A ThDP-dependent enzymatic carboligation reaction involved in Neocarazostatin A tricyclic carbazole formation

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dc.contributor.authorSu, L.
dc.contributor.authorLv, M.
dc.contributor.authorKyeremeh, K.
dc.contributor.authorDeng, Z.
dc.contributor.authorDeng, H.
dc.contributor.authorYu, Y.
dc.date.accessioned2019-04-17T10:20:42Z
dc.date.available2019-04-17T10:20:42Z
dc.date.issued2016
dc.description.abstractAlthough 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. © The Royal Society of Chemistry 2016.en_US
dc.description.abstractAlthough 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. © The Royal Society of Chemistry 2016.en_US
dc.identifier.issn14770520
dc.identifier.otherdoi.10.1039/c6ob01651k
dc.identifier.othervol.14.37
dc.identifier.urihttp://ugspace.ug.edu.gh/handle/123456789/29338
dc.language.isoenen_US
dc.titleA ThDP-dependent enzymatic carboligation reaction involved in Neocarazostatin A tricyclic carbazole formationen_US
dc.typeArticleen_US

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