Literature summary for 1.1.1.28 extracted from

Razeto, A.; Kochhar, S.; Hottinger, H.; Dauter, M.; Wilson, K.S.; Lamzin, V.S.
Domain closure, substrate specificity and catalysis of D-lactate dehydrogenase from Lactobacillus bulgaricus (2002), J. Mol. Biol., 318, 109-119.

Search for more literature for 1.1.1.28

Crystallization (Commentary)

Crystallization (Comment)	Organism
-	Lactobacillus delbrueckii subsp. bulgaricus

Protein Variants

Protein Variants	Comment	Organism
H296K	no significant changes in kcat or Km value, shift of optimum pH value from 7.0-7.5 to 6	Lactobacillus delbrueckii subsp. bulgaricus

Organism

Organism	UniProt	Comment	Textmining
Lactobacillus delbrueckii subsp. bulgaricus	P26297	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
(R)-lactate + NAD+ = pyruvate + NADH + H+	substrate binding model	Lactobacillus delbrueckii subsp. bulgaricus	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
(R)-lactate + NAD+	-	Lactobacillus delbrueckii subsp. bulgaricus	pyruvate + NADH	-	r
pyruvate + NADH + H+	-	Lactobacillus delbrueckii subsp. bulgaricus	(R)-lactate + NAD+	-	r

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
6	-	mutant H296K	Lactobacillus delbrueckii subsp. bulgaricus
7	7.5	wild-type	Lactobacillus delbrueckii subsp. bulgaricus

Cofactor

Cofactor	Comment	Organism	Structure
NAD+	-	Lactobacillus delbrueckii subsp. bulgaricus
NADH	-	Lactobacillus delbrueckii subsp. bulgaricus

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Release 2023.1 (January 2023)