D-alanine oxidase from Escherichia coli: participation in the oxidation of L-alanine.
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.
D000085:Acetates / Q000494:pharmacology; D000409:Alanine / Q000378:metabolism*; D000591:Amino Acid Isomerases / Q000037:antagonists & inhibitors / Q000378:metabolism; D000641:Ammonia / Q000096:biosynthesis; D002458:Cell Fractionation; D002462:Cell Membrane / Q000201:enzymology; D002474:Cell-Free System; D003523:Cycloserine / Q000494:pharmacology; D003605:D-Amino-Acid Oxidase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D003840:Deoxycholic Acid / Q000494:pharmacology; D004492:Edetic Acid; D004926:Escherichia coli / Q000201:enzymology* / Q000378:metabolism; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D009113:Muramidase; D010084:Oxidation-Reduction; D010101:Oxygen Consumption; D011773:Pyruvates / Q000096:biosynthesis; D013237:Stereoisomerism
D000085:Acetates; D011773:Pyruvates; D003840:Deoxycholic Acid; D000641:Ammonia; D003523:Cycloserine; D004492:Edetic Acid; D003605:D-Amino-Acid Oxidase; D009113:Muramidase; D000591:Amino Acid Isomerases; D000409:Alanine