Literature summary for 2.6.1.7 extracted from

Han, Q.; Gao, Y.G.; Robinson, H.; Li, J.
Structural insight into the mechanism of substrate specificity of Aedes kynurenine aminotransferase (2008), Biochemistry, 47, 1622-1630.

Crystallization (Commentary)

Crystallization (Comment)	Organism
Comparison of the active site residues of the Aedes aegypti enzyme-cysteine structure with those of the human isoform KAT I-phenylalanine structure reveals that Tyr286 in the Aedes aegypti enzyme is changed to Phe278 in the human enzyme, which may explain why the Aedes aegypti enzyme transaminates hydrophilic amino acids more efficiently than the human enzyme does	Homo sapiens
in complex with its best amino acid substrates, glutamine and cysteine. Glutamine is found in both subunits of the biological dimer, and cysteine is found in one of the two subunits. Both substrates form external aldemines with pyridoxal 5'-phosphate in the structures. All the units with substrate are in the closed conformation form, and the unit without substrate is in the open form. Tyr286 in the Aedes aegypti enzyme is changed to Phe278 in the human enzyme, which may explain why the Aedes enzyme transaminates hydrophilic amino acids more efficiently than the human enzyme does	Aedes aegypti

Crystallization (Comment)

Organism

Comparison of the active site residues of the Aedes aegypti enzyme-cysteine structure with those of the human isoform KAT I-phenylalanine structure reveals that Tyr286 in the Aedes aegypti enzyme is changed to Phe278 in the human enzyme, which may explain why the Aedes aegypti enzyme transaminates hydrophilic amino acids more efficiently than the human enzyme does

Homo sapiens

in complex with its best amino acid substrates, glutamine and cysteine. Glutamine is found in both subunits of the biological dimer, and cysteine is found in one of the two subunits. Both substrates form external aldemines with pyridoxal 5'-phosphate in the structures. All the units with substrate are in the closed conformation form, and the unit without substrate is in the open form. Tyr286 in the Aedes aegypti enzyme is changed to Phe278 in the human enzyme, which may explain why the Aedes enzyme transaminates hydrophilic amino acids more efficiently than the human enzyme does

Aedes aegypti

Organism

Organism	UniProt	Comment	Textmining
Aedes aegypti	-	-	-
Homo sapiens	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-cysteine + 2-oxobutanoate	-	Aedes aegypti	2-aminobutanoate + 3-mercapto-2-oxopropanoate	-	?
L-glutamine + 2-oxobutanoate	-	Aedes aegypti	2-oxoglutarate + 2-aminobutanoate	-	?

Cofactor

Cofactor	Comment	Organism	Structure
pyridoxal 5'-phosphate	-	Aedes aegypti

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Release 2023.1 (January 2023)