Reactome | PXLP-KYAT1 dimer transaminates L-KYN to KYNA

PXLP-KYAT1 dimer transaminates L-KYN to KYNA

Stable Identifier

R-HSA-893596

Type

Reaction [transition]

Species

Homo sapiens

Compartment

cytosol

Synonyms

L-kynurenine + 2-oxoglutarate => kynurenate + L-glutamate + H2O

ReviewStatus

5/5

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PXLP-KYAT1 dimer transaminates L-KYN to KYNA

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Kynurenine-oxoglutarate transaminase 1 (KYAT1, also known as CCBL) catalyzes the reaction of kynurenine (L-KYN) and 2-oxoglutarate (2OG) to form kynurenate (KYNA), L-glutamate, and water, in a two-step reaction involving an unstable intermediate, 4-(2-aminophenyl)-2,4-dioxobutanoate. The active form of KYAT1 is a homodimer with one molecule of pyridoxal phosphate (PXLP) bound to each monomer (Baran et al. 1994, Han et al. 2009, Rossi et al. 2004). The enzyme's cytosolic localization is inferred from that of recombinant protein overexpressed in transfected cells (Perry et al. 1995).

The alpha keto acids indole-3-propionic acid (I3PROPA) and indole-3-lactic acid (I3LACT) are potent inhibitors of KYAT1 (Han et al. 2009). Phenylalanine is an effective competitive inhibitor of kynurenine aminotransferase 1 (Han et al. 2004).

Literature References

PubMed ID	Title	Journal	Year
13069505	The transamination of kynurenine Miller, IL, Adelberg, EA, Tsuchida, M	J Biol Chem	1953
19338303	Structural insight into the inhibition of human kynurenine aminotransferase I/glutamine transaminase K Cai, T, Robinson, H, Li, J, Tagle, DA, Han, Q	J Med Chem	2009
7883047	Molecular cloning and expression of a cDNA for human kidney cysteine conjugate beta-lyase Scholfield, C, Perry, S, King, L, Harries, H, Goldfarb, P, Gibson, G, Lock, T	FEBS Lett	1995
15364907	Crystal structure of human kynurenine aminotransferase I Li, J, Li, J, Rizzi, M, Han, Q, Rossi, F	J Biol Chem	2004
8294935	Purification and characterization of kynurenine aminotransferase I from human brain Baran, H, Kido, R, Okuno, E, Schwarcz, R	J Neurochem	1994