Structural basis and enzymatic mechanism of the biosynthesis of C 9from C10-monoterpenoid indole alkaloids

Liuqing Yang; Marco Hill; Meitian Wang; Santosh Panjikar; Joachim Stöckigt

doi:10.1002/anie.200900150

Structural basis and enzymatic mechanism of the biosynthesis of C ₉from C₁₀-monoterpenoid indole alkaloids

Liuqing Yang, Marco Hill, Meitian Wang, Santosh Panjikar, Joachim Stöckigt

Research output: Contribution to journal › Article › Research › peer-review

36 Citations (Scopus)

Abstract

Cutting carbons: The three-dimensional structure of polyneuridine aldehyde esterase (PNAE) gives insight into the enzymatic mechanism of the biosynthesis of C₉- from C₁₀-monoterpenoid indole alkaloids (see scheme). PNAE is a very substrate-specific serine esterase. It harbors the catalytic triad S87-D216-H244, and is a new member of the α/ β-fold hydrolase superfamily. Its novel function leads to the diversification of alkaloid structures.

Original language	English
Pages (from-to)	5211-5213
Number of pages	3
Journal	Angewandte Chemie - International Edition
Volume	48
Issue number	28
DOIs	https://doi.org/10.1002/anie.200900150
Publication status	Published - 29 Jun 2009
Externally published	Yes

Keywords

Alkaloids
Biosynthesis
Enzyme catalysis
Esterases
Protein structures

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10.1002/anie.200900150

Cite this

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abstract = "Cutting carbons: The three-dimensional structure of polyneuridine aldehyde esterase (PNAE) gives insight into the enzymatic mechanism of the biosynthesis of C9- from C10-monoterpenoid indole alkaloids (see scheme). PNAE is a very substrate-specific serine esterase. It harbors the catalytic triad S87-D216-H244, and is a new member of the α/ β-fold hydrolase superfamily. Its novel function leads to the diversification of alkaloid structures.",

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AU - Yang, Liuqing

AU - Hill, Marco

AU - Wang, Meitian

AU - Panjikar, Santosh

AU - Stöckigt, Joachim

PY - 2009/6/29

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KW - Alkaloids

KW - Biosynthesis

KW - Enzyme catalysis

KW - Esterases

KW - Protein structures

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