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Heterogeneity of the Glyoxylate-Condensing Enzymes

1965; American Society for Microbiology; Volume: 90; Issue: 3 Linguagem: Inglês

10.1128/jb.90.3.594-598.1965

1098-5530

Warner S. Wegener, Henry C. Reeves, Samuel J. Ajl,

Food Quality and Safety Studies

Wegener, Warner S. (Albert Einstein Medical Center, Philadelphia, Pa.), Henry C. Reeves, and Samuel J. Ajl . Heterogeneity of the glyoxylate-condensing enzymes. J. Bacteriol. 90: 594–598. 1965.—Evidence is presented that the enzymatic condensations of glyoxylate with acetyl-CoA (malate synthase), propionyl-CoA (α-hydroxyglutarate synthase), butyryl-CoA (β-ethylmalate synthase), and valeryl-CoA (β- n -propylmalate synthase) are catalyzed by different enzymes. The possibility that these activities resulted from a single enzyme possessing a broad fatty acid acyl-CoA substrate specificity was ruled out. The latter was suggested by the fact that cells grown on a number of short-chain fatty acids exhibited all the above activities. The conclusion that these reactions are catalyzed by different enzymes is based on the following considerations: (i) the enzymes can be differentially inactivated by heat; (ii) under various growth conditions, where all the condensing enzymes are present, their respective activities do not show a constant ratio, as would be expected if they were catalyzed by a single enzyme; and (iii) under appropriate growth conditions, one or more of these enzymes has been shown to be present to the exclusion of others.