Inactivation of soybean sterol 24-C-methyltransferase by elongated sterol side chains at C26

Zhihong Song; W David Nes

doi:10.1016/j.bmcl.2007.07.096

Inactivation of soybean sterol 24-C-methyltransferase by elongated sterol side chains at C26

Bioorg Med Chem Lett. 2007 Nov 1;17(21):5902-6. doi: 10.1016/j.bmcl.2007.07.096. Epub 2007 Aug 23.

Authors

Zhihong Song¹, W David Nes

Affiliation

¹ Department of Chemistry and Biochemistry, Texas Tech University, Lubbock, TX 79409-1061, USA.

PMID: 17851075
DOI: 10.1016/j.bmcl.2007.07.096

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 k(inact) 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.

Publication types

Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

Affinity Labels
Chromatography, Gas
Chromatography, High Pressure Liquid
Electrophoresis, Polyacrylamide Gel
Glycine max / enzymology*
Kinetics
Methyltransferases / antagonists & inhibitors*
Methyltransferases / chemistry
Substrate Specificity

Substances

Affinity Labels
Methyltransferases
delta 24-sterol methyltransferase