P70712 · KYNU_RAT

Function

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.

Catalytic activity

Cofactor

pyridoxal 5'-phosphate (UniProtKB | Rhea| CHEBI:597326 )

Activity regulation

Inhibited by o-methylbenzoylalanine (OMBA).

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
440 μML-kynurenine
32 μMDL-3-hydroxykynurenine

pH Dependence

Optimum pH is about 9.0 with L-kynurenine as substrate, and about 8.5 with DL-3-hydroxykynurenine as substrate.

Pathway

Amino-acid degradation; L-kynurenine degradation; L-alanine and anthranilate from L-kynurenine: step 1/1.
Cofactor biosynthesis; NAD+ biosynthesis; quinolinate from L-kynurenine: step 2/3.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site137pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site138pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site165-168pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site221pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site250pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site253pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site275pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site305pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site333pyridoxal 5'-phosphate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentcytosol
Cellular Componentmitochondrion
Molecular Function3-hydroxykynureninase activity
Molecular Functionkynureninase activity
Molecular Functionprotein homodimerization activity
Molecular Functionpyridoxal phosphate binding
Biological Process'de novo' NAD biosynthetic process from tryptophan
Biological Processanthranilate metabolic process
Biological ProcessL-kynurenine catabolic process
Biological ProcessNAD biosynthetic process
Biological Processquinolinate biosynthetic process
Biological Processresponse to type II interferon
Biological Processresponse to vitamin B6
Biological Processtryptophan catabolic process
Biological Processtryptophan catabolic process to acetyl-CoA
Biological Processtryptophan catabolic process to kynurenine

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Kynureninase
  • EC number
  • Alternative names
    • L-kynurenine hydrolase

Gene names

    • Name
      Kynu

Organism names

  • Taxonomic identifier
  • Strain
    • Wistar
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus

Accessions

  • Primary accession
    P70712
  • Secondary accessions
    • Q68G25
    • Q7M0D0
    • Q9QW90

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Phenotypes & Variants

PTM/Processing

Features

Showing features for modified residue, chain.

TypeIDPosition(s)Description
Modified residue1N-acetylmethionine
ChainPRO_00002186591-464Kynureninase
Modified residue276N6-(pyridoxal phosphate)lysine

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

High levels in liver and kidney. Also detected in heart, retina, ovary. Lung, testis and brain.

Induction

Inhibited by thiol reagents and heavy metal ions.

Gene expression databases

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Chemistry

Structure

Family & Domains

Sequence similarities

Belongs to the kynureninase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    464
  • Mass (Da)
    52,470
  • Last updated
    2004-11-09 v2
  • Checksum
    1490A74EFF7287AC
MEPSPLELPVDAVRRIATELNCDPTDERVALRLDEEDKLKRFKDCFYIPKMRDLPSIDLSLVNEDDNAIYFLGNSLGLQPKMVKTYLEEELDKWAKIGAYGHEVGKRPWIIGDESIVSLMKDIVGAHEKEIALMNALTVNLHLLLLSFFKPTPKRHKILLEAKAFPSDHYAIESQIQLHGLDVEKSMRMIKPREGEETLRMEDILEVIEKEGDSIAVVLFSGLHFYTGQLFNIPAITQAGHAKGCFVGFDLAHAVGNVELHLHDWDVDFACWCSYKYLNSGAGGLAGAFIHEKHAHTIKPALVGWFGHELSTRFNMDNKLQLIPGVNGFRISNPPILLVCSLHASLEIFQQATMTALRRKSILLTGYLEYLLKHYHGGNDTENKRPVVNIITPSRAEERGCQLTLTFSISKKGVFKELEKRGVVCDKREPEGIRVAPVPLYNSFHDVYKFIRLLTAILDSTERN

Computationally mapped potential isoform sequences

There are 3 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A8L2QQS0A0A8L2QQS0_RATKynu465
A0A8I6A2I1A0A8I6A2I1_RATKynu480
A0A8I5ZW86A0A8I5ZW86_RATKynu432

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict18in Ref. 2; AAC53206
Sequence conflict26in Ref. 1; AA sequence
Sequence conflict118in Ref. 2; AAC53206

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U68168
EMBL· GenBank· DDBJ
AAC53206.1
EMBL· GenBank· DDBJ
mRNA
BC078762
EMBL· GenBank· DDBJ
AAH78762.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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