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KMID : 0364820100460020213
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Korean Journal of Microbiology
2010 Volume.46 No. 2 p.213 ~ p.218
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Enzymatic Characterization of Bacillus cereus Lactate Dehydrogenase Isozymes Expressed in Escherichia coli
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Jang Myoung-Uoon
Park Jung-Mi
Lee Hong-Gyun
Lee So-Ra
Kim Tae-Jip
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Abstract
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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.
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KEYWORD
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B. cereus, expression, gene cloning, L-lactate dehydrogenase (L-LDH), NAD+-dependent activity
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