PMID:4146873

Citation	Raunio, RP, Straus, LD and Jenkins, WT (1973) D-alanine oxidase from Escherichia coli: participation in the oxidation of L-alanine. J. Bacteriol. 115:567-73
Abstract	Cell wall-membrane preparations of Escherichia coli, prepared by the ethylenediaminetetraacetic acid-lysozyme method, contain enzymes which catalyze the oxidation of d-alanine and, to a lesser extent, l-alanine into pyruvate and ammonia without the formation of hydrogen peroxide. The kinetic parameters were (i) pH optima of 8.3 to 8.4 for l- and d-alanine and (ii) a K(m) value of 6.6 +/- 0.2 mM for d-alanine. Several coenzymes were without effect when added to the reaction mixture. The participation of d-alanine oxidase in the oxidation of l-alanine was demonstrated. The evidence is based on (i) results of cellular fractionation; (ii) labeling experiments; (iii) inhibition studies with aminooxyacetate and cycloserine; (iv) denaturation experiments; and (v) demonstration of the presence of an active racemase.
Links	PubMed PMC246284
Keywords	Acetates/pharmacology; Alanine/metabolism; Amino Acid Isomerases/antagonists & inhibitors; Amino Acid Isomerases/metabolism; Ammonia/biosynthesis; Cell Fractionation; Cell Membrane/enzymology; Cell-Free System; Cycloserine/pharmacology; D-Amino-Acid Oxidase/antagonists & inhibitors; D-Amino-Acid Oxidase/metabolism; Deoxycholic Acid/pharmacology; Edetic Acid; Escherichia coli/enzymology; Escherichia coli/metabolism; Hot Temperature; Hydrogen-Ion Concentration; Muramidase; Oxidation-Reduction; Oxygen Consumption; Pyruvates/biosynthesis; Stereoisomerism
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