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Molecules 2004, 9(4), 185-203; doi:10.3390/90400185
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Mechanism-based Enzyme Inactivators of Phytosterol Biosynthesis

, , , , , , ,  and *
Received: 27 February 2004 / Accepted: 8 March 2004 / Published: 31 March 2004
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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.
Keywords: Ergosterol; sitosterol; stereochemistry; sterol biosynthesis inhibitors Ergosterol; sitosterol; stereochemistry; sterol biosynthesis inhibitors
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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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.

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