These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Directed evolution experiments reveal mutations at cycloartenol synthase residue His477 that dramatically alter catalysis.
    Author: Segura MJ, Lodeiro S, Meyer MM, Patel AJ, Matsuda SP.
    Journal: Org Lett; 2002 Dec 12; 4(25):4459-62. PubMed ID: 12465912.
    Abstract:
    [reaction: see text] Cycloartenol synthase cyclizes and rearranges oxidosqualene to the protosteryl cation and then specifically deprotonates from C-19. To identify mutants that deprotonate differently, randomly generated mutant cycloartenol synthases were selected in a yeast lanosterol synthase mutant. A novel His477Asn mutant was uncovered that produces 88% lanosterol and 12% parkeol. The His477Gln mutant produces 73% parkeol, 22% lanosterol, and 5% Delta(7)-lanosterol. These are the most accurate lanosterol synthase and parkeol synthase that have been generated by mutagenesis.
    [Abstract] [Full Text] [Related] [New Search]