PMID: 6989607Apr 1, 1980Paper

Yeast mannosyl transferases requiring dolichyl phosphate and dolichyl phosphate mannose as substrate. Partial purification and characterization of the solubilized enzyme

European Journal of Biochemistry
P BabczinskiW Tanner

Abstract

The first mannosyl unit of manno-oligosaccharides of fungal mannoproteins is transferred in a dolichyl-phosphate-dependent reaction sequence to serine/threonine residues of the protein. The two membrane-bound enzymes catalyzing this transfer in the yeast Saccharomyces cerevisiae have been solubilized by detergents. The enzyme transferring mannose from guanosine diphosphate mannose to dolichyl phosphate has been purified 18-fold when based on membrane protein and 140-fold when based on total cell protein. The enzyme transferring mannose from dolichyl phosphate mannose to protein has been purified 48-fold and 380-fold, respectively. A HCl-treated cell-wall mannoprotein from yeast served as acceptor protein for the second enzyme. The solubilized enzyme catalyzing the formation of dolichyl diphosphate mannose has a Km for guanosine diphosphate mannose of 7 x 10(-6) M and is saturated with about 0.15 mM yeast dolichyl phosphate. The metal requirement, pH-optima, and the detergent concentration necessary for optimal activity have been determined for both solubilized enzymes.

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Citations

Oct 15, 1998·International Journal for Parasitology·L Vargas-RodríguezE López-Romero
Mar 1, 1982·Proceedings of the National Academy of Sciences of the United States of America·A Haselbeck, W Tanner
Nov 15, 1985·European Journal of Biochemistry·J W Jensen, J S Schutzbach
Apr 5, 2008·Biochimica Et Biophysica Acta·Yusuke Maeda, Taroh Kinoshita
Apr 1, 1980·European Journal of Biochemistry·G PalamarczykW Tanner
May 1, 1981·European Journal of Biochemistry·C B SharmaW Tanner
Dec 24, 1982·Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences·W TannerL Lehle
Jul 27, 2017·Nature Communications·Rosaria GandiniChristina Divne
Feb 14, 1991·Biochemical and Biophysical Research Communications·N DéglonN Fasel

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