CATH Domain 3fvuA01

CATH Classification

Level	CATH Code	Description
	3	Alpha Beta
	3.90	Alpha-Beta Complex
	3.90.1150	Aspartate Aminotransferase, domain 1
	3.90.1150.10	Aspartate Aminotransferase, domain 1

Domain Context

CATH Clusters

Superfamily	Aspartate Aminotransferase, domain 1
Functional Family	Kynurenine--oxoglutarate transaminase 1

Enzyme Information

2.6.1.64	Glutamine--phenylpyruvate transaminase. based on mapping to UniProt Q16773 L-glutamine + phenylpyruvate = 2-oxoglutaramate + L-phenylalanine. -!- L-methionine, L-histidine and L-tyrosine can act as donors. -!- Has little activity on pyruvate and glyoxylate (cf. EC 2.6.1.15).
4.4.1.13	Cysteine-S-conjugate beta-lyase. based on mapping to UniProt Q16773 An L-cysteine-S-conjugate + H(2)O = RSH + NH(3) + pyruvate. -!- A pyridoxal 5'-phosphate protein. -!- The enzyme is promiscuous regarding the moiety conjugated to L-cysteine, and can accept both aliphatic and aromatic substitutions. -!- The enzyme cleaves a carbon-sulfur bond, releasing a thiol and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia. -!- While bacteria and plants have dedicated enzymes, all of the animal enzymes discovered thus far are bifunctional, most of which also act as aminotransferases. -!- Formerly EC 4.4.1.6 and EC 4.4.1.8.
2.6.1.7	Kynurenine--oxoglutarate transaminase. based on mapping to UniProt Q16773 L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate. -!- Also acts on 3-hydroxykynurenine. -!- The product 4-(2-aminophenyl)-2,4-dioxobutanoate is converted into kynurenate by a spontaneous reaction.

UniProtKB Entries (1)

KAT1_HUMAN

Homo sapiens

Kynurenine--oxoglutarate transaminase 1

PDB Structure

PDB	3FVU
External Links	PDBSum Proteopedia
Method	X-RAY DIFFRACTION
Organism
Primary Citation	Structural insight into the inhibition of human kynurenine aminotransferase I/glutamine transaminase K Han, Q., Robinson, H., Cai, T., Tagle, D.A., Li, J. J.Med.Chem.