Pathways Not Available
Enzyme 9 Reactions Not Available
Enzyme 9 Pfam Domain Function Not Available
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 158259859 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID A8K053 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name A8K053_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence Not Available
Enzyme 9 GenBank Gene ID AK289418 Link Image
Enzyme 9 GeneCard ID A8K053 Link Image
Enzyme 9 GenAtlas ID Not Available
Enzyme 9 HGNC ID Not Available
Enzyme 9 Chromosome Location Not Available
Enzyme 9 Locus Not Available
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References Not Available
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 16440
Enzyme 10 Name cDNA, FLJ94340, Homo sapiens tryptophanyl tRNA synthetase 2 (mitochondrial)(WARS2), nuclear gene encoding mitochondrial protein, mRNA (Tryptophanyl tRNA synthetase 2 (Mitochondrial), isoform CRA_a)
Enzyme 10 Synonyms Not Available
Enzyme 10 Gene Name WARS2
Enzyme 10 Protein Sequence >cDNA, FLJ94340, Homo sapiens tryptophanyl tRNA synthetase 2 (mitochondrial)(WARS2), nuclear gene encoding mitochondrial protein, mRNA (Tryptophanyl tRNA synthetase 2 (Mitochondrial), isoform CRA_a) 
MALHSMRKARERWSFIRALHKGSAAAPALQKDSKKRVFSGIQPTGILHLGNYLGAIESWV
RLQDEYDSVLYSIVDLHSITVPQDPAVLRQSILDMTAVLLACGINPEKSILFQQSQVSEH
TQLSWILSCMVRLPRLQHLHQWKAKTTKQKHDGTVGLLTYPVLQAADILLYKSTHVPVGE
DQVQHMELVQDLAQGFNKKYGEFFPVPESILTSMKKVKSLRDPSAKMSKSDPDKLATVRI
TDSPEEIVQKFRKAVTDFTSEVTYDPAGRAGVSNIVAVHAAVTGLSVEEVVRRSAGMNTA
RYKLAVADAVIEKFAPIKREIEKLKLDKDHLEKVLQIGSAKAKELAYTVCQEVKKLVGFL
Enzyme 10 Number of Residues 360
Enzyme 10 Molecular Weight 40147
Enzyme 10 Theoretical pI 9.82
Enzyme 10 GO Classification
Function
  • ATP binding
  • RNA ligase activity
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • ligase activity
  • ligase activity, forming phosphoric ester bonds
  • nucleotide binding
  • purine nucleotide binding
  • tRNA ligase activity
  • tryptophan-tRNA ligase activity
Process
  • RNA metabolism
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
  • tRNA aminoacylation
  • tRNA aminoacylation for protein translation
  • tRNA metabolism
  • tryptophanyl-tRNA aminoacylation
Component
—
Enzyme 10 General Function Translation, ribosomal structure and biogenesis
Enzyme 10 Specific Function Not Available
Enzyme 10 Pathways Not Available
Enzyme 10 Reactions Not Available
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein Not Available
Enzyme 10 UniProtKB/Swiss-Prot ID B2R9D4 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name B2R9D4_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence Not Available
Enzyme 10 GenBank Gene ID AK313740 Link Image
Enzyme 10 GeneCard ID B2R9D4 Link Image
Enzyme 10 GenAtlas ID Not Available
Enzyme 10 HGNC ID Not Available
Enzyme 10 Chromosome Location Not Available
Enzyme 10 Locus Not Available
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References Not Available
Enzyme 10 Metabolite References Not Available