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From Proteopedia
Crystal structure of E. Coli FabI in complex with NAD and (R,E)-3-(7-amino-8-oxo-6,7,8,9-tetrahydro-5H-pyrido[2,3-b]azepin-3-yl)-N-methyl-N-((3-methylbenzofuran-2-yl)methyl)acrylamide
Structural highlights
FunctionFABI_ECOLI Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism and in the biotin biosynthesis.[1] [2] [3] Publication Abstract from PubMed[This corrects the article DOI: 10.1021/acscentsci.2c00598.]. Correction to "An Iterative Approach Guides Discovery of the FabI Inhibitor Fabimycin, a Late-Stage Antibiotic Candidate with In Vivo Efficacy against Drug-Resistant Gram-Negative Infections".,Parker EN, Cain BN, Hajian B, Ulrich RJ, Geddes EJ, Barkho S, Lee HY, Williams JD, Raynor M, Caridha D, Zaino A, Rohde JM, Zak M, Shekhar M, Munoz KA, Rzasa KM, Temple ER, Hunt D, Jin X, Vuong C, Pannone K, Kelly AM, Mulligan MP, Lee KK, Lau GW, Hung DT, Hergenrother PJ ACS Cent Sci. 2022 Sep 28;8(9):1362. doi: 10.1021/acscentsci.2c00969. Epub 2022 , Sep 6. PMID:36188352[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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