A common peptide stretch among enzymes localized to the Golgi apparatus: structural similarity of Golgi-associated glycosyltransferases.
A common peptide motif has been discovered among a series of Golgi-localized glycosyltransferases. The peptide stretch, (Ser/Thr)-X-(Glu/Gln)-(Arg/Lys), always occurs near a hydrophobic domain close to the N-terminus of these enzymes which is believed to anchor them to the membrane lipid bilayer (Paulson and Colley, J. Biol. Chem., 264, 17615-17618, 1989). The finding that this similar peptide motif is not associated with catalytic activity of these enzymes, and its presence near the hydrophobic domain suggest that the stretch may be involved in localization of these enzymes to the Golgi apparatus.
Bendiak
B
B
Biomembrane Institute, University of Washington, Seattle 98119.
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D006056:Golgi Apparatus / Q000201:enzymology*; D006602:Hexosyltransferases / Q000378:metabolism*; D006801:Humans; D008969:Molecular Sequence Data; D011487:Protein Conformation; D051381:Rats; D012689:Sequence Homology, Nucleic Acid
D006602:Hexosyltransferases; C018660:asparagine-N-glycosyltransferase