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Enzymatic Characterization of Bacillus cereus Lactate Dehydrogenase Isozymes Expressed in Escherichia coli  

Jang, Myoung-Uoon (Department of Food Science and Technology, Chungbuk National University)
Park, Jung-Mi (Department of Food Science and Technology, Chungbuk National University)
Lee, Hong-Gyun (Department of Food Science and Technology, Chungbuk National University)
Lee, So-Ra (Department of Food Science and Technology, Chungbuk National University)
Kim, Tae-Jip (Department of Food Science and Technology, Chungbuk National University)
Publication Information
Korean Journal of Microbiology / v.46, no.2, 2010 , pp. 213-218 More about this Journal
Abstract
Lactate dehydrogenases (LDHs) have been highly focused for long time, due to their important roles in biochemical and metabolic pathways of cells. On the basis of genome-wide searching results, three putative LDH genes from Bacillus cereus ATCC 14579 genome have been PCR-amplified, cloned, and well-expressed in E. coli. All three BcLDH isozymes are supposed to share highly conserved catalytic amino acid residues in common $NAD^+$-dependent LDHs. Meanwhile, BcLDH1 consisting of 314 amino acids shares 86 and 49% of identities with BcLDH2 and 3, respectively. Interestingly, only BcLDH1 showed the converting activities between L-lactate and pyruvate in the presence of $NAD^+$ coenzyme, while the other isozymes are likely to have almost no activity. As a result, it was revealed that BcLDH1 can be a typical $NAD^+$-dependent L-lactate-specific dehydrogenase.
Keywords
B. cereus; expression; gene cloning; L-lactate dehydrogenase (L-LDH); $NAD^+$-dependent activity;
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