Next Article in Journal
Synthesis of Some New 4,5-Substituted-4H-1,2,4-triazole-3-thiol Derivatives
Previous Article in Journal
Biaryl Product Formation from Cross-coupling in Palladiumcatalyzed Borylation of a Boc Protected Aminobromoquinoline Compound
Molecules 2004, 9(4), 185-203; doi:10.3390/90400185

Mechanism-based Enzyme Inactivators of Phytosterol Biosynthesis

, , , , , , ,  and *
Department of Chemistry and Biochemistry, Texas Tech University, Lubbock, Texas 79409-1061, USA
* Author to whom correspondence should be addressed.
Received: 27 February 2004 / Accepted: 8 March 2004 / Published: 31 March 2004
Download PDF [573 KB, uploaded 18 June 2014]


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.

Share & Cite This Article

Further Mendeley | CiteULike
Export to BibTeX |
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.

View more citation formats

Related Articles

Article Metrics

For more information on the journal, click here


Cited By

[Return to top]
Molecules EISSN 1420-3049 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert