The coenzyme A requirement of mammalian fatty acid synthetase: Evidence for involvement in the elongation of acyl-enzyme thioesters
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
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1. Characterization of fatty acid synthase monomers restrained from reassociating by immobilization to a solid support;Biochemical Journal;1993-06-01
2. Molecular cloning and sequencing of a cDNA encoding the thioesterase domain of the rat fatty acid synthetase.;Journal of Biological Chemistry;1988-01
3. Mammalian fatty acid synthetase is a structurally and functionally symmetrical dimer;European Journal of Biochemistry;1985-11
4. Inhibition In vitro of lipogenic enzymes from bovine (Bos taurus) mammary tissue by methylmalonyl-coenzyme A and coenzyme A;Comparative Biochemistry and Physiology Part B: Comparative Biochemistry;1984
5. Transient kinetic studies of fatty acid synthetase. A kinetic self-editing mechanism for the loading of acetyl and malonyl residues and the role of coenzyme A.;Journal of Biological Chemistry;1984-01
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