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Molecules 2004, 9(4), 185-203; doi:10.3390/90400185

Mechanism-based Enzyme Inactivators of Phytosterol Biosynthesis

Department of Chemistry and Biochemistry, Texas Tech University, Lubbock, Texas 79409-1061, USA
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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. View Full-Text
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 (CC BY 3.0).

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MDPI and ACS Style

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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