Enzymatic Formation of Multiple Triterpenes by Mutation of Tyrosine 510 of the Oxidosqualene-Lanosterol Cyclase from Saccharomyces cerevisiae
Author:
Publisher
Wiley
Subject
Organic Chemistry,Molecular Biology,Molecular Medicine,Biochemistry
Reference23 articles.
1. Enzymatic cyclization of squalene and oxidosqualene to sterols and triterpenes
2. Mechanismen der enzymatischen Bildung polycyclischer Triterpene
3. Enzyme Mechanisms for Polycyclic Triterpene Formation
4. Directed Evolution To Investigate Steric Control of Enzymatic Oxidosqualene Cyclization. An Isoleucine-to-Valine Mutation in Cycloartenol Synthase Allows Lanosterol and Parkeol Biosynthesis
5. beta-Amyrin synthase. Cloning of oxidosqualene cyclase that catalyzes the formation of the most popular triterpene among higher plants
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1. Engineering Critical Amino Acid Residues of Lanosterol Synthase to Improve the Production of Triterpenoids in Saccharomyces cerevisiae;ACS SYNTH BIOL;2022
2. Engineering Critical Amino Acid Residues of Lanosterol Synthase to Improve the Production of Triterpenoids in Saccharomyces cerevisiae;ACS Synthetic Biology;2022-08-03
3. Biosynthetic Mechanism of Lanosterol: A Completed Story;ACS Catalysis;2020-01-13
4. Oryza sativa Parkeol Cyclase: Changes in the Substrate‐Folding Conformation and the Deprotonation Sites on Mutation at Tyr257: Importance of the Hydroxy Group and Steric Bulk;ChemBioChem;2019-10-15
5. Deciphering the evolutionary history of microbial cyclic triterpenoids;Free Radical Biology and Medicine;2019-08
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