[A theoretical analysis of the secondary structure and topology of dolichol-coupled enzymes].
Hydropathic profile for several dolichol-coupled enzymes (mammal N-acetylglucosamine-1-phosphate transferases (GPT), yeast products of genes ALG7, ALG1, DMP1 and SEC59) taking part in the biosynthesis of complex oligosaccharide used for N-glycosylation of proteins in endoplasmic reticulum (ER) of eukaryotic cells has been calculated and constructed. On the basis of analysis of present research and available data sites of amino acid sequence (AAS) potentially capable to penetrate ER membrane were identified. A tendency of AAS segments of dolichol-coupled enzymes to form alpha-helices, beta-folded structures and beta-bends was calculated using correlational methods. For COOH-terminal part of ALG1 the prediction about the capability to form helix-helix structures was made. It was concluded that at least three types of topological models in ER membrane were present for the mentioned dolichol-coupled enzymes.
D000595:Amino Acid Sequence; D000818:Animals; D004286:Dolichols / Q000737:chemistry*; D004721:Endoplasmic Reticulum / Q000201:enzymology; D005656:Fungal Proteins / Q000737:chemistry; D006031:Glycosylation; D051379:Mice; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017351:N-Acetylglucosaminyltransferases / Q000737:chemistry*; D009844:Oligosaccharides / Q000096:biosynthesis; D017433:Protein Structure, Secondary; D015003:Yeasts / Q000201:enzymology / Q000235:genetics
D004286:Dolichols; D005656:Fungal Proteins; D009844:Oligosaccharides; D017351:N-Acetylglucosaminyltransferases
Teoreticheskiĭ analiz vtorichnoĭ struktury i topologii dolikhol-sopriazhennykh fermentov.