Abstract: Current progress on the mechanism and substrate recognition by sterol methyl transferase (SMT), the role of mechanism-based inactivators, other inhibitors of SMT action to probe catalysis and phytosterol synthesis is reported. SMT is a membrane-bound enzyme which catalyzes the coupled C-methylation-deprotonation reaction of sterol acceptor molecules generating the 24-alkyl sterol side chains of fungal ergosterol and plant sitosterol. This C-methylation step can be rate-limiting in the post-lanosterol (fungal) or post-cycloartenol (plant) pathways. A series of sterol analogs designed to impair SMT activity irreversibly have provided deep insight into the C-methylation reaction and topography of the SMT active site and as reviewed provide leads for the development of antifungal agents.
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Zhou, W.; Song, Z.; Kanagasabai, R.; Liu, J.; Jayasimha, P.; Sinha, A.; Veeramachanemi, P.; Miller, M.B.; Nes, W.D. Mechanism-based Enzyme Inactivators of Phytosterol Biosynthesis. Molecules 2004, 9, 185-203.
Zhou W, Song Z, Kanagasabai R, Liu J, Jayasimha P, Sinha A, Veeramachanemi P, Miller MB, Nes WD. Mechanism-based Enzyme Inactivators of Phytosterol Biosynthesis. Molecules. 2004; 9(4):185-203.
Zhou, Wenxu; Song, Zhihong; Kanagasabai, Ragu; Liu, Jialin; Jayasimha, Pruthvi; Sinha, Archana; Veeramachanemi, Phani; Miller, Mathew B.; Nes, W. D. 2004. "Mechanism-based Enzyme Inactivators of Phytosterol Biosynthesis." Molecules 9, no. 4: 185-203.