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PMID: 5660627 Published · ppublish English Journal Article

The kinetics of enzyme changes in yeast under conditions that cause the loss of mitochondria.

The Biochemical journal ·Vol. 107 ·No. 4 ·1968-04-00 ·Pages 455-65

Chapman C, Bartley W

Abstract

1. Aerobically grown yeast having a high activity of glyoxylate-cycle, citric acid-cycle and electron-transport enzymes was transferred to a medium containing 10% glucose. After a lag phase of 30min. the yeast grew exponentially with a mean generation time of 94min. 2. The enzymes malate dehydrogenase, isocitrate lyase, succinate-cytochrome c oxidoreductase and NADH-cytochrome c oxidoreductase lost 45%, 17%, 27% and 46% of their activity respectively during the lag phase. 3. When growth commenced pyruvate kinase, pyruvate decarboxylase, alcohol dehydrogenase, glutamate dehydrogenase (NADP(+)-linked) and NADPH-cytochrome c oxidoreductase increased in activity, whereas aconitase, isocitrate dehydrogenase (NAD(+)- and NADP(+)-linked), alpha-oxoglutarate dehydrogenase, fumarase, malate dehydrogenase, succinate-cytochrome c oxidoreductase, NADH-cytochrome c oxidoreductase, NADH oxidase, NADPH oxidase, cytochrome c oxidase, glutamate dehydrogenase (NAD(+)-linked), glutamate-oxaloacetate transaminase, isocitrate lyase and glucose 6-phosphate dehydrogenase decreased. 4. During the early stages of growth the loss of activity of aconitase, alpha-oxoglutarate dehydrogenase, fumarase and glucose 6-phosphate dehydrogenase could be accounted for by dilution by cell division. The lower rate of loss of activity of isocitrate dehydrogenase (NAD(+)- and NADP(+)-linked), glutamate dehydrogenase (NAD(+)-linked), glutamate-oxaloacetate transaminase, NADPH oxidase and cytochrome c oxidase implies their continued synthesis, whereas the higher rate of loss of activity of malate dehydrogenase, isocitrate lyase, succinate-cytochrome c oxidoreductase, NADH-cytochrome c oxidoreductase and NADH oxidase means that these enzymes were actively removed. 5. The mechanisms of selective removal of enzyme activity and the control of the residual metabolic pathways are discussed.

MeSH Terms
Alcohol Oxidoreductases/analysis Amino Acid Oxidoreductases/analysis Carboxy-Lyases/analysis Glucosephosphate Dehydrogenase/analysis Hydro-Lyases/analysis Isocitrate Dehydrogenase/analysis Kinetics Lyases/analysis Malate Dehydrogenase/analysis Mitochondria Oxidoreductases/analysis Pyruvate Kinase/analysis Succinate Dehydrogenase/analysis Time Factors Transaminases/analysis Yeasts/enzymology
Chemicals
Oxidoreductases Alcohol Oxidoreductases Malate Dehydrogenase Isocitrate Dehydrogenase Glucosephosphate Dehydrogenase Succinate Dehydrogenase Amino Acid Oxidoreductases Transaminases Pyruvate Kinase Lyases Carboxy-Lyases Hydro-Lyases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Chapman C
Bartley W
References (20)
20 references, click to expand
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
Published
1968-04-00
Pages
455-65
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1198688
Subset
IM
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