Structural Basis and Enzymatic Mechanism of the Biosynthesis of C9- from C10-Monoterpenoid Indole Alkaloids

6533b860fe1ef96bd12c2fd7

RESEARCH PRODUCT

Structural Basis and Enzymatic Mechanism of the Biosynthesis of C9- from C10-Monoterpenoid Indole Alkaloids

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

subject

Stereochemistry chemistry [Secologanin Tryptamine Alkaloids]polyneuridine aldehyde esterase Polyneuridine-aldehyde esterase Catalysis Substrate Specificity Enzyme catalysis chemistry.chemical_compound Protein structure Biosynthesis Hydrolase Catalytic triad metabolism [Mutant Proteins]Indole test chemistry.chemical_classification General Chemistry Secologanin Tryptamine Alkaloids Protein Structure Tertiary metabolism [Carboxylic Ester Hydrolases]metabolism [Secologanin Tryptamine Alkaloids]Enzyme Amino Acid Substitution chemistry Biochemistry ddc:540 Biocatalysis Mutant Proteins Carboxylic Ester Hydrolases

description

Cutting carbons: The three-dimensional structure of polyneuridine aldehyde esterase (PNAE) gives insight into the enzymatic mechanism of the biosynthesis of C(9)- from C(10)-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 alpha/beta-fold hydrolase superfamily. Its novel function leads to the diversification of alkaloid structures.

year	journal	country	edition	language
2009-06-05	Angewandte Chemie International Edition

https://doi.org/10.1002/anie.200900150

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