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Literature summary 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.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.1.28
-
 Lactobacillus delbrueckii subsp. bulgaricus

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.28 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

EC Number Organism UniProt Comment Textmining
1.1.1.28 Lactobacillus delbrueckii subsp. bulgaricus P26297
-
-

Reaction

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

Substrates and Products (Substrate)

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

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.28 6
-
 mutant H296K Lactobacillus delbrueckii subsp. bulgaricus
1.1.1.28 7 7.5 wild-type Lactobacillus delbrueckii subsp. bulgaricus

Cofactor

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