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Human Metabolome Database Version 2.5

 

Showing metabocard for L-Kynurenine (HMDB00684)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-06-15 11:23:33
Accession Number HMDB00684
Secondary Accession Numbers HMDB00183
Common Name L-Kynurenine
Description Kynurenine is a metabolite of the amino acid tryptophan used in the production of niacin. L-kynurenine is a central compound of the pathway of tryptophan metabolism pathway since it can change to the neuroprotective agent kynurenic acid or to the neurotoxic agent quinolinic acid. The break-up of these endogenous compounds' balance can be observable in many disorders. It can occur in neurodegenerative disorders, such as Parkinson's disease, Huntington's and Alzheimer's disease, in stroke, in epilepsy, in multiple sclerosis, in amyotrophic lateral sclerosis, and in mental failures, such as schizophrenia and depression.
Synonyms
  1. (S)-alpha,2-diamino-3-hydroxy-gamma-oxo-Benzenebutanoate
  2. (S)-alpha,2-diamino-3-hydroxy-gamma-oxo-Benzenebutanoic acid
  3. (alphaS)-alpha,2-diamino-3-hydroxy-gamma-oxo-Benzenebutanoate
  4. (alphaS)-alpha,2-diamino-3-hydroxy-gamma-oxo-Benzenebutanoic acid
  5. 3-(3-Hydroxyanthraniloyl)-L-alanine
  6. 3-Anthraniloylalanine
  7. 3-Hydroxy-L-kynurenine
  8. 3-anthraniloyl-Alanine
  9. 3-anthraniloyl-L-alanine
  10. DL-Kynureninefree base
  11. Kynurenin
  12. Quinurenine
  13. alpha,2-diamino-gamma-oxo-Benzenebutanoate
  14. alpha,2-diamino-gamma-oxo-Benzenebutanoic acid
  15. dl-Kynurenine
Chemical IUPAC Name 2-amino-4-(2-aminophenyl)-4-oxo-butanoic acid
Chemical Formula C10H12N2O3
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Amino acids and Amino Acid conjugates
Class
  • Amino Acids
Sub Class
  • NA
Family
  • Mammalian Metabolite
Species
  • ketone
  • primary amine
  • primary aliphatic amine (alkylamine)
  • primary aromatic amine
  • carboxylic acid
  • aromatic compound
  • alpha-aminoacid
Biofunction
  • Component of Tryptophan metabolism
Application
—
Source
  • Endogenous
Average Molecular Weight 208.214
Monoisotopic Molecular Weight 208.084793
Isomeric SMILES N[C@@H](CC(=O)C1=CC=CC=C1N)C(O)=O
Canonical SMILES NC(CC(=O)C1=CC=CC=C1N)C(O)=O
KEGG Compound ID C01718 Link Image
BioCyc ID L-KYNURENINE Link Image
BiGG ID 1445574 Link Image
Wikipedia Link Kynurenine Link Image
NuGOwiki Link HMDB00684 Link Image
Metagene Link HMDB00684 Link Image
METLIN ID 72 Link Image
PubChem Compound 846 Link Image
PubChem Substance 11375672 Link Image
ChEBI ID Not Available
CAS Registry Number 343-65-7
InChI Identifier InChI=1/C10H12N2O3/c11-7-4-2-1-3-6(7)9(13)5-8(12)10(14)15/h1-4,8H,5,11-12H2,(H,14,15)/t8-/m0/s1
Synthesis Reference Hayaishi, Osamu. L-Kynurenine sulfate monohydrate. Biochemical Preparations (1953), 3 108-11.
Melting Point (Experimental) 191 oC
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 986.0 mg/mL [MEYLAN,WM et al. (1996)]; 1.67 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -1.93 [Predicted by ALOGPS]; -2.2 [Predicted by PubChem via XLOGP]; -2.25 [MEYLAN,WM & HOWARD,PH (1995)] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID 1T5M Link Image
Experimental PDB File Show
Experimental PDB Structure
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Bruker)
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 (Predicted from LogP)
Biofluid Location
  • Blood
  • Cerebrospinal Fluid
  • Urine
Tissue Location
Tissue References
Brain —
Central Nervous System —
Epidermis —
Fibroblasts —
Intestine —
Liver —
Neuron —
Placenta —
Spleen —
Concentrations (Normal)
Biofluid Blood
Value 2.4 +/- 0.5 uM
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid Blood
Value 1.4 (0.7-3.0) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Herve C, Beyne P, Jamault H, Delacoux E: Determination of tryptophan and its kynurenine pathway metabolites in human serum by high-performance liquid chromatography with simultaneous ultraviolet and fluorimetric detection. J Chromatogr B Biomed Appl. 1996 Jan 12;675(1):157-61. [PubMed Link Image]
Biofluid Blood
Value 1.6 +/- 0.1 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Fujigaki S, Saito K, Takemura M, Fujii H, Wada H, Noma A, Seishima M: Species differences in L-tryptophan-kynurenine pathway metabolism: quantification of anthranilic acid and its related enzymes. Arch Biochem Biophys. 1998 Oct 15;358(2):329-35. [PubMed Link Image]
Biofluid CSF
Value 0.052 +/- 0.0031 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 0.054 +/- 0.007 uM
Age Adult:>18 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Heyes MP, Saito K, Milstien S, Schiff SJ: Quinolinic acid in tumors, hemorrhage and bacterial infections of the central nervous system in children. J Neurol Sci. 1995 Nov;133(1-2):112-8. [PubMed Link Image]
Biofluid CSF
Value 0.0019 +/- 0.00021 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Fujigaki S, Saito K, Takemura M, Fujii H, Wada H, Noma A, Seishima M: Species differences in L-tryptophan-kynurenine pathway metabolism: quantification of anthranilic acid and its related enzymes. Arch Biochem Biophys. 1998 Oct 15;358(2):329-35. [PubMed Link Image]
Biofluid Urine
Value 2.85 +/- 1.94 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by Cornelius Lentner.
  • West Cadwell, N.J. : Medical education Div., Ciba-Geigy Corp.
  • Basel, Switzerland c1981-1992.
