Fatty acid synthetase. A steady state kinetic analysis of the reaction catalyzed by the enzyme from pigeon liver.
Open Access
- 1 April 1975
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 250 (7) , 2709-2717
- https://doi.org/10.1016/s0021-9258(19)41660-8
Abstract
No abstract availableKeywords
This publication has 32 references indexed in Scilit:
- Substrate inhibition of pigeon liver fatty acid synthetase and optimum assay conditions for over-all synthetase activityArchives of Biochemistry and Biophysics, 1974
- Synthesis of fatty acids from malonyl-CoA and NADPH by pigeon liver fatty acid synthetaseArchives of Biochemistry and Biophysics, 1974
- The mechanism of synthesis of fatty acids by the pigeon liver enzyme systemArchives of Biochemistry and Biophysics, 1970
- Intermediates of fatty acid synthesis: Sites of binding to the pigeon liver fatty acid synthetaseArchives of Biochemistry and Biophysics, 1970
- Identification of the sites of binding of acetyl and malonyl groups to the pigeon liver fatty acid synthetase complexArchives of Biochemistry and Biophysics, 1970
- Studies on the substrate binding sites of the pigeon liver fatty acid synthetaseArchives of Biochemistry and Biophysics, 1968
- The kinetics of enzyme-catalyzed reactions with two or more substrates or productsBiochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects, 1963
- Statistical estimations in enzyme kineticsBiochemical Journal, 1961
- Tissue sulfhydryl groupsArchives of Biochemistry and Biophysics, 1959
- A Schematic Method of Deriving the Rate Laws for Enzyme-Catalyzed ReactionsThe Journal of Physical Chemistry, 1956