A ThDP-dependent enzymatic carboligation reaction involved in Neocarazostatin A tricyclic carbazole formation. Issue 37 (9th September 2016)

• Record Type: Journal Article
• Authors: Su, Li; Lv, Meinan; Kyeremeh, Kwaku; Deng, Zixin; Deng, Hai; Yu, Yi
• Is Part Of: Organic & biomolecular chemistry. Volume 14:Issue 37(2016)
• Page Start: 8679
• Page End: 8684
• Publication Date: 2016-09-09
• Subjects: Chemistry, Organic -- Periodicals; Bioorganic chemistry -- Periodicals; Chemistry, Physical organic -- Periodicals; 547
• DOI: 10.1039/c6ob01651k
• Languages: English
• ISSNs: 1477-0520

Abstract

Abstract : The ThDP-dependent enzyme NzsH catalyzes an acyloin condensation reaction using indole-3-pyruvate as the acyl acceptor in the biosynthesis of Neocarazostatin A. Abstract : Although the biosynthetic pathway of Neocarazostatin A (1 ) has been identified, the detailed enzymatic reactions underlying the assembly of the carbazole ring still remain largely unknown. We demonstrate here that NzsH, a putative thiamine diphosphate dependent enzyme, can catalyze an acyloin coupling reaction between indole-3-pyruvate and pyruvate to generate a β-ketoacid intermediate. Our findings thus shed light on further characterization of the unusual biosynthetic pathway of the bacterial tricyclic carbazole alkaloids.