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• W2037972355 abstract "Citrate synthase (citrate oxaloacetate-lyase, CoA-acetylating, EC 4.1.3.7) from cells of Azotobacter vinelandii and Acinetobacter anitratum was purified to apparent homogeneity. The molecular weight of native citrate synthase from A. anitratum was determined to be 242 000, and the enzyme from A. vinelandii had a molecular weight of 250 000. The subunit molecular weights of A. vinelandii and A. anitratum citrate synthases appeared identical. Each had a monomeric molecular weight, determined by sedimentation equilibrium studies, of 58 500–59 000. Purification of citrate synthase from Bacillus subtilis was hampered by low specific activity levels and poor enzyme stability and was not purified to homogeneity. The molecular weight of the active enzyme was determined to be 60 000–95 000 by acrylamide gel electrophoresis. The patterns observed from initial velocity and product inhibition studies of citrate synthase catalysis are consistent with those predicted for a random sequential reaction order mechanism. Extensively purified citrate synthase from each of the three genera studied gave similar kinetic patterns, despite variations in enzyme size and regulatory complexity." @default.
• W2037972355 created "2016-06-24" @default.
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• W2037972355 date "1974-06-01" @default.
• W2037972355 modified "2023-09-27" @default.
• W2037972355 title "Bacterial citrate synthases: Purification, molecular weight and kinetic mechanism" @default.
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• W2037972355 doi "https://doi.org/10.1016/0005-2744(74)90508-7" @default.
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