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The effect of growth substrate on the levels of citric acid cycle enzymes in the facultative methylotroph Arthrobacter 2B2
Author(s) -
Paddon C. J.,
Payton M. A.,
Hartley B. S.
Publication year - 1985
Publication title -
journal of basic microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.58
H-Index - 54
eISSN - 1521-4028
pISSN - 0233-111X
DOI - 10.1002/jobm.3620250118
Subject(s) - methylotroph , oxoglutarate dehydrogenase complex , citric acid cycle , biochemistry , pyruvate dehydrogenase complex , arthrobacter , enzyme , dehydrogenase , facultative , pyruvate dehydrogenase kinase , pyruvate dehydrogenase phosphatase , citrate synthase , branched chain alpha keto acid dehydrogenase complex , citric acid , biology , pyruvate decarboxylation , chemistry , botany
All enzymes of the citric acid cycle were found to be present in cell‐free extracts of the facultative methylotroph Arthrobacter 2B2 except 2‐oxoglutarate dehydrogenase and pyruvate dehydrogenase. The dehydrogenase (E 1 ) and lipoamide dehydrogenase (E 2 ) component of 2‐oxoglutarate could be detected indicating that the complex was present, but may be very labile. No great differences in enzyme levels were detected between cells grown on trimethylamine and those on multicarbon substrates. Citrate synthase was found to be insensitive to inhibition by NADH or 2‐oxoglutarate, but some inhibition was observed with ATP.