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

Shengying Li; Jennifer M. Finefield; James D. Sunderhaus; Timothy J. McAfoos; Robert M. Williams; David H. Sherman

doi:10.1021/ja2093212

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

Shengying Li, Jennifer M. Finefield, James D. Sunderhaus, Timothy J. McAfoos, Robert M. Williams, David H. Sherman

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90 Scopus citations

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 [ ¹³C]₂-[¹⁵N]₂ quadruply labeled notoamide S (10), demonstrates 10 as a pivotal branching point in notoamide biosynthesis.

Original language	English (US)
Pages (from-to)	788-791
Number of pages	4
Journal	Journal of the American Chemical Society
Volume	134
Issue number	2
DOIs	https://doi.org/10.1021/ja2093212
State	Published - Jan 18 2012
Externally published	Yes

ASJC Scopus subject areas

Catalysis
General Chemistry
Biochemistry
Colloid and Surface Chemistry

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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 [ 13C]2-[15N]2 quadruply labeled notoamide S (10), demonstrates 10 as a pivotal branching point in notoamide biosynthesis.",

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T1 - Biochemical characterization of NotB as an FAD-dependent oxidase in the biosynthesis of notoamide indole alkaloids

AU - Li, Shengying

AU - Finefield, Jennifer M.

AU - Sunderhaus, James D.

AU - McAfoos, Timothy J.

AU - Williams, Robert M.

AU - Sherman, David H.

PY - 2012/1/18

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AB - 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 [ 13C]2-[15N]2 quadruply labeled notoamide S (10), demonstrates 10 as a pivotal branching point in notoamide biosynthesis.

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

Abstract

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