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Regulation of isocitrate lyase in a mutant ofRhodopseudomonas capsulataadapted to growth on acetate

✍ Scribed by Allen M. Nielsen; Brian J. Rampsch; Gary A. Sojka

Publisher: Springer
Year: 1979
Tongue: English
Weight: 613 KB
Volume: 120
Category: Article
ISSN: 0302-8933
DOI: 10.1007/bf00413271

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✦ Synopsis

Studies on acetate utilization by Rhodopseudomonas capsutata strain St. Louis indicated that the wild type grew poorly on acetate and made little if any of the glyoxylate cycle enzyme isocitrate lyase. A spontaneous mutant, Ac-l, capable of vigorous and immediate growth on acetate and exhibiting high levels of isocitrate lyase activity, was isolated in the course of those studies.

Isocitrate lyase was not formed when the mutant was grown on matate. Addition of malate to cultures of Ac-1 growing on acetate resulted in loss of the enzyme by dilution through growth.

Starvation of acetate-grown Ac-1 for acetate resulted in a rapid and complete loss of isocitrate lyase activity which was shown to be energy dependent. Readdition of acetate to a starved culture previously grown on acetate resulted in a rapid recovery of enzyme activity. The recovery required energy and was sensitive to chloramphenicol inhibition at any time during the recovery phase.

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