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.
Original language | English |
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Pages (from-to) | 5902-5906 |
Number of pages | 5 |
Journal | Bioorganic and Medicinal Chemistry Letters |
Volume | 17 |
Issue number | 21 |
DOIs | |
State | Published - Nov 1 2007 |
Keywords
- Cycloartenol
- Mechanism-based inhibitor
- Phytosterol
- Sterol methylation
- Sterol methyltransferase