title: Relative catalytic efficiency of ldhL- and ldhD-encoded products is crucial for optical purity of lactic acid produced by lactobacillus strains.
abstract: NAD-dependent l- and d-lactate dehydrogenases coexist in Lactobacillus genomes and may convert pyruvic acid into l-lactic acid and d-lactic acid, respectively. Our findings suggest that the relative catalytic efficiencies of ldhL- and ldhD-encoded products are crucial for the optical purity of lactic acid produced by Lactobacillus strains.
authors.affiliation: State Key Laboratory of Microbial Technology, Shandong University, Jinan, People’s Republic of China.
authors.forename: Zhaojuan
authors.initials: Z
authors.lastname: Zheng
authors.forename: Binbin
authors.initials: B
authors.lastname: Sheng
authors.forename: Cuiqing
authors.initials: C
authors.lastname: Ma
authors.forename: Haiwei
authors.initials: H
authors.lastname: Zhang
authors.forename: Chao
authors.initials: C
authors.lastname: Gao
authors.forename: Fei
authors.initials: F
authors.lastname: Su
authors.forename: Ping
authors.initials: P
authors.lastname: Xu
mesh_terms: D007770:L-Lactate Dehydrogenase / Q000378:metabolism*; D045022:Lactate Dehydrogenases / Q000378:metabolism*; D019344:Lactic Acid / Q000737:chemistry* / Q000378:metabolism*; D007778:Lactobacillus / Q000201:enzymology* / Q000378:metabolism*; D009904:Optical Rotation; D019289:Pyruvic Acid / Q000378:metabolism
chemical_list: D019344:Lactic Acid; D019289:Pyruvic Acid; D045022:Lactate Dehydrogenases; D007770:L-Lactate Dehydrogenase; C071195:D-lactate dehydrogenase