| Literature DB >> 11114942 |
K Arai1, T Kamata, H Uchikoba, S Fushinobu, H Matsuzawa, H Taguchi.
Abstract
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.Entities:
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Year: 2001 PMID: 11114942 PMCID: PMC94891 DOI: 10.1128/JB.183.1.397-400.2001
Source DB: PubMed Journal: J Bacteriol ISSN: 0021-9193 Impact factor: 3.490