Chemical modification of an essential lysine at the active site of enoyl-CoA reductase in fatty acid synthetase
- 1 April 1980
- journal article
- research article
- Published by Elsevier in Archives of Biochemistry and Biophysics
- Vol. 201 (1), 313-321
- https://doi.org/10.1016/0003-9861(80)90516-0
Abstract
No abstract availableThis publication has 32 references indexed in Scilit:
- Presence of one essential arginine that specifically binds the 2′-phosphate of NADPH on each of the ketoacyl reductase and enoyl reductase active sites of fatty acid synthetaseArchives of Biochemistry and Biophysics, 1980
- Dihydrofolate reductase from Lactobacillus caSci. Stereochemistry of NADPH binding.Published by Elsevier ,1979
- Isolation and characterization of a tryptic fragment containing the thioesterase segment of fatty acid synthetase from the uropygial gland of gooseArchives of Biochemistry and Biophysics, 1978
- Reaction of pyridoxal 5′-phosphate with Escherichia coli CoA transferase: Evidence for an essential lysine residueArchives of Biochemistry and Biophysics, 1977
- One-step purification and properties of a two-peptide fatty acid synthetase from the uropygial gland of the gooseBiochemistry, 1976
- Evidence for an “active serine” in each fatty acid synthetase peptideBiochemical and Biophysical Research Communications, 1976
- Horse liver alcohol dehydrogenase. A study of the essential lysine residueBiochemical Journal, 1975
- The equilibrium position of the reaction of bovine liver glutamate dehydrogenase with pyridoxal 5′-phosphate. A demonstration that covalent modification with this reagent completely abolishes catalytic activityBiochemical Journal, 1975
- Functional arginyl residues as NADH binding sites of alcohol dehydrogenasesBiochemistry, 1974
- Inhibition of Glutamic Dehydrogenase by Pyridoxal 5'-Phosphate*Biochemistry, 1966