| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1365532 | Bioorganic & Medicinal Chemistry Letters | 2007 | 5 Pages |
Abstract
The enzymatic C-methylation reaction catalyzed by the Glycine max sterol 24-C-methyltransferase was studied with substrate analogs containing a cycloartenol nucleus (CA) and a double bond (8) or triple bond (14) attached to C26. The production of the corresponding C24(28)-methylene olefin and time-dependent inhibition kinetics of kinact 0.24 min−1 (CA-8) or 0.06 min−1 (CA-14) indicates an active-site directed process and partitioning to produce novel products.
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Related Topics
Physical Sciences and Engineering
Chemistry
Organic Chemistry
Authors
Zhihong Song, W. David Nes,