[Comparative analysis of primary structures of yeast dolicholphosphomannosyl- and dolichophosphoglucosyl synthetases and other dolichol-conjugated enzymes].
Primary structure of yeast dolicholphosphomannosyl- (DPMS) and dolicholphosphoglucosylsynthetases (DPGS) have been compared both between themselves and DPMS and DPGS with yeast beta- and alpha-1, 3-mannosyltransferases, glucosyltransferases and rat mannosyl-binding proteins. The long homological segments were revealed. The homological segments of beta- and alpha-1, 3-mannosyltransferases were located in regions having potency to form coiled-coil structures. These structures are known to be included in carbohydrate-binding protein domains. The previous data and the results presented now have made it possible to conclude that the dolichol-coupled enzymes have evolutionary relationship between themselves and common evolutionary roots with carbohydrate-binding proteins (lectins).
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D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D050260:Carbohydrate Metabolism; D002352:Carrier Proteins / Q000378:metabolism; D002384:Catalysis; D005964:Glucosyltransferases / Q000737:chemistry*; D008364:Mannosyltransferases; D008969:Molecular Sequence Data; D051381:Rats; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D017386:Sequence Homology, Amino Acid
D002352:Carrier Proteins; D005964:Glucosyltransferases; D008364:Mannosyltransferases; C022755:dolichyl-phosphate beta-D-mannosyltransferase