Article
Expression, purification, crystallization and preliminary X-ray crystallographic analysis of L-lactate dehydrogenase and its H171C mutant from Bacillus subtilis.
Acta crystallographica. Section F, Structural biology and crystallization communications - 1 Jan 2012
Zhang Yanfeng, Gao Xiaoli
Abstract excerpt
L-Lactate dehydrogenase (LDH) is an important enzyme involved in the last step of glycolysis that catalyzes the reversible conversion of pyruvate to L-lactate with the simultaneous oxidation of NADH to NAD(+). In this study, wild-type LDH from Bacillus subtilis (BsLDH-WT) and the H171C mutant (BsLDH-H171C) were expressed in Escherichia coli and purified to near-homogeneity. BsLDH-WT was crystallized in the...
Topics
- Bacillus subtilis
- Crystallization
- Crystallography, X-Ray
- Gene Expression
- L-Lactate Dehydrogenase
- Mutation