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

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., Or...

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Veröffentlicht in:	The Journal of biological chemistry 1993-11, Vol.268 (32), p.24190-24196
Hauptverfasser:	SCHUTZBACH, J. S, ZIMMERMAN, J. W, FORSEE, W. T
Format:	Artikel
Sprache:	eng
Schlagworte:	actividad enzimatica activite enzymatique Amino Acid Sequence Analytical, structural and metabolic biochemistry Base Sequence Binding Sites Biological and medical sciences Catalysis Dolichols - metabolism Electrophoresis, Polyacrylamide Gel Enzymes and enzyme inhibitors enzymic activity escherichia Escherichia coli - genetics Fundamental and applied biological sciences. Psychology gene genes Genes, Fungal genetic transformation glicosiltransferasas glycosyltransferase glycosyltransferases Mannosyltransferases - genetics Mannosyltransferases - isolation & purification Mannosyltransferases - metabolism Molecular Sequence Data mutacion Mutagenesis, Site-Directed mutation Oligodeoxyribonucleotides oligosacaridos oligosaccharide oligosaccharides purificacion purification Recombinant Proteins - genetics Recombinant Proteins - isolation & purification Recombinant Proteins - metabolism Saccharomyces cerevisiae Saccharomyces cerevisiae - enzymology Saccharomyces cerevisiae - genetics Transferases transformacion genetica transformation genetique
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