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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 |
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Genomics Inform. 2015;13(1):15-24. Published online March 31, 2015 DOI: https://doi.org/10.5808/GI.2015.13.1.15 |
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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 Genomics & Informatics. 2015;13(1):15  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 International Journal of Biochemistry. 1980;12(4):591-596 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 Archives of Biochemistry and Biophysics. 1980;199(2):457-464 Sequence of a tryptic peptide from the NADPH binding site of the enoyl reductase domain of fatty acid synthase Archives of Biochemistry and Biophysics. 1983;220(2):652-656 Crystal structure of the β-ketoacyl reductase (KR) domain of fatty acid synthase (FASN; FAS)–small molecule inhibitor complex Science-Business eXchange. 2014;7(34):1026-1026 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;63(1):50-56 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. Journal of Biological Chemistry. 1984;259(11):6748-6751 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. Journal of Biological Chemistry. 1984;259(12):7460-7467 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 PLoS ONE. 2009;4(11):e7791 |
