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kynurenine-oxoglutarate transaminase 1 (kynurenine aminotransferase 1, KATI, glutamine-phenylpyruvate transaminase, glutamine transaminase K, GTK, cysteine-S-conjugate beta-lyase, CCBL1)
Function:
1) glutamine catabolism
2) catalyzes irreversible transamination of L-tryptophan metabolite L-kinurenine to form kynurenic acid
3) metabolizes cysteine conjugates of certain halogenated alkenes & alkanes to form reactive metabolites
4) catalyzes the beta-elimination of S-conjugates & Se-conjugates of L-(seleno)cysteine, resulting in cleavage of the C-S or C-Se bond
L-kynurenine + 2-oxoglutarate
4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate
L-glutamine + phenylpyruvate
2-oxoglutaramate + L-phenylalanine
RS-CH2-CH(NH3+)-COO- RSH + NH3 + pyruvate
Cofactor: pyridoxal phosphate
Structure:
1) homodimer
2) belongs to the class-1 pyridoxal-phosphate-dependent aminotransferase family
Compartment: cytoplasm
Alternative splicing: named isoforms=3
General
enzyme
Properties
SIZE: MW = 48 kD
entity length = 422 aa
COMPARTMENT: cytoplasm
MOTIF: cofactor-binding site [247-247]
FOR-BINDING-OF: pyridoxal phosphate
Database Correlations
OMIM 600547
UniProt Q16773
Pfam PF00155
ENZYME correlations
References
UniProt :accession Q16773