Literature summary for 4.3.1.18 extracted from

Marceau, M.; Lewis, S.D.; Shafer, J.A.
The glycine-rich region of Escherichia coli D-serine dehydratase. Altered interactions with pyridoxal 5'-phosphate produced by substitutions of aspartic acid for glycine (1988), J. Biol. Chem., 263, 16934-16941.

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Protein Variants

Protein Variants	Comment	Organism
G279D	mutant G279D and G281D, loss of activity, the mutant enzymes form a Schiff base linkage with pyridoxal 5'-phosphate but do not hold the cofactor in a catalytically competent orientation. G279D has 225fold reduced cofactor affinity, the ability to retain a cofactor:glycine complex is decreased 765fold. Mutant G281D has 50fold decreased cofactor affinity, the ability to retain a cofactor:glycine complex is decreased 1970fold	Escherichia coli
G281D	mutant G279D and G281D, loss of activity, the mutant enzymes form a Schiff base linkage with pyridoxal 5'-phosphate but do not hold the cofactor in a catalytically competent orientation. G279D has 225fold reduced cofactor affinity, the ability to retain a cofactor:glycine complex is decreased 765fold. Mutant G281D has 50fold decreased cofactor affinity, the ability to retain a cofactor:glycine complex is decreased 1970fold	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
D-serine	-	Escherichia coli	pyruvate + NH3	-	?

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Release 2023.1 (January 2023)