title: Distribution of Threonine Aldolase Activity with Different Stereospecificities in Aerobic Bacteria.
abstract: Threonine aldolase activities (threonine acetaldehyde-lyase activity) with different stereospecificities toward 4 isomers of threonine were found in a variety of aerobic bacteria. The strains could be divided into three groups on the basis of the substrate specificity of a cell-free extract. The enzyme activities toward D-allo- and D-threonine were inhibited by EDTA, which suggested that a metal ion participates in the D-specific aldolase reaction.
authors.affiliation: a Division of Applied Life Science, Graduate School of Agriculture, Kyoto University.
authors.forename: M
authors.initials: M
authors.lastname: Wada
authors.affiliation: a Division of Applied Life Science, Graduate School of Agriculture, Kyoto University.
authors.forename: M
authors.initials: M
authors.lastname: Sakamoto
authors.affiliation: a Division of Applied Life Science, Graduate School of Agriculture, Kyoto University.
authors.forename: M
authors.initials: M
authors.lastname: Kataoka
authors.affiliation: b Laboratory of Biocatalytic Chemistry, Biotechnology Research Center, Toyama Prefectural University.
authors.forename: J Q
authors.initials: JQ
authors.lastname: Liu
authors.affiliation: b Laboratory of Biocatalytic Chemistry, Biotechnology Research Center, Toyama Prefectural University.
authors.forename: H
authors.initials: H
authors.lastname: Yamada
authors.affiliation: a Division of Applied Life Science, Graduate School of Agriculture, Kyoto University.
authors.forename: S
authors.initials: S
authors.lastname: Shimizu
keywords: D-allo-threonin; L-allo-threonine; threonine aldolase