Biofluid Urine
Value 0.56 +/- 0.91 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 0.41 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)
Biofluid CSF
Value 0.18 +/- 0.040 uM
Age Adult:>18 yrs old
Sex N/A
Condition Hydrocephalus
Comments Not Available
References
  • Heyes MP, Saito K, Milstien S, Schiff SJ: Quinolinic acid in tumors, hemorrhage and bacterial infections of the central nervous system in children. J Neurol Sci. 1995 Nov;133(1-2):112-8. [PubMed Link Image]
Biofluid CSF
Value 0.25 +/- 0.12 uM
Age Adult:>18 yrs old
Sex N/A
Condition Intraventricular hemorrhage
Comments Not Available
References
  • Heyes MP, Saito K, Milstien S, Schiff SJ: Quinolinic acid in tumors, hemorrhage and bacterial infections of the central nervous system in children. J Neurol Sci. 1995 Nov;133(1-2):112-8. [PubMed Link Image]
Biofluid CSF
Value 1.6 +/- 0.58 uM
Age Adult:>18 yrs old
Sex N/A
Condition CNS tumors
Comments Not Available
References
  • Heyes MP, Saito K, Milstien S, Schiff SJ: Quinolinic acid in tumors, hemorrhage and bacterial infections of the central nervous system in children. J Neurol Sci. 1995 Nov;133(1-2):112-8. [PubMed Link Image]
Biofluid CSF
Value 2.6 +/- 1.06 uM
Age Adult:>18 yrs old
Sex N/A
Condition CNS infections
Comments Not Available
References
  • Heyes MP, Saito K, Milstien S, Schiff SJ: Quinolinic acid in tumors, hemorrhage and bacterial infections of the central nervous system in children. J Neurol Sci. 1995 Nov;133(1-2):112-8. [PubMed Link Image]
Associated Disorders
Condition References
CNS infections
  • Heyes MP, Saito K, Milstien S, Schiff SJ: Quinolinic acid in tumors, hemorrhage and bacterial infections of the central nervous system in children. J Neurol Sci. 1995 Nov;133(1-2):112-8. [PubMed Link Image]
CNS tumors
  • Heyes MP, Saito K, Milstien S, Schiff SJ: Quinolinic acid in tumors, hemorrhage and bacterial infections of the central nervous system in children. J Neurol Sci. 1995 Nov;133(1-2):112-8. [PubMed Link Image]
Hydrocephalus
  • Heyes MP, Saito K, Milstien S, Schiff SJ: Quinolinic acid in tumors, hemorrhage and bacterial infections of the central nervous system in children. J Neurol Sci. 1995 Nov;133(1-2):112-8. [PubMed Link Image]
Intraventricular hemorrhage
  • Heyes MP, Saito K, Milstien S, Schiff SJ: Quinolinic acid in tumors, hemorrhage and bacterial infections of the central nervous system in children. J Neurol Sci. 1995 Nov;133(1-2):112-8. [PubMed Link Image]
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Tryptophan Metabolism SMP00063 Link Image map00380 Link Image
General References
  1. Moroni F, Carpenedo R, Chiarugi A: Kynurenine hydroxylase and kynureninase inhibitors as tools to study the role of kynurenine metabolites in the central nervous system. Adv Exp Med Biol. 1996;398:203-10. [PubMed Link Image]
  2. Widner B, Sepp N, Kowald E, Ortner U, Wirleitner B, Fritsch P, Baier-Bitterlich G, Fuchs D: Enhanced tryptophan degradation in systemic lupus erythematosus. Immunobiology. 2000 Apr;201(5):621-30. [PubMed Link Image]
  3. Calandra P: Research on tryptophan metabolites "via kynurenine" in epidermis of man and mouse. Acta Vitaminol Enzymol. 1975;29(1-6):158-60. [PubMed Link Image]
  4. Manuelpillai U, Nicholls T, Wallace EM, Phillips DJ, Guillemin G, Walker D: Increased mRNA expression of kynurenine pathway enzymes in human placentae exposed to bacterial endotoxin. Adv Exp Med Biol. 2003;527:85-9. [PubMed Link Image]
  5. Greengard O: Relationship between urinary excretion of kynurenine and liver tryptophan oxygenase activity. Am J Clin Nutr. 1971 Jun;24(6):709-11. [PubMed Link Image]
  6. Widner B, Sepp N, Kowald E, Kind S, Schmuth M, Fuchs D: Degradation of tryptophan in patients with systemic lupus erythematosus. Adv Exp Med Biol. 1999;467:571-7. [PubMed Link Image]
  7. Joseph MH: Determination of kynurenine by a simple gas-liquid chromatographic method applicable to urine, plasma, brain and cerebrospinal fluid. J Chromatogr. 1978 Jul 1;146(1):33-41. [PubMed Link Image]
  8. Heyes MP, Saito K, Lackner A, Wiley CA, Achim CL, Markey SP: Sources of the neurotoxin quinolinic acid in the brain of HIV-1-infected patients and retrovirus-infected macaques. FASEB J. 1998 Jul;12(10):881-96. [PubMed Link Image]
  9. Fujigaki S, Saito K, Takemura M, Fujii H, Wada H, Noma A, Seishima M: Species differences in L-tryptophan-kynurenine pathway metabolism: quantification of anthranilic acid and its related enzymes. Arch Biochem Biophys. 1998 Oct 15;358(2):329-35. [PubMed Link Image]
  10. Heinmets F: Computer simulation and analysis of tryptophan metabolism via kynurenine pathway in liver. Comput Biol Med. 1974 Sep;1(4):323-36. [PubMed Link Image]
