Oxidation D-malic and beta-alkylmalic acids wild-type and mutant strains of Salmonella typhimurium and by Aerobacter aerogenes.

Journal of Bacteriology
J R Stern, R W O'Brien

Abstract

A mutant strain of Salmonella typhimurium (SL 1634 dml-51) capable of growth on d-malate as sole carbon source was shown to produce d-malic enzyme. This enzyme was absent in the parent wild-type strain which was unable to grow on d-malate. Growth of the mutant on d-malate also resulted in a greatly increased level of beta-isopropylmalic enzyme compared with its level in the wild-type strain grown on citrate or l-malate. The d-malic and beta-isopropylmalic enzymes, both of which catalyze a nicotinamide adenine dinucleotide- and Mg(++)-dependent oxidative decarboxylation of their respective substrates, were shown to be distinct enzymes by selective inhibition with erythro-dl-beta-hydroxyaspartate and by other methods. Cell extracts of the mutant strain also oxidized dl-beta-methyl-, dl-beta-ethyl-, dl-beta-propyl- and dl-betabeta-dimethylmalates, in order of decreasing activity. dl-beta-Methyl-malate was shown to be oxidized by both the d-malic and the beta-isopropylmalic enzymes, whereas the oxidation of the other beta-alkylmalates appeared to be effected exclusively by the beta-isopropylmalic enzyme. beta-Isopropylmalic enzyme activity was induced by d-malate but not by l-malate, showing that it behaved as a d-malictype enzyme....Continue Reading

Citations

Apr 1, 1982·European Journal of Biochemistry·W Knichel, F Radler
Dec 1, 1970·Journal of Bacteriology·D J HopperS Dagley
Dec 1, 1972·Bacteriological Reviews·K E Sanderson
Jun 13, 1980·Biochimica Et Biophysica Acta·M Lähdesmäki, P Mäntsälä
Jun 1, 1970·Bacteriological Reviews·K E Sanderson

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