title: Conversion of Lactobacillus pentosus D-lactate dehydrogenase to a D-hydroxyisocaproate dehydrogenase through a single amino acid replacement.
abstract: The single amino acid replacement of Tyr52 with Leu drastically increased the activity of Lactobacillus pentosus NAD-dependent D-lactate dehydrogenase toward larger aliphatic or aromatic 2-ketoacid substrates by 3 or 4 orders of magnitude and decreased the activity toward pyruvate by about 30-fold, converting the enzyme into a highly active D-2-hydroxyisocaproate dehydrogenase.
authors.affiliation: Department of Applied Biological Science, Faculty of Science and Technology, Science University of Tokyo, Noda, Chiba 278-8510, Japan.
authors.forename: Chizuka
authors.initials: C
authors.lastname: Tokuda
authors.forename: Yoshiro
authors.initials: Y
authors.lastname: Ishikura
authors.forename: Mayu
authors.initials: M
authors.lastname: Shigematsu
authors.forename: Hiroyuki
authors.initials: H
authors.lastname: Mutoh
authors.forename: Shino
authors.initials: S
authors.lastname: Tsuzuki
authors.forename: Yusaku
authors.initials: Y
authors.lastname: Nakahira
authors.forename: Yusuke
authors.initials: Y
authors.lastname: Tamura
authors.forename: Takeshi
authors.initials: T
authors.lastname: Shinoda
authors.forename: Kazuhito
authors.initials: K
authors.lastname: Arai
authors.forename: O
authors.initials: O
authors.lastname: Takahashi
authors.forename: Hayao
authors.initials: H
authors.lastname: Taguchi
mesh_terms: D000429:Alcohol Oxidoreductases / Q000235:genetics*; D019943:Amino Acid Substitution; D001665:Binding Sites; D002208:Caproates / Q000737:chemistry / Q000378:metabolism*; D005818:Genetic Engineering; D007770:L-Lactate Dehydrogenase / Q000235:genetics*; D007778:Lactobacillus / Q000201:enzymology* / Q000235:genetics; D008958:Models, Molecular; D013379:Substrate Specificity
chemical_list: D002208:Caproates; C034527:isocaproic acid; D000429:Alcohol Oxidoreductases; D007770:L-Lactate Dehydrogenase; C021379:D-2-hydroxyacid dehydrogenase