Properties of d-lactate dehydrogenase fromLactobacillus bulgaricus: a possible different evolutionary origin for the d- and l-lactate dehydrogenases

Autor:	Gisèle Le Bras, Jean-Renaud Garel
Rok vydání:	1991
Předmět:	chemistry.chemical_classification Molecular mass Dehydrogenase Biology biology.organism_classification Microbiology chemistry.chemical_compound Enzyme chemistry Biochemistry Oxidoreductase Lactobacillus Lactate dehydrogenase Genetics D-lactate dehydrogenase Specific activity Molecular Biology
Zdroj:	FEMS Microbiology Letters. 79:89-94
ISSN:	1574-6968 0378-1097
DOI:	10.1111/j.1574-6968.1991.tb04510.x
Popis:	The NAD-dependent d-lactate dehydrogenase from Lactobacillus bulgaricus has been purified to homogeneity. This enzyme was a dimer made of two identical chains of molecular mass 37 000. Saturation by either substrate was hyperbolic, with Km values of 50 μM for NADH and 1 mM for pyruvate. The specific activity was 2200 units/mg and was not affected by the presence of fructose-1,6-bisphosphate, Mn2+ ions, ATP or ADP. The amino-terminal sequence determined on 50 residues showed no significant homology with known lactate dehydrogenases, suggesting that the d-lactate lactate dehydrogenase from L. bulgaricus could not be evolutionarily related to the family of NAD-dependent l-lactate dehydrogenases.
Databáze:	OpenAIRE
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