  11. Widner B, Werner ER, Schennach H, Fuchs D: An HPLC method to determine tryptophan and kynurenine in serum simultaneously. Adv Exp Med Biol. 1999;467:827-32. [PubMed Link Image]
  12. Okuno E, Nakamura M, Schwarcz R: Two kynurenine aminotransferases in human brain. Brain Res. 1991 Mar 1;542(2):307-12. [PubMed Link Image]
  13. Altman K, Greengard O: Correlation of kynurenine excretion with liver tryptophan pyrrolase levels in disease and after hydrocortisone induction. J Clin Invest. 1966 Oct;45(10):1527-34. [PubMed Link Image]
  14. Saito K, Fujigaki S, Heyes MP, Shibata K, Takemura M, Fujii H, Wada H, Noma A, Seishima M: Mechanism of increases in L-kynurenine and quinolinic acid in renal insufficiency. Am J Physiol Renal Physiol. 2000 Sep;279(3):F565-72. [PubMed Link Image]
  15. Pearson SJ, Meldrum A, Reynolds GP: An investigation of the activities of 3-hydroxykynureninase and kynurenine aminotransferase in the brain in Huntington's disease. J Neural Transm Gen Sect. 1995;102(1):67-73. [PubMed Link Image]
  16. Medana IM, Day NP, Salahifar-Sabet H, Stocker R, Smythe G, Bwanaisa L, Njobvu A, Kayira K, Turner GD, Taylor TE, Hunt NH: Metabolites of the kynurenine pathway of tryptophan metabolism in the cerebrospinal fluid of Malawian children with malaria. J Infect Dis. 2003 Sep 15;188(6):844-9. Epub 2003 Sep 9. [PubMed Link Image]
  17. Heyes MP, Saito K, Milstien S, Schiff SJ: Quinolinic acid in tumors, hemorrhage and bacterial infections of the central nervous system in children. J Neurol Sci. 1995 Nov;133(1-2):112-8. [PubMed Link Image]
  18. 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]
  19. Hartai Z, Klivenyi P, Janaky T, Penke B, Dux L, Vecsei L: Kynurenine metabolism in plasma and in red blood cells in Parkinson's disease. J Neurol Sci. 2005 Dec 15;239(1):31-5. Epub 2005 Aug 15. [PubMed Link Image]
  20. Martinsons A, Rudzite V, Groma V, Bratslavska O, Widner B, Fuchs D: Kynurenine and neopterin in chronic glomerulonephritis. Adv Exp Med Biol. 1999;467:579-86. [PubMed Link Image]
  21. Wikipedia Link Image
Metabolic Enzymes
  1. Kynureninase
  2. Kynurenine/alpha-aminoadipate aminotransferase mitochondrial precursor
  3. Kynurenine--oxoglutarate transaminase 1
  4. Kynurenine 3-monooxygenase
  5. Hypothetical protein AADAT
  6. Probable arylformamidase
  7. Kynureninase
  8. Kynurenine--oxoglutarate transaminase 3
Enzyme 1 [top]
Enzyme 1 ID 5561
Enzyme 1 Name Kynureninase
Enzyme 1 Synonyms
  1. L-kynurenine hydrolase
Enzyme 1 Gene Name KYNU
Enzyme 1 Protein Sequence >Kynureninase 
MEPSSLELPADTVQRIAAELKCHPTDERVALHLDEEDKLRHFRECFYIPKIQDLPPVDLS
LVNKDENAIYFLGNSLGLQPKMVKTYLEEELDKWAKIAAYGHEVGKRPWITGDESIVGLM
KDIVGANEKEIALMNALTVNLHLLMLSFFKPTPKRYKILLEAKAFPSDHYAIESQLQLHG
LNIEESMRMIKPREGEETLRIEDILEVIEKEGDSIAVILFSGVHFYTGQHFNIPAITKAG
QAKGCYVGFDLAHAVGNVELYLHDWGVDFACWCSYKYLNAGAGGIAGAFIHEKHAHTIKP
ALVGWFGHELSTRFKMDNKLQLIPGVCGFRISNPPILLVCSLHASLEIFKQATMKALRKK
SVLLTGYLEYLIKHNYGKDKAATKKPVVNIITPSHVEERGCQLTITFSVPNKDVFQELEK
RGVVCDKRNPNGIRVAPVPLYNSFHDVYKFTNLLTSILDSAETKN
Enzyme 1 Number of Residues 465
Enzyme 1 Molecular Weight 52352
Enzyme 1 Theoretical pI 7.04
Enzyme 1 GO Classification
Function
  • binding
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on acid carbon-carbon bonds
  • hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances
  • kynureninase activity
  • pyridoxal phosphate binding
  • transaminase activity
  • transferase activity
  • transferase activity, transferring nitrogenous groups
  • vitamin binding
Process
  • NAD biosynthesis
  • amino acid and derivative metabolism
  • amino acid derivative metabolism
  • biogenic amine metabolism
  • cellular metabolism
  • coenzyme biosynthesis
  • coenzyme metabolism
  • cofactor metabolism
  • indolalkylamine metabolism
  • metabolism
  • physiological process
  • pyridine nucleotide biosynthesis
  • tryptophan catabolism
  • tryptophan metabolism
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 1 General Function Amino acid transport and metabolism
Enzyme 1 Specific Function Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3- hydroxykynurenine (L-3OHKyn) into anthranilic (AA) and 3- hydroxyanthranilic acids (3-OHAA), respectively. Has a preference for the L-3-hydroxy form. Also has cysteine-conjugate-beta-lyase activity
Enzyme 1 Pathways
Enzyme 1 Reactions
  • L-kynurenine + H2O = anthranilate + L-alanine
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 1323715 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q16719 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name KYNU_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1398 bp 
