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J Bacteriol. 1973 August; 115(2): 560-566
Copyright © 1973 American Society for Microbiology. All Rights Reserved.

D-Alanine Oxidase from Escherichia coli: Localization and Induction by L-Alanine

^a Department of Chemistry, Indiana University, Bloomington, Indiana 47401

ABSTRACT

Dialyzed membranes of Escherichia coli prepared by an ethylenediaminetetraacetic acid-lysozyme method catalyze the oxidation of both L-alanine and D-alanine. The specific activities for the oxidations of both D-alanine and L-alanine are increased fivefold when the cells are grown in the presence of either L-alanine or DL-alanine, but are increased only slightly when grown in the presence of D-alanine. In the DL-alanine-induced system, the specific activities for the oxidations of some other D-amino acids are also raised. DL-alanine also induces two other alanine catabolizing enzymes, alanine dehydrogenase and alanine-glutamate aminotransferase which are found in the "soluble" fraction of lysozyme-treated cells. The oxidations of both L-alanine and D-alanine were associated with the membranes of induced cells. After the membranes were disintegrated by sonic treatment, both L-alanine and D-alanine oxidation catalysts sedimented in a sucrose density gradient together with D-lactate and L-lactate dehydrogenases, apparently as a single multienzyme complex.

¹ Present address: Department of Biochemistry, University of Turku, 20500 Turku 50, Finland.