A ThDP-dependent enzymatic carboligation reaction involved in Neocarazostatin A tricyclic carbazole formation
dc.contributor.author | Su, L. | |
dc.contributor.author | Lv, M. | |
dc.contributor.author | Kyeremeh, K. | |
dc.contributor.author | Deng, Z. | |
dc.contributor.author | Deng, H. | |
dc.contributor.author | Yu, Y. | |
dc.date.accessioned | 2019-04-17T10:20:42Z | |
dc.date.available | 2019-04-17T10:20:42Z | |
dc.date.issued | 2016 | |
dc.description.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. © The Royal Society of Chemistry 2016. | en_US |
dc.description.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. © The Royal Society of Chemistry 2016. | en_US |
dc.identifier.issn | 14770520 | |
dc.identifier.other | doi.10.1039/c6ob01651k | |
dc.identifier.other | vol.14.37 | |
dc.identifier.uri | http://ugspace.ug.edu.gh/handle/123456789/29338 | |
dc.language.iso | en | en_US |
dc.title | A ThDP-dependent enzymatic carboligation reaction involved in Neocarazostatin A tricyclic carbazole formation | en_US |
dc.type | Article | en_US |
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