PublisherDOIYearVolumeIssuePageTitleAuthor(s)Link
Genomics & Informatics10.5808/gi.2015.13.1.15201513115Comparative Modeling and Molecular Dynamics Simulation of Substrate Binding in Human Fatty Acid Synthase: Enoyl Reductase and β-Ketoacyl Reductase Catalytic DomainsArun John, Vetrivel Umashankar, Subramanian Krishnakumar, Perinkulam Ravi Deepahttp://synapse.koreamed.org/DOIx.php?id=10.5808/GI.2015.13.1.15
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology10.1016/0167-4838(84)90304-219847881124-131The 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 liverCatherine M. Vernon, Robert Y. Hsuhttps://api.elsevier.com/content/article/PII:0167483884903042?httpAccept=text/xml, https://api.elsevier.com/content/article/PII:0167483884903042?httpAccept=text/plain
International Journal of Biochemistry10.1016/0020-711x(80)90011-71980124591-596Selective chemical modification of the active sites of the ketoacyl reductase and enoyl reductase of fatty acid synthetase from lactating rat mammary glandsA.J. Poulose, Linda Rogers, P.E. Kolattukudyhttps://api.elsevier.com/content/article/PII:0020711X80900117?httpAccept=text/xml, https://api.elsevier.com/content/article/PII:0020711X80900117?httpAccept=text/plain
Archives of Biochemistry and Biophysics10.1016/0003-9861(80)90302-119801992457-464Presence 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 synthetaseA.J. Poulose, P.E. Kolattukudyhttps://api.elsevier.com/content/article/PII:0003986180903021?httpAccept=text/xml, https://api.elsevier.com/content/article/PII:0003986180903021?httpAccept=text/plain
Archives of Biochemistry and Biophysics10.1016/0003-9861(83)90459-919832202652-656Sequence of a tryptic peptide from the NADPH binding site of the enoyl reductase domain of fatty acid synthaseA.J. Poulose, P.E. Kolattukudyhttps://api.elsevier.com/content/article/PII:0003986183904599?httpAccept=text/xml, https://api.elsevier.com/content/article/PII:0003986183904599?httpAccept=text/plain
Science-Business eXchange10.1038/scibx.2014.102620147341026-1026Crystal structure of the β-ketoacyl reductase (KR) domain of fatty acid synthase (FASN; FAS)–small molecule inhibitor complexhttp://link.springer.com/content/pdf/10.1038/scibx.2014.1026.pdf, http://link.springer.com/article/10.1038/scibx.2014.1026/fulltext.html, http://link.springer.com/content/pdf/10.1038/scibx.2014.1026.pdf
Canadian Journal of Biochemistry and Cell Biology10.1139/o85-007198563150-56Isolation, 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 synthetaseRajinder N. Puri, John W. Porterhttp://www.nrcresearchpress.com/doi/pdf/10.1139/o85-007
Journal of Biological Chemistry10.1016/s0021-9258(17)39791-01984259116748-6751Elementary steps in the reaction mechanism of chicken liver fatty acid synthase. pH dependence of NADPH binding and isotope rate effect for beta-ketoacyl reductase.Z Yuan, G G Hammeshttps://api.elsevier.com/content/article/PII:S0021925817397910?httpAccept=text/xml, https://api.elsevier.com/content/article/PII:S0021925817397910?httpAccept=text/plain
Journal of Biological Chemistry10.1016/s0021-9258(17)42813-41984259127460-7467Rat 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.M R Prasad, L Cook, R Vieth, D L Cintihttps://api.elsevier.com/content/article/PII:S0021925817428134?httpAccept=text/xml, https://api.elsevier.com/content/article/PII:S0021925817428134?httpAccept=text/plain
PLoS ONE10.1371/journal.pone.00077912009411e7791A C. elegans Model for Mitochondrial Fatty Acid Synthase II: The Longevity-Associated Gene W09H1.5/mecr-1 Encodes a 2-trans-Enoyl-Thioester ReductaseAner Gurvitzhttp://dx.plos.org/10.1371/journal.pone.0007791