Topological Study of Mechanistic Diversity in Conjugated Fatty Acid Biosynthesis

Variations on an oxidative theme: The precision with which FAD2‐type desaturases carry out CH activation reactions on flexible lipidic substrates is astonishing. The conformational space available within the active site of these enzymes has been explored using deuterium‐labeled substrates, and evid...

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Bibliographic Details
Published in:Angewandte Chemie International Edition 2012-07, Vol.51 (27), p.6686-6690
Main Authors: Bhar, Palash, Reed, Darwin W., Covello, Patrick S., Buist, Peter H.
Format: Article
Language:English
Subjects:
Aleurites - enzymology
Aleurites - metabolism
conformation analysis
CH activation
desaturases
enzyme mechanisms
Fatty Acid Desaturases - metabolism
Fatty Acids - biosynthesis
Fatty Acids - chemistry
Glycine max - enzymology
Glycine max - metabolism
kinetic isotope effects
Models, Chemical
Plant Proteins - metabolism
Stereoisomerism
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Summary:Variations on an oxidative theme: The precision with which FAD2‐type desaturases carry out CH activation reactions on flexible lipidic substrates is astonishing. The conformational space available within the active site of these enzymes has been explored using deuterium‐labeled substrates, and evidence for a novel quasi‐eclipsed conformer has been uncovered. The scheme shows some prototypical substrate conformations.
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.201202080