Geranylgeranyltransferase I of Candida albicans: null mutants or enzyme inhibitors produce unexpected phenotypes.

@article{Kelly2000GeranylgeranyltransferaseIO,
  title={Geranylgeranyltransferase I of Candida albicans: null mutants or enzyme inhibitors produce unexpected phenotypes.},
  author={Rosemarie Kelly and Deborah J. Card and Elizabeth A. Register and Paul Mazur and Therese Kelly and Ken ichi Tanaka and Junko Onishi and Joanne M. Williamson and Huizhou Fan and Tamao Satoh and Myra Kurtz},
  journal={Journal of bacteriology},
  year={2000},
  volume={182 3},
  pages={704-13}
}
Geranylgeranyltransferase I (GGTase I) catalyzes the transfer of a prenyl group from geranylgeranyl diphosphate to the carboxy-terminal cysteine of proteins with a motif referred to as a CaaX box (C, cysteine; a, usually aliphatic amino acid; X, usually L). The alpha and beta subunits of GGTase I from Saccharomyces cerevisiae are encoded by RAM2 and CDC43, respectively, and each is essential for viability. We are evaluating GGTase I as a potential target for antimycotic therapy of the related… CONTINUE READING
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