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Identification
HMDB Protein ID HMDBP00325
Secondary Accession Numbers
  • 5561
  • HMDBP04409
  • HMDBP07418
Name Kynureninase
Synonyms
  1. L-kynurenine hydrolase
  2. SubName: Kynureninase (L-kynurenine hydrolase), isoform CRA_a
Gene Name KYNU
Protein Type Unknown
Biological Properties
General Function Involved in metabolic process
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.
Pathways
  • L-kynurenine degradation
  • NAD(+) biosynthesis
  • Tryptophan Metabolism
  • Tryptophan metabolism
Reactions
L-Kynurenine + Water → 2-Aminobenzoic acid + L-Alanine details
L-3-Hydroxykynurenine + Water → 3-Hydroxyanthranilic acid + L-Alanine details
L-Formylkynurenine + Water → Formylanthranilic acid + L-Alanine details
GO Classification
Biological Process
NAD biosynthetic process
quinolinate biosynthetic process
tryptophan catabolic process
anthranilate metabolic process
response to vitamin B6
tryptophan catabolic process to acetyl-CoA
tryptophan catabolic process to kynurenine
response to interferon-gamma
L-kynurenine catabolic process
Cellular Component
cytosol
mitochondrion
nucleus
Component
cell part
intracellular part
cytoplasm
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
cofactor binding
pyridoxal phosphate binding
Molecular Function
kynureninase activity
pyridoxal phosphate binding
protein homodimerization activity
Process
metabolic process
coenzyme biosynthetic process
pyridine nucleotide biosynthetic process
nicotinamide nucleotide biosynthetic process
nad biosynthetic process
indolalkylamine metabolic process
tryptophan metabolic process
tryptophan catabolic process
cellular metabolic process
cellular amino acid derivative metabolic process
cofactor metabolic process
cellular biogenic amine metabolic process
coenzyme metabolic process
cellular amino acid and derivative metabolic process
Cellular Location
  1. Cytoplasmic
  2. Cytoplasm
Gene Properties
Chromosome Location 2
Locus 2q22.2
SNPs KYNU
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
Protein Properties
Number of Residues 465
Molecular Weight 34634.47
Theoretical pI 5.845
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Kynureninase
MEPSSLELPADTVQRIAAELKCHPTDERVALHLDEEDKLRHFRECFYIPKIQDLPPVDLS
LVNKDENAIYFLGNSLGLQPKMVKTYLEEELDKWAKIAAYGHEVGKRPWITGDESIVGLM
KDIVGANEKEIALMNALTVNLHLLMLSFFKPTPKRYKILLEAKAFPSDHYAIESQLQLHG
LNIEESMRMIKPREGEETLRIEDILEVIEKEGDSIAVILFSGVHFYTGQHFNIPAITKAG
QAKGCYVGFDLAHAVGNVELYLHDWGVDFACWCSYKYLNAGAGGIAGAFIHEKHAHTIKP
ALVGWFGHELSTRFKMDNKLQLIPGVCGFRISNPPILLVCSLHASLEIFKQATMKALRKK
SVLLTGYLEYLIKHNYGKDKAATKKPVVNIITPSHVEERGCQLTITFSVPNKDVFQELEK
RGVVCDKRNPNGIRVAPVPLYNSFHDVYKFTNLLTSILDSAETKN
GenBank ID Protein 12654129
UniProtKB/Swiss-Prot ID Q16719
UniProtKB/Swiss-Prot Entry Name KYNU_HUMAN
PDB IDs
GenBank Gene ID U57721
GeneCard ID KYNU
GenAtlas ID KYNU
HGNC ID HGNC:6469
References
General References
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  3. 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:8706755 ]
  4. 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:9180257 ]
  5. 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:11985583 ]
  6. 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:17300176 ]
  7. 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:17334708 ]
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