The purification and characterization of recombinant yeast dolichyl-phosphate-mannose synthase. Site-directed mutagenesis of the putative dolichol recognition sequence.

@article{Schutzbach1993ThePA,
  title={The purification and characterization of recombinant yeast dolichyl-phosphate-mannose synthase. Site-directed mutagenesis of the putative dolichol recognition sequence.},
  author={John S. Schutzbach and John W. Zimmerman and W Thomas Forsee},
  journal={The Journal of biological chemistry},
  year={1993},
  volume={268 32},
  pages={24190-6}
}
Yeast dolichyl-phosphate-mannose synthase was purified from cultures of Escherichia coli carrying the gene for this enzyme in a high expression vector. The synthase contains a highly conserved hydrophobic amino acid sequence proposed to be involved in the recognition of dolichols (Albright, C. F., Orlean, P., and Robbins, P. W. (1989) Proc. Natl. Acad. Sci. U. S. A. 86, 7366-7369) and amino acid residues in this sequence were altered by site-directed mutagenesis. Conservative substitutions had… CONTINUE READING