GENTZSCH, M and STRAHLBOLSINGER, S and TANNER, W (1995) A NEW DOL-P-MAN-PROTEIN O-D-MANNOSYLTRANSFERASE ACTIVITY FROM SACCHAROMYCES-CEREVISIAE. GLYCOBIOLOGY, 5 (1). pp. 77-82. ISSN 0959-6658, 1460-2423
Full text not available from this repository.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 K-m 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 preference between the two enzymes, however, 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,
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | GLYCOPROTEIN-BIOSYNTHESIS; PROTEIN GLYCOSYLATION; LINKED GLYCOSYLATION; N-GLYCOSYLATION; ALPHA-FACTOR; YEAST; GENE; DOLICHOLMONOPHOSPHATE; LOCALIZATION; PURIFICATION; GLYCOPROTEIN; O-GLYCOSYLATION; MANNOSYLTRANSFERASE; SACCHAROMYCES CEREVISIAE |
| Depositing User: | Dr. Gernot Deinzer |
| Last Modified: | 19 Oct 2022 08:38 |
| URI: | https://pred.uni-regensburg.de/id/eprint/52760 |
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