ATGGAGCCTTCATCTCTTGAGCTGCCGGCTGACACAGTGCAGCGCATTGCGGCTGAACTC
AAATGCCACCCAACGGATGAGAGGGTGGCTCTCCACCTAGATGAGGAAGATAAGCTGAGG
CACTTCAGGGAGTGCTTTTATATTCCCAAAATACAGGATCTGCCTCCAGTTGATTTATCA
TTAGTGAATAAAGATGAAAATGCCATCTATTTCTTGGGAAATTCTCTTGGCCTTCAACCA
AAAATGGTTAAAACATATCTTGAAGAAGAACTAGATAAGTGGGCCAAAATAGCAGCCTAT
GGTCATGAAGTGGGGAAGCGTCCTTGGATTACAGGAGATGAGAGTATTGTAGGCCTTATG
AAGGACATTGTAGGAGCCAATGAGAAAGAAATAGCCCTAATGAATGCTTTGACTGTAAAT
TTACATCTTCTAATGTTATCATTTTTTAAGCCTACGCCAAAACGATATAAAATTCTTCTA
GAAGCCAAAGCCTTCCCTTCTGATCATTATGCTATTGAGTCACAACTACAACTTCACGGA
CTTAACATTGAAGAAAGTATGCGGATGATAAAGCCAAGAGAGGGGGAAGAAACCTTAAGA
ATAGAGGATATCCTTGAAGTAATTGAGAAGGAAGGAGACTCAATTGCAGTGATCCTGTTC
AGTGGGGTGCATTTTTACACTGGACAGCACTTTAATATTCCTGCCATCACAAAAGCTGGA
CAAGCGAAGGGTTGTTATGTTGGCTTTGATCTAGCACATGCAGTTGGAAATGTTGAACTC
TACTTACATGACTGGGGAGTTGATTTTGCCTGCTGGTGTTCCTACAAGTATTTAAATGCA
GGAGCAGGAGGAATTGCTGGTGCCTTCATTCATGAAAAGCATGCCCATACGATTAAACCT
GCATTAGTGGGATGGTTTGGCCATGAACTCAGCACCAGATTTAAGATGGATAACAAACTG
CAGTTAATCCCTGGGGTCTGTGGATTCCGAATTTCAAATCCTCCCATTTTGTTGGTCTGT
TCCTTGCATGCTAGTTTAGAGATCTTTAAGCAAGCGACAATGAAGGCATTGCGGAAAAAA
TCTGTTTTGCTAACTGGCTATCTGGAATACCTGATCAAGCATAACTATGGCAAAGATAAA
GCAGCAACCAAGAAACCAGTTGTGAACATAATTACTCCGTCTCATGTAGAGGAGCGGGGG
TGCCAGCTAACAATAACATTTTCTGTTCCAAACAAAGATGTTTTCCAAGAACTAGAAAAA
AGAGGAGTGGTTTGTGACAAGCGGAATCCAAATGGCATTCGAGTGGCTCCAGTTCCTCTC
TATAATTCTTTCCATGATGTTTATAAATTTACCAATCTGCTCACTTCTATACTTGACTCT
GCAGAAACAAAAAATTAG
Enzyme 1 GenBank Gene ID U57721 Link Image
Enzyme 1 GeneCard ID KYNU Link Image
Enzyme 1 GenAtlas ID KYNU Link Image
Enzyme 1 HGNC ID HGNC:6469 Link Image
Enzyme 1 Chromosome Location 2
Enzyme 1 Locus 2q22.2
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Alberati-Giani D, Buchli R, Malherbe P, Broger C, Lang G, Kohler C, Lahm HW, Cesura AM: Isolation and expression of a cDNA clone encoding human kynureninase. Eur J Biochem. 1996 Jul 15;239(2):460-8. [PubMed Link Image]
  2. Toma S, Nakamura M, Tone S, Okuno E, Kido R, Breton J, Avanzi N, Cozzi L, Speciale C, Mostardini M, Gatti S, Benatti L: Cloning and recombinant expression of rat and human kynureninase. FEBS Lett. 1997 May 12;408(1):5-10. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5615
Enzyme 2 Name Kynurenine/alpha-aminoadipate aminotransferase mitochondrial precursor
Enzyme 2 Synonyms
  1. KAT/AadAT
  2. Kynurenine--oxoglutarate transaminase II
  3. Kynurenine aminotransferase II
  4. Kynurenine--oxoglutarate aminotransferase II
  5. 2-aminoadipate transaminase
  6. 2- aminoadipate aminotransferase
  7. Alpha-aminoadipate aminotransferase
  8. AadAT
Enzyme 2 Gene Name AADAT
Enzyme 2 Protein Sequence >Kynurenine/alpha-aminoadipate aminotransferase mitochondrial precursor 
MNYARFITAASAARNPSPIRTMTDILSRGPKSMISLAGGLPNPNMFPFKTAVITVENGKT
IQFGEEMMKRALQYSPSAGIPELLSWLKQLQIKLHNPPTIHYPPSQGQMDLCVTSGSQQG
LCKVFEMIINPGDNVLLDEPAYSGTLQSLHPLGCNIINVASDESGIVPDSLRDILSRWKP
EDAKNPQKNTPKFLYTVPNGNNPTGNSLTSERKKEIYELARKYDFLIIEDDPYYFLQFNK
FRVPTFLSMDVDGRVIRADSFSKIISSGLRIGFLTGPKPLIERVILHIQVSTLHPSTFNQ
LMISQLLHEWGEEGFMAHVDRVIDFYSNQKDAILAAADKWLTGLAEWHVPAAGMFLWIKV
KGINDVKELIEEKAVKMGVLMLPGNAFYVDSSAPSPYLRASFSSASPEQMDVAFQVLAQL
IKESL
Enzyme 2 Number of Residues 425
Enzyme 2 Molecular Weight 47352
Enzyme 2 Theoretical pI 6.96
Enzyme 2 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring nitrogenous groups
Process
  • biosynthesis
  • metabolism
  • physiological process
Component
—
Enzyme 2 General Function Transcription
Enzyme 2 Specific Function Shows activity also towards tryptophan, aspartate and hydroxykinurenine
Enzyme 2 Pathways
Enzyme 2 Reactions
  • L-2-aminoadipate + 2-oxoglutarate = 2-oxoadipate + L-glutamate
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 6165634 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q8N5Z0 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name AADAT_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1278 bp 
ATGAATTACGCACGGTTCATCACGGCAGCGAGCGCAGCCAGAAACCCTTCTCCCATCCGG
ACCATGACTGACATATTGAGCAGAGGACCAAAATCGATGATCTCCTTGGCTGGTGGCTTA
CCAAATCCAAACATGTTTCCTTTTAAGACTGCCGTAATCACTGTAGAAAATGGAAAGACC
ATCCAATTTGGAGAAGAGATGATGAAGAGAGCACTTCAGTATTCTCCGAGTGCTGGAATT
CCAGAGCTTTTGTCCTGGCTAAAACAGTTACAAATAAAATTGCATAATCCTCCTACCATC
CATTACCCACCCAGTCAAGGACAAATGGATCTATGTGTCACATCTGGCAGCCAACAAGGT
CTTTGTAAGGTGTTTGAAATGATCATTAATCCTGGAGATAATGTCCTCCTAGATGAACCT
GCTTATTCAGGAACTCTTCAAAGTCTGCACCCACTGGGCTGCAACATTATTAATGTTGCC
AGTGATGAAAGTGGGATTGTTCCAGATTCCCTAAGAGACATACTTTCCAGATGGAAACCA
GAAGATGCAAAGAATCCCCAGAAAAACACCCCCAAATTTCTTTATACTGTTCCAAATGGC
AACAACCCTACTGGAAACTCATTAACCAGTGAACGCAAAAAGGAAATCTATGAGCTTGCA
AGAAAATATGATTTCCTCATAATAGAAGATGATCCTTACTATTTTCTCCAGTTTAACAAG
