Comparative molecular field analysis (CoMFA) for sulfoxidation reactions in Mortierella isabellina ATCC 42613 and Helminthosporium sp. NRRL 4671

Previous models for mechanisms of enzymatic sulfoxidation have been somewhat limited by a lack of knowledge of the essential features of substrate-enzyme versus product-enzyme relationships. Computerized methods for modeling ligand-protein (substrate-enzyme) interactions can overcome some of these l...

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Bibliographic Details
Published in:Journal of molecular modeling 2002-01, Vol.8 (1), p.8-23
Main Authors: Huang, Wen-Hsin, Wilcox, Richard E, Davis, Patrick J
Format: Article
Language:English
Subjects:
Computer Simulation
Helminthosporium - metabolism
Models, Chemical
Models, Molecular
Mortierella - metabolism
Oxidation-Reduction
Reproducibility of Results
Stereoisomerism
Sulfides - chemistry
Sulfides - metabolism
Sulfones - chemistry
Sulfones - metabolism
Sulfoxides - chemistry
Sulfoxides - metabolism
Sulfur Compounds - chemistry
Sulfur Compounds - metabolism
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Summary:Previous models for mechanisms of enzymatic sulfoxidation have been somewhat limited by a lack of knowledge of the essential features of substrate-enzyme versus product-enzyme relationships. Computerized methods for modeling ligand-protein (substrate-enzyme) interactions can overcome some of these limitations. Specifically, CoMFA (comparative molecular field analysis) provided a useful general approach in which to evaluate substrate-enzyme and product-enzyme relationships. The present investigation examined the relationship between substrate and product structure in predicting enantioselective sulfoxidation reactions using CoMFA for two species of microorganisms that have been used as models for mammalian metabolism, Mortierella isabellina and Helminthosporium sp. The overall enantioselectivity observed was based on the composite stereoselectivity of sulfoxide formation, sulfone formation (from the sulfoxide), and sulfoxide reduction back to the achiral substrate (sulfide).
ISSN:1610-2940
0948-5023
DOI:10.1007/s00894-001-0060-y