Bauke W. Dijkstra , Niels van Oosterwijk , Ali Rohman
{"title":"Structure and Catalytic Mechanism of 3-Ketosteroid Dehydrogenases","authors":"Bauke W. Dijkstra , Niels van Oosterwijk , Ali Rohman","doi":"10.1016/j.proche.2016.01.006","DOIUrl":null,"url":null,"abstract":"<div><p>3-Ketosteroid dehydrogenases (KSTDs) are FAD-dependent enzymes that introduce a double bond in the A ring of 3-ketosteroid substrates to initiate degradation of the steroid nucleus. Δ<sup>1</sup>-KSTD desaturates the C1-C2 bond of the steroid, while Δ<sup>4</sup>-KSTD targets the C4-C5 bond. Crystal structures with bound products showed that Δ<sup>1</sup>- and Δ<sup>4</sup>-KSTD use different amino acid residues to catalyze an otherwise mechanistically very similar reaction (Δ<sup>1</sup>-KSTD: Tyr318, Tyr119, and Tyr487; Δ<sup>4</sup>-KSTD: Ser468, Tyr319, and Tyr466). However, the substrates are rotated by ∼40° about an axis perpendicular to their plane to bring the target bond (C1-C2 or C4-C5) in the right position.</p></div>","PeriodicalId":20431,"journal":{"name":"Procedia Chemistry","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"2016-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.proche.2016.01.006","citationCount":"9","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Procedia Chemistry","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S1876619616000073","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 9
Abstract
3-Ketosteroid dehydrogenases (KSTDs) are FAD-dependent enzymes that introduce a double bond in the A ring of 3-ketosteroid substrates to initiate degradation of the steroid nucleus. Δ1-KSTD desaturates the C1-C2 bond of the steroid, while Δ4-KSTD targets the C4-C5 bond. Crystal structures with bound products showed that Δ1- and Δ4-KSTD use different amino acid residues to catalyze an otherwise mechanistically very similar reaction (Δ1-KSTD: Tyr318, Tyr119, and Tyr487; Δ4-KSTD: Ser468, Tyr319, and Tyr466). However, the substrates are rotated by ∼40° about an axis perpendicular to their plane to bring the target bond (C1-C2 or C4-C5) in the right position.
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