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Biochemical characterization of NotB as an FAD-dependent oxidase in the biosynthesis of notoamide indole alkaloids.

ABSTRACT: Notoamides produced by Aspergillus spp. bearing the bicyclo[2.2.2]diazaoctane core structure with unusual structural diversity represent a compelling system to understand the biosynthesis of fungal prenylated indole alkaloids. Herein, we report the in vitro characterization of NotB, which catalyzes the indole 2,3-oxidation of notoamide E (13), leading to notoamides C (11) and D (12) through an apparent pinacol-like rearrangement. This unique enzymatic reaction with high substrate specificity, together with the information derived from precursor incorporation experiments using [(13)C](2)-[(15)N](2) quadruply labeled notoamide S (10), demonstrates 10 as a pivotal branching point in notoamide biosynthesis.

SUBMITTER: Li S

PROVIDER: S-EPMC3275806 | biostudies-literature | 2012 Jan

REPOSITORIES: biostudies-literature

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Biochemical characterization of NotB as an FAD-dependent oxidase in the biosynthesis of notoamide indole alkaloids.

Li Shengying S Finefield Jennifer M JM Sunderhaus James D JD McAfoos Timothy J TJ Williams Robert M RM Sherman David H DH

Journal of the American Chemical Society 20111228 2

Notoamides produced by Aspergillus spp. bearing the bicyclo[2.2.2]diazaoctane core structure with unusual structural diversity represent a compelling system to understand the biosynthesis of fungal prenylated indole alkaloids. Herein, we report the in vitro characterization of NotB, which catalyzes the indole 2,3-oxidation of notoamide E (13), leading to notoamides C (11) and D (12) through an apparent pinacol-like rearrangement. This unique enzymatic reaction with high substrate specificity, to ...[more]

PMID: 22188465

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