SGD Paper 
Gentzsch M, et al. (1995) A new Dol-P-Man:protein O-D-mannosyltransferase activity from Saccharomyces cerevisiae. Glycobiology 5(1):77-82
Abstract: The deletion of the protein mannosyltransferase 1 gene (PMT1) of Saccharomyces cerevisiae results in viable cells. O-Mannosylation of proteins is reduced to about half of the value in comparison to wild-type cells. In order to distinguish between the the PMT1 gene product (= Pmt1p) and residual transferase activity, an in vitro assay to measure Dol-P-Man:protein mannosyltransferase activity in cells deleted for PMT1 has been developed. The transferase activity of these cells exhibits a pH optimum of 6.5 as compared to pH 7.5 for Pmt1p. The Km value of the residual enzyme activity for the hexapeptide YNPTSV is 7 times higher than that of Pmt1p and shows a clear preference for the seryl residue. Differences in substrate affinities as well as in seryl/threonyl depend on the specific sequence of the peptides used in the enzyme assay. The new enzyme activity shows a significantly lower thermal stability as compared to Pmt1p.
| Status: Published | Type: Journal Article | PubMed ID: 7772870 |
Topics addressed in this paper
- To find other papers on a gene and topic, click on the colored ball in the appropriate box.
- displays other papers with information about that topic for that gene.
- displays other papers in SGD that are associated with that topic.
The topic is addressed in these papers but does not describe a specific gene or chromosomal feature.
- To go to the Locus page for a gene, click on the gene name.
| Topics | Genes linked to topics |
|---|---|
| PMT1 | |
| Function/Process |  |
| Mutants/Phenotypes | |
| Primary Literature | |
| Regulation of | |
| Strains/Constructs | |
| Substrates/Ligands/Cofactors | |
| Techniques and Reagents | |
