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. © 1998, Taylor & Francis Group, LLC. All rights reserved.
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Wada, M., Sakamoto, M., Kataoka, M., Liu, J. Q., Yamada, H., & Shimizu, S. (1998). Distribution of threonine aldolase activity with different stereospecificities in aerobic bacteria. Bioscience, Biotechnology and Biochemistry, 62(8), 1586–1588. https://doi.org/10.1271/bbb.62.1586
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