TTCAGGGTACCAACATTTCTTTCCATGGATGTTGATGGACGTGTCATCAGAGCTGACTCT
TTTTCAAAAATCATTTCCTCTGGGTTGAGAATAGGATTTTTAACTGGTCCAAAACCCTTA
ATAGAGAGAGTTATTTTACACATACAAGTTTCAACATTGCACCCCAGCACTTTTAACCAG
CTCATGATATCACAGCTTCTACACGAATGGGGAGAAGAAGGTTTCATGGCTCATGTAGAC
AGGGTTATTGATTTCTATAGTAACCAGAAGGATGCAATACTGGCAGCTGCAGACAAGTGG
TTAACTGGTTTGGCAGAATGGCATGTTCCTGCTGCTGGAATGTTTTTATGGATTAAAGTT
AAAGGCATTAATGATGTAAAAGAACTGATTGAAGAAAAGGCCGTTAAGATGGGGGTATTA
ATGCTCCCTGGAAATGCTTTCTACGTCGATAGCTCAGCTCCTAGCCCTTACTTGAGAGCA
TCCTTCTCTTCAGCTTCTCCAGAACAGATGGATGTGGCCTTCCAGGTATTAGCACAACTT
ATAAAAGAATCTTTATGA
Enzyme 2 GenBank Gene ID AF097994 Link Image
Enzyme 2 GeneCard ID AADAT Link Image
Enzyme 2 GenAtlas ID AADAT Link Image
Enzyme 2 HGNC ID HGNC:17929 Link Image
Enzyme 2 Chromosome Location 4
Enzyme 2 Locus 4q33
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References Not Available
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5703
Enzyme 3 Name Kynurenine--oxoglutarate transaminase 1
Enzyme 3 Synonyms
  1. Kynurenine-- oxoglutarate transaminase I
  2. Kynurenine aminotransferase I
  3. KATI
  4. Glutamine--phenylpyruvate transaminase
  5. Glutamine transaminase K
  6. GTK
  7. Cysteine-S-conjugate beta-lyase
Enzyme 3 Gene Name CCBL1
Enzyme 3 Protein Sequence >Kynurenine--oxoglutarate transaminase 1 
MAKQLQARRLDGIDYNPWVEFVKLASEHDVVNLGQGFPDFPPPDFAVEAFQHAVSGDFML
NQYTKTFGYPPLTKILASFFGELLGQEIDPLRNVLVTVGGYGALFTAFQALVDEGDEVII
IEPFFDCYEPMTMMAGGRPVFVSLKPGPIQNGELGSSSNWQLDPMELAGKFTSRTKALVL
NTPNNPLGKVFSREELELVASLCQQHDVVCITDEVYQWMVYDGHQHISIASLPGMWERTL
TIGSAGKTFSATGWKVGWVLGPDHIMKHLRTVHQNSVFHCPTQSQAAVAESFEREQLLFR
QPSSYFVQFPQAMQRCRDHMIRSLQSVGLKPIIPQGSYFLITDISDFKRKMPDLPGAVDE
PYDRRFVKWMIKNKGLVAIPVSIFYSVPHQKHFDHYIRFCFVKDEATLQAMDEKLRKWKV
EL
Enzyme 3 Number of Residues 422
Enzyme 3 Molecular Weight 47876
Enzyme 3 Theoretical pI 6.45
Enzyme 3 GO Classification
Function
  • 1-aminocyclopropane-1-carboxylate synthase activity
  • carbon-sulfur lyase activity
  • catalytic activity
  • lyase activity
  • transferase activity
  • transferase activity, transferring nitrogenous groups
Process
  • biosynthesis
  • metabolism
  • physiological process
Component
—
Enzyme 3 General Function Amino acid transport and metabolism
Enzyme 3 Specific Function Catalyzes the irreversible transamination of the L- tryptophan metabolite L-kinurenine to form kynurenic acid (KA). Metabolizes the cysteine conjugates of certain halogenated alkenes and alkanes to form reactive metabolites. Catalyzes the beta- elimination of S-conjugates and Se-conjugates of L- (seleno)cysteine, resulting in the cleavage of the C-S or C-Se bond
Enzyme 3 Pathways
Enzyme 3 Reactions
  • RS-CH2-CH(NH3+)COO- = RSH + ammonia + pyruvate
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 758591 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q16773 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name KAT1_HUMAN Link Image
Enzyme 3 PDB ID 1W7N Link Image
Enzyme 3 PDB File Show
Enzyme 3 3D Structure
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1269 bp 
ATGGCCAAACAGCTGCAGGCCCGAAGGCTAGACGGGATCGACTACAACCCCTGGGTGGAG
TTTGTGAAACTGGCCAGTGAGCATGACGTCGTGAACTTGGGCCAGGGCTTCCCGGATTTC
CCACCACCAGACTTTGCCGTGGAAGCCTTTCAGCACGCTGTCAGTGGAGACTTCATGCTT
AACCAGTACACCAAGACATTTGGTTACCCACCACTGACGAAGATCCTGGCAAGTTTCTTT
GGGGAGCTGCTGGGTCAGGAGATAGACCCGCTCAGGAATGTGCTGGTGACTGTTGGTGGC
TATGGGGCCCTGTTCACAGCCTTCCAGGCCCTGGTGGACGAAGGAGACGAGGTCATCATC
ATCGAACCCTTTTTTGACTGCTACGAGCCCATGACAATGATGGCAGGGGGTCGTCCTGTG
TTTGTGTCCCTGAAGCCGGGTCCCATCCAGAATGGAGAACTGGGTTCCAGCAGCAACTGG
CAGCTGGACCCCATGGAGCTGGCCGGCAAATTCACATCACGCACCAAAGCCCTGGTCCTC
AACACCCCCAACAACCCCCTGGGCAAGGTGTTCTCCAGGGAAGAGCTGGAGCTGGTGGCC
AGCCTTTGCCAGCAGCATGACGTGGTGTGTATCACTGATGAAGTCTACCAGTGGATGGTC
TACGACGGGCACCAGCACATCAGCATTGCCAGCCTCCCTGGCATGTGGGAACGGACCCTG
ACCATCGGCAGCGCCGGCAAGACCTTCAGCGCCACTGGCTGGAAGGTGGGCTGGGTCCTG
GGTCCAGATCACATCATGAAGCACCTGCGGACCGTGCACCAGAACTCCGTCTTCCACTGC
CCCACGCAGAGCCAGGCTGCAGTAGCCGAGAGCTTTGAACGGGAGCAGCTGCTCTTCCGC
CAACCCAGCAGCTACTTTGTGCAGTTCCCGCAGGCCATGCAGCGCTGCCGTGACCACATG
ATACGTAGCCTACAGTCAGTGGGCCTGAAGCCCATCATCCCTCAGGGCAGCTACTTCCTC
ATCACAGACATCTCAGACTTCAAGAGGAAGATGCCTGACTTGCCTGGAGCTGTGGATGAG
CCCTATGACAGACGCTTCGTCAAGTGGATGATCAAGAACAAGGGCTTGGTGGCCATCCCT
GTCTCCATCTTCTATAGTGTGCCACATCAGAAGCACTTTGACCACTATATCCGCTTCTGT
TTTGTGAAGGATGAAGCCACGCTCCAGGCCATGGACGAGAAGCTGCGGAAGTGGAAGGTG
GAACTCTAG
Enzyme 3 GenBank Gene ID X82224 Link Image
Enzyme 3 GeneCard ID CCBL1 Link Image
Enzyme 3 GenAtlas ID CCBL1 Link Image
Enzyme 3 HGNC ID HGNC:1564 Link Image
Enzyme 3 Chromosome Location 9
Enzyme 3 Locus 9q34.11
