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- W80964436 abstract "Abstract In extracts of Bacillus subtilis, CO2 fixation occurs primarily through the apparently constitutive enzyme carboxylase, which is strongly activated by acetyl-CoA. This enzyme is necessary for growth on glucose but is not required for sporulation, as was established with a carboxylase mutant. The malic enzyme can use either NAD or, less effectively, NADP as cofactor. The ratio of these activities remains constant through enzyme purification and during enzyme induction by l-malate. Enzyme synthesis is not repressed by glucose. Malic enzyme and carboxylase form a pyruvate shunt to the citric acid cycle, which apparently is necessary during growth on malate for the production of oxalacetate in substrate amounts; malic dehydrogenase functions mainly to provide energy via the citric acid cycle. A specific and sensitive [γ-32P]ATP assay for P-enolpyruvate carboxykinase has been developed. Using this assay, a purified enzyme preparation gave a Km for oxalacetate of about 25 µm. Enzyme synthesis is repressed by glucose. P-enolpyruvate carboxykinase mutants have established that the enzyme is needed for gluconeogenesis and, under normal growth conditions, for sporulation. Sporulation can be restored by the continuous feeding of gluconate." @default.
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- W80964436 date "1973-09-01" @default.
- W80964436 modified "2023-10-17" @default.
- W80964436 title "Role of Pyruvate Carboxylase, Phosphoenolpyruvate Carboxykinase, and Malic Enzyme during Growth and Sporulation of Bacillus subtilis" @default.
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- W80964436 doi "https://doi.org/10.1016/s0021-9258(19)43509-6" @default.
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