Crystal structure and site-directed mutagenesis of 3-ketosteroid δ1-dehydrogenase from rhodococcus erythropolis SQ1 explain its catalytic mechanism

Ali Rohman, Niels Van Oosterwijk, Andy Mark W.H. Thunnissen, Bauke W. Dijkstra

Research output: Contribution to journalArticlepeer-review

44 Citations (Scopus)

Abstract

Background: 3-Ketosteroid δ1-dehydrogenases catalyze the 1,2-desaturation of 3-ketosteroids. Results: First structures of the enzyme from Rhodococcus erythropolis SQ1, combined with site-directed mutagenesis, clarify its catalytic mechanism. Conclusion: Tyr487 and Gly491 promote keto-enol tautomerization, whereas Tyr318/Tyr119 and FAD abstract a proton and hydride ion, respectively. Significance: This study is an important step toward tailoring the enzyme for steroid biotransformation applications.

Original languageEnglish
Pages (from-to)35559-35568
Number of pages10
JournalJournal of Biological Chemistry
Volume288
Issue number49
DOIs
Publication statusPublished - 6 Dec 2013

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