Enzymatic Carboxylation of Biotin: Molecular and Catalytic Properties of a Component Enzyme of Acetyl CoA Carboxylase
- 1 November 1970
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 67 (3) , 1353-1360
- https://doi.org/10.1073/pnas.67.3.1353
Abstract
The biotin carboxylase component of acetyl CoA carboxylase has been purified approximately 2000 times from Escherichia coli . This protein, which catalyzes the carboxylation of free d -biotin, is free of the biotin-containing carboxyl carrier protein, is homogeneous by polyacrylamide gel electrophoresis and analytical ultracentrifugation, and has been crystallized. Biotin carboxylase, with a molecular weight of approximately 100,000, is composed of two 50,000-dalton subunits. The catalytic capacity of biotin carboxylase is markedly enhanced by ethanol (11 times at 15% v/v), and certain other organic solvents; this may mimic an effector-mediated response. The kinetic effect is exclusively on the maximal velocity of the reaction. Activation by ethanol is reversible and not accompanied by aggregation or disaggregation of the enzyme.Keywords
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