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Human Metabolome Database Version 2.5

 

Showing metabocard for L-3-Hydroxykynurenine (HMDB11631)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2009-01-30 14:47:12
Update Date 2009-06-09 11:13:54
Accession Number HMDB11631
Secondary Accession Numbers Not Available
Common Name L-3-Hydroxykynurenine
Description L-3-Hydroxykynurenine (L-3-HK) is a metabolite in the kynurenine pathway, the major route of tryptophan degradation in mammals. Kynurenine 3-monooxygenase, an NADPH-dependent flavin monooxygenase, catalyses the hydroxylation of L-kynurenine to L-3-hydroxykynurenine. 3-hydroxykynurenine can be converted to 3-hydroxyanthranilate by the enzyme 3-hydroxykinureninase. It may also be converted to 4-(2-amino-3-hydroxphenyl)-2,4-dioxobutanoate by the enzyme kynurenine-oxoglutarate transaminase. L-3-Hydroxykynurenine (L-3-HK) is a known generator of highly reactive free radicals. An elevation of L-3-HK levels has been shown to constitute a significant hazard in situations of excitotoxic injury. In particular, L-3-HK may contribute to the neuronal deficits underlying HIV-associated dementia (PMID: 7830088). Pharmacological interventions aimed at decreasing L-3-HK formation may therefore be particularly useful for the treatment of neurological diseases which are associated with an abnormally enhanced flux through the kynurenine pathway (PMID: 10583474)
Synonyms
  1. 3-Hydroxy-L-kynurenine
  2. 3-(3-hydroxyanthraniloyl)-L-alanine
  3. 3-(2-amino-3-hydroxybenzoyl)-L-alanine
  4. L-3-HK
Chemical IUPAC Name (2S)-2-amino-4-(2-amino-3-hydroxyphenyl)-4-oxobutanoic acid
Chemical Formula C10H12N2O4
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
—
Class
—
Sub Class
—
Family
  • Mammalian Metabolite
Species
  • ketone
  • phenol or hydroxyhetarene
  • primary amine
  • primary aliphatic amine (alkylamine)
  • primary aromatic amine
  • carboxylic acid
  • aromatic compound
  • alpha-aminoacid
Biofunction
—
Application
—
Source
  • Endogenous
Average Molecular Weight 224.213
Monoisotopic Molecular Weight 224.079712
Isomeric SMILES N[C@@H](CC(=O)C1=CC=CC(O)=C1N)C(O)=O
Canonical SMILES NC(CC(=O)C1=CC=CC(O)=C1N)C(O)=O
KEGG Compound ID C03227 Link Image
BioCyc ID 3-HYDROXY-L-KYNURENINE Link Image
BiGG ID Not Available
Wikipedia Link Not Available
NuGOwiki Link HMDB11631 Link Image
Metagene Link HMDB11631 Link Image
METLIN ID Not Available
PubChem Compound 11811 Link Image
PubChem Substance 6099 Link Image
ChEBI ID 17380 Link Image
CAS Registry Number 606-14-4
InChI Identifier InChI=1/C10H12N2O4/c11-6(10(15)16)4-8(14)5-2-1-3-7(13)9(5)12/h1-3,6,13H,4,11-12H2,(H,15,16)/t6-/m0/s1
Synthesis Reference Not Available
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 3.33 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -2.09 [Predicted by ALOGPS] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show Link Image
SDF File Show Link Image
PDB File Show Link Image
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Not Available
Not Available
Predicted 13C NMR Spectrum Not Available
Not Available
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location Not Available
Biofluid Location
  • Urine
Tissue Location Not Available
Concentrations (Normal)
Biofluid Urine
Value 2.2 (1.0-3.4) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 130. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp. Basel, Switzerland c1981-1992.
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Tryptophan Metabolism SMP00063 Link Image map00380 Link Image
General References Not Available
Metabolic Enzymes
  1. Kynureninase
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 52351.1
Enzyme 1 Theoretical pI 7.04
Enzyme 1 GO Classification
Function
  • binding
  • catalytic activity
  • cofactor binding
  • 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
Process
  • NAD biosynthetic process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid derivative metabolic process
  • cellular biogenic amine metabolic process
  • cellular metabolic process
  • coenzyme biosynthetic process
  • coenzyme metabolic process
  • cofactor metabolic process
  • indolalkylamine metabolic process
  • metabolic process
  • nicotinamide nucleotide biosynthetic process
  • pyridine nucleotide biosynthetic process
  • tryptophan catabolic process
  • tryptophan metabolic process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 1 General Function Involved in metabolic process
Enzyme 1 Specific Function Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3- hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3- hydroxyanthranilic acid (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 [RN:R00987]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein Not Available
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]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Walsh HA, Botting NP: Purification and biochemical characterization of some of the properties of recombinant human kynureninase. Eur J Biochem. 2002 Apr;269(8):2069-74. [PubMed Link Image]
  5. Lima S, Khristoforov R, Momany C, Phillips RS: Crystal structure of Homo sapiens kynureninase. Biochemistry. 2007 Mar 13;46(10):2735-44. Epub 2007 Feb 15. [PubMed Link Image]
  6. Christensen M, Duno M, Lund AM, Skovby F, Christensen E: Xanthurenic aciduria due to a mutation in KYNU encoding kynureninase. J Inherit Metab Dis. 2007 Apr;30(2):248-55. Epub 2007 Mar 1. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available