Inactivation of soybean sterol 24-C-methyltransferase by elongated sterol side chains at C26.
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.
Song
Zhihong
Z
Department of Chemistry and Biochemistry, Texas Tech University, Lubbock, TX 79409-1061, USA.
Nes
W David
WD
D000345:Affinity Labels; D002849:Chromatography, Gas; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D007700:Kinetics; D008780:Methyltransferases / Q000037:antagonists & inhibitors* / Q000737:chemistry; D013025:Glycine max / Q000201:enzymology*; D013379:Substrate Specificity
D000345:Affinity Labels; D008780:Methyltransferases; C022670:delta 24-sterol methyltransferase