TY - JOUR T1 - [Regulation of glyoxylate cycle enzymes in Saccharomycopsis lipolytica. I. Effect of the carbon source on isocitrate lyase and malate synthase activity]. A1 - Hönes,I, PY - 1983/1/1/pubmed PY - 1983/1/1/medline PY - 1983/1/1/entrez SP - 163 EP - 71 JF - Zeitschrift fur allgemeine Mikrobiologie JO - Z Allg Mikrobiol VL - 23 IS - 3 N2 - Comparative studies on the activities of isocitrate lyase (ICL) and malate synthase (MS) were carried out with Saccharomycopsis lipolytica incubating the yeast on media with different carbon sources. When cells were incubated in minimal medium with glucose, the activities of both enzymes were very low. In contrast, in minimal medium with acetate enhanced enzyme activities could be demonstrated. It is probably that the synthesis of ICL is repressed in presence of glucose. Furthermore the activity of ICL was inhibited by tricarboxylic acid cycle intermediates like succinic acid and oxalacetic acid. It was concluded that the syntheses of enzymes are derepressed. When cells of Sm. lipolytica were incubated in minimal medium with acetate, a high enzyme activity is evident. Synthesis of ICL on acetate was inhibited by cycloheximide and actinomycin D. The results were discussed comparing them with data obtained from other organisms. SN - 0044-2208 UR - https://www.unboundmedicine.com/medline/citation/6880249/[Regulation_of_glyoxylate_cycle_enzymes_in_Saccharomycopsis_lipolytica__I__Effect_of_the_carbon_source_on_isocitrate_lyase_and_malate_synthase_activity]_ L2 - https://onlinelibrary.wiley.com/resolve/openurl?genre=article&sid=nlm:pubmed&issn=0044-2208&date=1983&volume=23&issue=3&spage=163 DB - PRIME DP - Unbound Medicine ER -