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Perry S, Harries H, Scholfield C, Lock T, King L, Gibson G, Goldfarb P: Molecular cloning and expression of a cDNA for human kidney cysteine conjugate beta-lyase. FEBS Lett. 1995 Mar 6;360(3):277-80. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 8105
Enzyme 4 Name Kynurenine 3-monooxygenase
Enzyme 4 Synonyms
  1. Kynurenine 3-hydroxylase
Enzyme 4 Gene Name KMO
Enzyme 4 Protein Sequence >Kynurenine 3-monooxygenase 
MDSSVIQRKKVAVIGGGLVGSLQACFLAKRNFQIDVYEAREDTRVATFTRGRSINLALSH
RGRQALKAVGLEDQIVSQGIPMRARMIHSLSGKKSAIPYGTKSQYILSVSRENLNKDLLT
AAEKYPNVKMHFNHRLLKCNPEEGMITVLGSDKVPKDVTCDLIVGCDGAYSTVRSHLMKK
PRFDYSQQYIPHGYMELTIPPKNGDYAMEPNYLHIWPRNTFMMIALPNMNKSFTCTLFMP
FEEFEKLLTSNDVVDFFQKYFPDAIPLIGEKLLVQDFFLLPAQPMISVKCSSFHFKSHCV
LLGDAAHAIVPFFGQGMNAGFEDCLVFDELMDKFSNDLSLCLPVFSRLRIPDDHAISDLS
MYNYIEMRAHVNSSWFIFQKNMERFLHAIMPSTFIPLYTMVTFSRIRYHEAVQRWHWQKK
VINKGLFFLGSLIAISSTYLLIHYMSPRSFLRLRRPWNWIAHFRNTTCFPAKAVDSLEQI
SNLISR
Enzyme 4 Number of Residues 486
Enzyme 4 Molecular Weight 55811
Enzyme 4 Theoretical pI 9.34
Enzyme 4 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
—
Enzyme 4 General Function Coenzyme transport and metabolism
Enzyme 4 Specific Function Required for synthesis of quinolinic acid, a neurotoxic NMDA receptor antagonist and potential endogenous inhibitor of NMDA receptor signaling in axonal targeting, synaptogenesis and apoptosis during brain development. Quinolinic acid may also affect NMDA receptor signaling in pancreatic beta cells, osteoblasts, myocardial cells, and the gastrointestinal tract
Enzyme 4 Pathways
Enzyme 4 Reactions
  • L-kynurenine + NADPH + H+ + O2 = 3-hydroxy-L-kynurenine + NADP+ + H2O
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • 384-404 425-445
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 2239124 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID O15229 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name KMO_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1461 bp 
ATGGACTCATCTGTCATTCAAAGGAAAAAAGTAGCTGTCATTGGTGGTGGCTTGGTTGGC
TCATTACAAGCATGCTTTCTTGCAAAGAGGAATTTCCAGATTGATGTATATGAAGCTAGG
GAAGATACTCGAGTGGCTACCTTCACACGTGGAAGAAGCATTAACTTAGCCCTTTCTCAT
AGAGGACGACAAGCCTTGAAAGCTGTTGGCCTGGAAGATCAGATTGTATCCCAAGGTATT
CCCATGAGAGCAAGAATGATCCACTCTCTTTCAGGAAAAAAGTCTGCAATTCCCTATGGG
ACAAAGTCTCAGTATATTCTTTCTGTAAGCAGAGAAAATCTAAACAAGGATCTATTGACT
GCTGCTGAGAAATACCCCAATGTGAAAATGCACTTTAACCACAGGCTGTTGAAATGTAAT
CCAGAGGAAGGAATGATCACAGTGCTTGGATCTGACAAAGTTCCCAAAGATGTCACTTGT
GACCTCATTGTAGGATGTGATGGAGCCTATTCAACTGTCAGATCTCACCTGATGAAGAAA
CCTCGCTTTGATTACAGTCAGCAGTACATTCCTCATGGGTACATGGAGTTGACTATTCCA
CCTAAGAACGGAGATTATGCCATGGAACCTAATTATCTGCATATTTGGCCTAGAAATACC
TTTATGATGATTGCACTTCCTAACATGAACAAATCATTCACATGTACTTTGTTCATGCCC
TTTGAAGAGTTTGAAAAACTTCTAACCAGTAATGATGTGGTAGATTTCTTCCAGAAATAC
TTTCCGGATGCCATCCCTCTAATTGGAGAGAAACTCCTAGTGCAAGATTTCTTCCTGTTG
CCTGCCCAGCCCATGATATCTGTAAAGTGCTCTTCATTTCACTTTAAATCTCACTGTGTA
CTGCTGGGAGATGCAGCTCATGCTATAGTGCCGTTTTTTGGGCAAGGAATGAATGCGGGC
TTTGAAGACTGCTTGGTATTTGATGAGTTAATGGATAAATTCAGTAACGACCTTAGTTTG
TGTCTTCCTGTGTTCTCAAGATTGAGAATCCCAGATGATCACGCGATTTCAGACCTATCC
ATGTACAATTACATAGAGATGCGAGCACATGTCAACTCAAGCTGGTTCATTTTTCAGAAG
AACATGGAGAGATTTCTTCATGCGATTATGCCATCGACCTTTATCCCTCTCTATACAATG
GTCACTTTTTCCAGAATAAGATACCATGAGGCTGTGCAGCGTTGGCATTGGCAAAAAAAG
GTGATAAACAAAGGACTCTTTTTCTTGGGATCACTGATAGCCATCAGCAGTACCTACCTA
CTTATACACTACATGTCACCACGATCTTTCCTCTGCTTGAGAAGACCATGGAACTGGATA
GCTCACTTCCGGAATACAACATGTTTCCCCGCAAAGGCCGTGGACTCCCTAGAACAAATT
TCCAATCTCATTAGCAGGTGA
Enzyme 4 GenBank Gene ID Y13153 Link Image
Enzyme 4 GeneCard ID KMO Link Image
Enzyme 4 GenAtlas ID KMO Link Image
Enzyme 4 HGNC ID HGNC:6381 Link Image
Enzyme 4 Chromosome Location 1
Enzyme 4 Locus 1q42-q44
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References Not Available
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 8585
Enzyme 5 Name Hypothetical protein AADAT
Enzyme 5 Synonyms Not Available
Enzyme 5 Gene Name AADAT
Enzyme 5 Protein Sequence >Hypothetical protein AADAT 
MNYARFITAASAARNPSPIRTMTDILSRGPKSMISLAGGLPNPNMFPFKTAVITVENGKT
IQFGEEMMKRALQYSPSAGIPELLSWLKQLQIKLHNPPTIHYPPSQGQMDLCVTSGSQQG
LCKVFEMIINPGDNVLLDEPAYSGTLQSLHPLGCNIINVASDESGIVPDSLRDILSRWKP
EDAKNPQKNTPKFLYTVPNGNNPTGNSLTSERKKEIYELARKYDFLIIEDDPYYFLQFNK
FRVPTFLSMDVDGRVIRADSFSKIISSGLRIGFLTGPKPLIERVILHIQVSTLHPSTFNQ
LMISQLLHEWGEEGFMAHVDRVIDFYSNQKDAILAAADKWLTGLAEWHVPAAGMFLWIKV
KGINDVKELIEEKAVKMGVLMLPGNAFYVDSSAPSPYLRASFSSASPEQMDVAFQVLAQL
IKESL
Enzyme 5 Number of Residues 425
Enzyme 5 Molecular Weight 47352
Enzyme 5 Theoretical pI 6.96
Enzyme 5 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring nitrogenous groups
Process
  • biosynthesis
  • metabolism
  • physiological process
Component
—
Enzyme 5 General Function Transcription
