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|Comparative Modeling and Molecular Dynamics Simulation of Substrate Binding in Human Fatty Acid Synthase: Enoyl Reductase and β-Ketoacyl Reductase Catalytic Domains|
|Arun John, Vetrivel Umashankar, Subramanian Krishnakumar, Perinkulam Ravi Deepa|
Genomics Inform. 2015;13(1):15-24. Published online March 31, 2015
Comparative Modeling and Molecular Dynamics Simulation of Substrate Binding in Human Fatty Acid Synthase: Enoyl Reductase and β-Ketoacyl Reductase Catalytic Domains
The presence of essential arginine residues at the NADPH-binding sites of β-ketoacyl reductase and enoyl reductase domains of the multifunctional fatty acid synthetase of chicken liver
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1984;788(1):124-131
Selective chemical modification of the active sites of the ketoacyl reductase and enoyl reductase of fatty acid synthetase from lactating rat mammary glands
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 synthetase
Sequence of a tryptic peptide from the NADPH binding site of the enoyl reductase domain of fatty acid synthase
Crystal structure of the β-ketoacyl reductase (KR) domain of fatty acid synthase (FASN; FAS)–small molecule inhibitor complex
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
Elementary steps in the reaction mechanism of chicken liver fatty acid synthase. pH dependence of NADPH binding and isotope rate effect for beta-ketoacyl reductase.
Rat hepatic microsomal acetoacetyl-CoA reductase. A beta-ketoacyl-CoA reductase distinct from the long chain beta-ketoacyl-CoA reductase component of the microsomal fatty acid chain elongation system.
A C. elegans Model for Mitochondrial Fatty Acid Synthase II: The Longevity-Associated Gene W09H1.5/mecr-1 Encodes a 2-trans-Enoyl-Thioester Reductase