Evidence for an “active serine” in each fatty acid synthetase peptide
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference15 articles.
1. The Purification and Properties of the Fatty Acid Synthetase of Pigeon Liver
2. Fatty Acid Synthetase from Lactating Rat Mammary Gland
3. Fatty Acid Synthetase of Chicken Liver
4. Factors affecting the reassociation and reactivation of the half-molecular weight nonidentical subunits of pigeon liver fatty acid synthetase.
Cited by 32 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献
1. The Multifunctional Polypeptide Chains of Rabbit-Mammary Fatty-Acid Synthase;European Journal of Biochemistry;2005-03-03
2. Amino acid sequence around the reactive serine residue of the thioesterase domain of rabbit fatty acid synthase;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1985-04
3. Measurement of distance between the active serine of the thioesterase domain and the pantetheine thiol of fatty acid synthase by fluorescence resonance energy transfer.;Journal of Biological Chemistry;1985-03
4. Isolation, purification, and characterization of a peptide that contains the β-ketoacyl reductase, enoyl reductase, and β-hydroxyacyl dehydrase activities of the pigeon liver fatty acid synthetase;Canadian Journal of Biochemistry and Cell Biology;1985-01-01
5. Specific modification of the condensation domain of fatty acid synthase and the determination of the primary structure of the modified active site peptides;Archives of Biochemistry and Biophysics;1984-04
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