Browsing by Author "Lv, M."
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Item Biosynthesis of Neocarazostatin A Reveals the Sequential Carbazole Prenylation and Hydroxylation in the Tailoring Steps(Chemistry & Biology, 2015-12) Huang, S.; Elsayed, S.S.; Lv, M.; Tabudravu, J.; Rateb, E.M.; Gyampoh, R.; Kyeremeh, K.; Ebel, R.; Jaspars, M.; Deng, Z.; Yu, YI.; Deng, H.Neocarazostatin A (NZS) is a bacterial alkaloid with promising bioactivities against free radicals, featuring a tricyclic carbazole nucleus with a prenyl moiety at C-6 of the carbazole ring. Here, we report the discovery and characterization of the biosynthetic pathway of NZS through genome mining and gene inactivation. The in vitro assays characterized two enzymes: NzsA is a P450 hydroxylase and NzsG is a new phytoene-synthase-like prenyltransferase (PTase). This is the first reported native PTase that specifically acts on the carbazole nucleus. Finally, our in vitro reconstituted experiment demonstrated a coupled reaction catalyzed by NzsG and NzsA tailoring the NZS biosynthesis.Item A ThDP-dependent enzymatic carboligation reaction involved in Neocarazostatin A tricyclic carbazole formation(2016) Su, L.; Lv, M.; Kyeremeh, K.; Deng, Z.; Deng, H.; Yu, Y.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.