Some Lactobacillus L-lactate dehydrogenases exhibit comparable catalytic activities for pyruvate and oxaloacetate.
The nonallosteric and allosteric L-lactate dehydrogenases of Lactobacillus pentosus and L. casei, respectively, exhibited broad substrate specificities, giving virtually the same maximal reaction velocity and substrate K(m) values for pyruvate and oxaloacetate. Replacement of Pro101 with Asn reduced the activity of the L. pentosus enzyme toward these alternative substrates to a greater extent than the activity toward pyruvate.
Arai
K
K
Department of Applied Biological Science, Faculty of Science and Technology, Science University of Tokyo, 2641 Yamazaki, Noda, Chiba 278-8510, Japan.
Kamata
T
T
Uchikoba
H
H
Fushinobu
S
S
Matsuzawa
H
H
Taguchi
H
H
D000595:Amino Acid Sequence; D020134:Catalytic Domain; D007700:Kinetics; D007770:L-Lactate Dehydrogenase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D007778:Lactobacillus / Q000201:enzymology*; D007780:Lacticaseibacillus casei / Q000201:enzymology; D008969:Molecular Sequence Data; D062907:Oxaloacetic Acid / Q000378:metabolism*; D019289:Pyruvic Acid / Q000378:metabolism*; D013379:Substrate Specificity
D062907:Oxaloacetic Acid; D019289:Pyruvic Acid; D007770:L-Lactate Dehydrogenase