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Tchem
KYNU
Kynureninase

Protein Classes
Protein Summary
Description
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. Kynureninase is a pyridoxal-5'-phosphate (pyridoxal-P) dependent enzyme that catalyzes the cleavage of L-kynurenine and L-3-hydroxykynurenine into anthranilic and 3-hydroxyanthranilic acids, respectively. Kynureninase is involved in the biosynthesis of NAD cofactors from tryptophan through the kynurenine pathway. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Nov 2010]
Uniprot Accession IDs
Gene Name
Ensembl ID
  • ENST00000264170
  • ENSP00000264170
  • ENSG00000115919
  • ENST00000375773
  • ENSP00000364928
  • ENST00000409512
  • ENSP00000386731

Symbol
  • KYNUU
  • VCRL2
Illumination Graph
Knowledge Table
Most Knowledge About
Knowledge Value (0 to 1 scale)
gene perturbation
0.94
small molecule perturbation
0.93
virus perturbation
0.88
PubMedID
0.87
trait
0.86


IDG Development Level Summary
Tdark

These are targets about which virtually nothing is known. They do not have known drug or small molecule activities
- AND - satisfy two or more of the following criteria:

Pubmed score: 39.25   (req: < 5)
Gene RIFs: 6   (req: <= 3)
Antibodies: 262   (req: <= 50)
Tbio

These targets do not have known drug or small molecule activities
- AND - satisfy two or more of the following criteria:

Pubmed score: 39.25   (req: >= 5)
Gene RIFs: 6   (req: > 3)
Antibodies: 262   (req: > 50)

- OR - satisfy the following criterion:

Gene Ontology Terms: 15
Tchem

Target has at least one ChEMBL compound with an activity cutoff of < 30 nM - AND - satisfies the preceding conditions

Active Ligands: 3
Tclin

Target has at least one approved drug - AND - satisfies the preceding conditions

Active Drug: 0
Protein Data Bank (2)
1 – 2 of 2
PDB Structure Id
Ligand
Method
Resolution (Å)
M.W. (kDa)
Pub Year
Title
PDB Structure Id
M.W.
Resolution
Pub Year
Pathways (15)
Metabolism (R-HSA-1430728)

Click on a row in the table to change the structure displayed.

Items per page:
1 – 3 of 3
Data Source
Name
Explore in Pharos
Explore in Source
Reactome
Metabolism
Reactome
Metabolism of amino acids and derivatives
Reactome
Tryptophan catabolism
Name
Explore in Pharos
Explore in Source
Metabolism
Metabolism of amino acids and derivatives
Tryptophan catabolism
Protein-Protein Interactions (105)
1 – 10 of 105
KMO
Tchem
Family: Enzyme
Novelty: 0.00558444
Score: 0.999
Data Source: STRINGDB
HAAO
Tbio
Family: Enzyme
Novelty: 0.02398057
Score: 0.998
Data Source: STRINGDB
TDO2
Tchem
Family: Enzyme
Novelty: 0.00123905
Score: 0.996
Data Source: STRINGDB
KYAT1
Tbio
Family: Enzyme
Novelty: 0.01429382
Score: 0.988
Data Source: STRINGDB
AADAT
Tchem
Family: Enzyme
Novelty: 0.0054217
Score: 0.982
Data Source: STRINGDB
KYAT3
Tbio
Family: Enzyme
Novelty: 0.09558489
Score: 0.982
Data Source: STRINGDB
AFMID
Tbio
Family: Enzyme
Novelty: 0.02056908
Score: 0.973
Data Source: STRINGDB
IDO1
Tchem
Family: Enzyme
Novelty: 0.00188077
Score: 0.972
Data Source: STRINGDB
IDO2
Tchem
Family: Enzyme
Novelty: 0.01019298
Score: 0.97
Data Source: STRINGDB
ACMSD
Tbio
Family: Enzyme
Novelty: 0.01978706
Score: 0.919
Data Source: STRINGDB
Publication Statistics
PubMed Score  39.25

PubMed score by year
PubTator Score  22.22

PubTator score by year
Amino Acid Sequence
Residue Counts
Protein Sequence
ProtVista Viewer
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