Enzyme 5 Specific Function Not Available
Enzyme 5 Pathways Not Available
Enzyme 5 Reactions Not Available
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals Not Available
Enzyme 5 Transmembrane Regions Not Available
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 63995204 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID Q4W5N8 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name Q4W5N8_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >1278 bp 
ATGAATTACGCACGGTTCATCACGGCAGCGAGCGCAGCCAGAAACCCTTCTCCCATCCGG
ACCATGACTGACATATTGAGCAGAGGACCAAAATCGATGATCTCCTTGGCTGGTGGCTTA
CCAAATCCAAACATGTTTCCTTTTAAGACTGCCGTAATCACTGTAGAAAATGGAAAGACC
ATCCAATTTGGAGAAGAGATGATGAAGAGAGCACTTCAGTATTCTCCGAGTGCTGGAATT
CCAGAGCTTTTGTCCTGGCTAAAACAGTTACAAATAAAATTGCATAATCCTCCTACCATC
CATTACCCACCCAGTCAAGGACAAATGGATCTATGTGTCACATCTGGCAGCCAACAAGGT
CTTTGTAAGGTGTTTGAAATGATCATTAATCCTGGAGATAATGTCCTCCTAGATGAACCT
GCTTATTCAGGAACTCTTCAAAGTCTGCACCCACTGGGCTGCAACATTATTAATGTTGCC
AGTGATGAAAGTGGGATTGTTCCAGATTCCCTAAGAGACATACTTTCCAGATGGAAACCA
GAAGATGCAAAGAATCCCCAGAAAAACACCCCCAAATTTCTTTATACTGTTCCAAATGGC
AACAACCCTACTGGAAACTCATTAACCAGTGAACGCAAAAAGGAAATCTATGAGCTTGCA
AGAAAATATGATTTCCTCATAATAGAAGATGATCCTTACTATTTTCTCCAGTTTAACAAG
TTCAGGGTACCAACATTTCTTTCCATGGATGTTGATGGACGTGTCATCAGAGCTGACTCT
TTTTCAAAAATCATTTCCTCTGGGTTGAGAATAGGATTTTTAACTGGTCCAAAACCCTTA
ATAGAGAGAGTTATTTTACACATACAAGTTTCAACATTGCACCCCAGCACTTTTAACCAG
CTCATGATATCACAGCTTCTACACGAATGGGGAGAAGAAGGTTTCATGGCTCATGTAGAC
AGGGTTATTGATTTCTATAGTAACCAGAAGGATGCAATACTGGCAGCTGCAGACAAGTGG
TTAACTGGTTTGGCAGAATGGCATGTTCCTGCTGCTGGAATGTTTTTATGGATTAAAGTT
AAAGGCATTAATGATGTAAAAGAACTGATTGAAGAAAAGGCCGTTAAGATGGGGGTATTA
ATGCTCCCTGGAAATGCTTTCTACGTCGATAGCTCAGCTCCTAGCCCTTACTTGAGAGCA
TCCTTCTCTTCAGCTTCTCCAGAACAGATGGATGTGGCCTTCCAGGTATTAGCACAACTT
ATAAAAGAATCTTTATGA
Enzyme 5 GenBank Gene ID AC084866 Link Image
Enzyme 5 GeneCard ID AADAT Link Image
Enzyme 5 GenAtlas ID AADAT Link Image
Enzyme 5 HGNC ID HGNC:17929 Link Image
Enzyme 5 Chromosome Location 4
Enzyme 5 Locus 4q33
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References Not Available
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 13059
Enzyme 6 Name Probable arylformamidase
Enzyme 6 Synonyms
  1. Kynurenine formamidase
  2. KF
Enzyme 6 Gene Name AFMID
Enzyme 6 Protein Sequence >Probable arylformamidase 
MMDVSGVGFPSKVPWKKMSAEELENQYCPSRWVVRLGAEEALRTYSQIGIEATTRARATR
KSLLHVPYGDGEGEKVDIYFPDESSEALPFFLFFHGGYWQSGSKDESAFMVHPLTAQGVA
VVIVAYGIAPKGTLDHMVDQVTRSVAFVQKRYPSNKGIYLCGHSAGAHLAAMMLLADWTK
HGVTPNLRGFFLVSGVFDLEPIVYTSQNVALQLTLEDAQRNNPQLKVAQAQPVDPTCRVL
VVVGQFDSPEFHRQSWEFYQVLPVQTLCQGEWKASFEELHDVDHFEIVENLTQKDNVLTQ
IILKTIFQ
Enzyme 6 Number of Residues 308
Enzyme 6 Molecular Weight 34556
Enzyme 6 Theoretical pI 5.78
Enzyme 6 GO Classification Not Available
Enzyme 6 General Function Lipid transport and metabolism
Enzyme 6 Specific Function Catalyzes the hydrolysis of N-formyl-L-kynurenine to L- kynurenine, the second step in the conversion of tryptophan to nicotinic acid, NAD(H) and NADP(H). Required for elimination of toxic metabolites
Enzyme 6 Pathways
Enzyme 6 Reactions
  • N-formyl-L-kynurenine + H2O = formate + L-kynurenine [RN:R01959] ALL_REAC R01959
  • (other) R00988 R04911
Enzyme 6 Pfam Domain Function Not Available
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 52545961 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID Q63HM1 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name AFMID_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence Not Available
Enzyme 6 GenBank Gene ID BX648442 Link Image
Enzyme 6 GeneCard ID Q63HM1 Link Image
Enzyme 6 GenAtlas ID AFMID Link Image
Enzyme 6 HGNC ID HGNC:20910 Link Image
Enzyme 6 Chromosome Location Not Available
Enzyme 6 Locus Not Available
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References Not Available
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 13118
Enzyme 7 Name Kynureninase
Enzyme 7 Synonyms
  1. L-kynurenine hydrolase
  2. Kynureninase
  3. L-kynurenine hydrolase, isoform CRA_a
Enzyme 7 Gene Name KYNU
Enzyme 7 Protein Sequence >Kynureninase 
MEPSSLELPADTVQRIAAELKCHPTDERVALHLDEEDKLRHFRECFYIPKIQDLPPVDLS
LVNKDENAIYFLGNSLGLQPKMVKTYLEEELDKWAKIAAYGHEVGKRPWITGDESIVGLM
KDIVGANEKEIALMNALTVNLHLLMLSFFKPTPKRYKILLEAKAFPSDHYAIESQLQLHG
LNIEESMRMIKPREGEETLRIEDILEVIEKEGDSIAVILFSGVHFYTGQHFNIPAITKAG
QAKGCYVGFDLAHAVGNVELYLHDWGVDFACWCSYKYLNAGAGGIAGAFIHEKHAHTIKP
ARSEFFN
Enzyme 7 Number of Residues 307
Enzyme 7 Molecular Weight 34635
Enzyme 7 Theoretical pI 5.71
Enzyme 7 GO Classification
Function
  • binding
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on acid carbon-carbon bonds
  • hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances
  • kynureninase activity
  • pyridoxal phosphate binding
  • vitamin binding
Process
  • NAD biosynthesis
  • amino acid and derivative metabolism
  • amino acid derivative metabolism
  • biogenic amine metabolism
  • cellular metabolism
  • coenzyme biosynthesis
  • coenzyme metabolism
  • cofactor metabolism
  • indolalkylamine metabolism
  • metabolism
  • physiological process
  • pyridine nucleotide biosynthesis
  • tryptophan catabolism
  • tryptophan metabolism
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 7 General Function Amino acid transport and metabolism
Enzyme 7 Specific Function Not Available
Enzyme 7 Pathways Not Available
Enzyme 7 Reactions Not Available
Enzyme 7 Pfam Domain Function Not Available
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 12654129 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID Q9BVW3 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name Q9BVW3_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence Not Available
Enzyme 7 GenBank Gene ID BC000879 Link Image
Enzyme 7 GeneCard ID Q9BVW3 Link Image
Enzyme 7 GenAtlas ID KYNU Link Image
Enzyme 7 HGNC ID HGNC:6469 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. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 14702
Enzyme 8 Name Kynurenine--oxoglutarate transaminase 3
Enzyme 8 Synonyms
  1. Kynurenine-- oxoglutarate transaminase III
  2. Kynurenine aminotransferase III
  3. KATIII
  4. Cysteine-S-conjugate beta-lyase 2
Enzyme 8 Gene Name CCBL2
Enzyme 8 Protein Sequence >Kynurenine--oxoglutarate transaminase 3 
MFLAQRSLCSLSGRAKFLKTISSSKILGFSTSAKMSLKFTNAKRIEGLDSNVWIEFTKLA
ADPSVVNLGQGFPDISPPTYVKEELSKIAAIDSLNQYTRGFGHPSLVKALSYLYEKLYQK
QIDSNKEILVTVGAYGSLFNTIQALIDEGDEVILIVPFYDCYEPMVRMAGATPVFIPLRS
KPVYGKRWSSSDWTLDPQELESKFNSKTKAIILNTPHNPLGKVYNREELQVIADLCIKYD
TLCISDEVYEWLVYSGNKHLKIATFPGMWERTITIGSAGKTFSVTGWKLGWSIGPNHLIK
HLQTVQQNTIYTCATPLQEALAQAFWIDIKRMDDPECYFNSLPKELEVKRDRMVRLLESV
GLKPIVPDGGYFIIADVSLLDPDLSDMKNNEPYDYKFVKWMTKHKKLSAIPVSAFCNSET
KSQFEKFVRFCFIKKDSTLDAAEEIIKAWSVQKS
Enzyme 8 Number of Residues 454
Enzyme 8 Molecular Weight 51401
Enzyme 8 Theoretical pI 8.34
Enzyme 8 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring nitrogenous groups
Process
  • biosynthesis
  • metabolism
  • physiological process
Component
—
Enzyme 8 General Function Amino acid transport and metabolism
Enzyme 8 Specific Function Catalyzes the irreversible transamination of the L- tryptophan metabolite L-kinurenine to form kynurenic acid (KA). May catalyze the beta-elimination of S-conjugates and Se- conjugates of L-(seleno)cysteine, resulting in the cleavage of the C-S or C-Se bond
Enzyme 8 Pathways
Enzyme 8 Reactions
  • RS-CH2-CH(NH3+)COO- = RSH + NH3 + pyruvate [RN:R03528] ALL_REAC R03528
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 37542047 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID Q6YP21 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name KAT3_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >1365 bp 
ATGTTTTTGGCCCAGAGGAGCCTCTGCTCTCTTAGCGGTAGAGCAAAATTCCTGAAGACA
ATTTCTTCTTCCAAAATCCTCGGATTCTCTACTTCTGCTAAAATGTCACTGAAATTCACA
AATGCAAAACGGATTGAAGGACTTGATAGTAATGTGTGGATTGAATTTACCAAATTGGCT
GCAGACCCTTCTGTTGTGAATCTTGGCCAAGGCTTTCCAGATATATCCCCTCCTACATAT
GTAAAAGAAGAATTATCAAAGATTGCAGCAATCGATAGCCTGAATCAGTATACACGAGGC
TTTGGCCATCCATCACTTGTGAAAGCTCTGTCCTATCTGTATGAAAAGCTTTATCAAAAG
CAAATTGATTCAAATAAAGAAATCCTTGTGACAGTAGGAGCATATGGATCTCTTTTTAAC
ACCATTCAAGCATTAATTGATGAGGGAGATGAAGTCATACTAATAGTGCCTTTCTATGAC
TGCTATGAGCCCATGGTGAGAATGGCTGGAGCAACACCTGTTTTTATTCCCCTGAGATCT
AAACCTGTTTATGGAAAAAGATGGTCTAGTTCTGACTGGACATTAGATCCTCAAGAACTG
GAAAGTAAATTTAATTCCAAAACCAAAGCTATTATACTAAATACTCCACATAACCCACTT
GGCAAGGTGTATAACAGAGAGGAACTGCAAGTAATTGCTGACCTTTGCATCAAATATGAC
ACACTCTGCATCAGCGATGAGGTTTATGAATGGCTTGTATATTCTGGAAATAAGCACTTA
AAAATAGCTACTTTTCCAGGTATGTGGGAGAGAACAATAACAATAGGAAGTGCTGGAAAG
ACTTTCAGTGTAACTGGCTGGAAGCTTGGCTGGTCCATTGGTCCAAATCATTTGATAAAA
CATTTACAGACAGTTCAACAAAACACGATTTATACTTGTGCAACTCCTTTACAGGAAGCC
TTGGCTCAAGCTTTCTGGATTGACATCAAGCGCATGGATGACCCAGAATGTTACTTTAAT
TCTTTGCCAAAAGAGTTAGAAGTAAAAAGAGATCGGATGGTACGTTTACTTGAAAGTGTT
GGCCTAAAACCCATAGTTCCTGATGGAGGATACTTCATCATCGCTGATGTGTCTTTGCTA
GATCCAGACCTCTCTGATATGAAGAATAATGAGCCTTATGACTATAAGTTTGTGAAATGG
ATGACTAAACATAAGAAACTATCAGCCATCCCCGTTTCAGCATTCTGTAACTCAGAGACT
AAATCACAGTTTGAGAAGTTTGTGCGTTTTTGCTTCATTAAAAAAGACAGCACACTGGAT
GCTGCTGAAGAAATCATCAAGGCATGGAGTGTACAGAAGTCTTGA
Enzyme 8 GenBank Gene ID AY028624 Link Image
Enzyme 8 GeneCard ID Q6YP21 Link Image
Enzyme 8 GenAtlas ID CCBL2 Link Image
Enzyme 8 HGNC ID HGNC:33238 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