P70712 · KYNU_RAT
- ProteinKynureninase
- GeneKynu
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids464 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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
- H2O + L-kynurenine = anthranilate + H+ + L-alanine
Cofactor
Activity regulation
Inhibited by o-methylbenzoylalanine (OMBA).
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
440 μM | L-kynurenine | |||||
32 μM | DL-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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 137 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 138 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 165-168 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: FPSD | ||||||
Binding site | 221 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 250 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 253 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 275 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 305 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 333 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: N |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | mitochondrion | |
Molecular Function | 3-hydroxykynureninase activity | |
Molecular Function | kynureninase activity | |
Molecular Function | protein homodimerization activity | |
Molecular Function | pyridoxal phosphate binding | |
Biological Process | 'de novo' NAD biosynthetic process from tryptophan | |
Biological Process | anthranilate metabolic process | |
Biological Process | L-kynurenine catabolic process | |
Biological Process | NAD biosynthetic process | |
Biological Process | quinolinate biosynthetic process | |
Biological Process | response to type II interferon | |
Biological Process | response to vitamin B6 | |
Biological Process | tryptophan catabolic process | |
Biological Process | tryptophan catabolic process to acetyl-CoA | |
Biological Process | tryptophan catabolic process to kynurenine |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameKynureninase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionP70712
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Chemistry
PTM/Processing
Features
Showing features for modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 1 | N-acetylmethionine | ||||
Sequence: M | ||||||
Chain | PRO_0000218659 | 1-464 | Kynureninase | |||
Sequence: MEPSPLELPVDAVRRIATELNCDPTDERVALRLDEEDKLKRFKDCFYIPKMRDLPSIDLSLVNEDDNAIYFLGNSLGLQPKMVKTYLEEELDKWAKIGAYGHEVGKRPWIIGDESIVSLMKDIVGAHEKEIALMNALTVNLHLLLLSFFKPTPKRHKILLEAKAFPSDHYAIESQIQLHGLDVEKSMRMIKPREGEETLRMEDILEVIEKEGDSIAVVLFSGLHFYTGQLFNIPAITQAGHAKGCFVGFDLAHAVGNVELHLHDWDVDFACWCSYKYLNSGAGGLAGAFIHEKHAHTIKPALVGWFGHELSTRFNMDNKLQLIPGVNGFRISNPPILLVCSLHASLEIFQQATMTALRRKSILLTGYLEYLLKHYHGGNDTENKRPVVNIITPSRAEERGCQLTLTFSISKKGVFKELEKRGVVCDKREPEGIRVAPVPLYNSFHDVYKFIRLLTAILDSTERN | ||||||
Modified residue | 276 | N6-(pyridoxal phosphate)lysine | ||||
Sequence: K |
Keywords
- PTM
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
Structure
Sequence
- Sequence statusComplete
- Length464
- Mass (Da)52,470
- Last updated2004-11-09 v2
- Checksum1490A74EFF7287AC
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8L2QQS0 | A0A8L2QQS0_RAT | Kynu | 465 | ||
A0A8I6A2I1 | A0A8I6A2I1_RAT | Kynu | 480 | ||
A0A8I5ZW86 | A0A8I5ZW86_RAT | Kynu | 432 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 18 | in Ref. 2; AAC53206 | ||||
Sequence: T → A | ||||||
Sequence conflict | 26 | in Ref. 1; AA sequence | ||||
Sequence: D → N | ||||||
Sequence conflict | 118 | in Ref. 2; AAC53206 | ||||
Sequence: S → T |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U68168 EMBL· GenBank· DDBJ | AAC53206.1 EMBL· GenBank· DDBJ | mRNA | ||
BC078762 EMBL· GenBank· DDBJ | AAH78762.1 EMBL· GenBank· DDBJ | mRNA |