[Comparative analysis of primary structures of yeast dolicholphosphomannosyl- and dolichophosphoglucosyl synthetases and other dolichol-conjugated enzymes]

Ukr Biokhim Zh (1978). 1996 Jul-Aug;68(4):64-75.
[Article in Russian]

Abstract

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).

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Carbohydrate Metabolism
  • Carrier Proteins / metabolism
  • Catalysis
  • Glucosyltransferases / chemistry*
  • Mannosyltransferases
  • Molecular Sequence Data
  • Rats
  • Saccharomyces cerevisiae / enzymology*
  • Sequence Homology, Amino Acid

Substances

  • Carrier Proteins
  • Glucosyltransferases
  • Mannosyltransferases
  • dolichyl-phosphate beta-D-mannosyltransferase