Literature summary for 1.1.1.274 extracted from

Khurana, S.; Sanli, G.; Powers, D.B.; Anderson, S.; Blaber, M.
Molecular modeling of substrate binding in wild-type and mutant Corynebacteria 2,5-diketo-D-gluconate reductases (2000), Proteins, 39, 68-75.

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Protein Variants

Protein Variants	Comment	Organism
F22Y	isoenzyme A, similar kcat as wild-type	Corynebacterium sp.
Q192R	isoenzyme A, 2.5fold increase in kcat	Corynebacterium sp.

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.0123	-	2,5-didehydro-D-gluconate	isoenzyme A, F22Y mutant enzyme	Corynebacterium sp.
0.0312	-	2,5-didehydro-D-gluconate	isoenzyme A, wild-type	Corynebacterium sp.

Organism

Organism	UniProt	Comment	Textmining
Corynebacterium sp.	-	isoenzyme A	-

Reaction

Reaction	Comment	Organism	Reaction ID
2-dehydro-D-gluconate + NADP+ = 2,5-didehydro-D-gluconate + NADPH + H+	reaction mechanism	Corynebacterium sp.	a

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Release 2023.1 (January 2023)