Literature DB >> 2383270

A common peptide stretch among enzymes localized to the Golgi apparatus: structural similarity of Golgi-associated glycosyltransferases.

B Bendiak1.   

Abstract

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.

Entities:  

Mesh:

Substances:

Year:  1990        PMID: 2383270     DOI: 10.1016/0006-291x(90)92173-w

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  3 in total

1.  NCB5OR is a novel soluble NAD(P)H reductase localized in the endoplasmic reticulum.

Authors:  Hao Zhu; Kevin Larade; Timothy A Jackson; Jianxin Xie; Annie Ladoux; Helmut Acker; Utta Berchner-Pfannschmidt; Joachim Fandrey; Andrew R Cross; Gudrun S Lukat-Rodgers; Kenton R Rodgers; H Franklin Bunn
Journal:  J Biol Chem       Date:  2004-05-06       Impact factor: 5.157

2.  The 17-residue transmembrane domain of beta-galactoside alpha 2,6-sialyltransferase is sufficient for Golgi retention.

Authors:  S H Wong; S H Low; W Hong
Journal:  J Cell Biol       Date:  1992-04       Impact factor: 10.539

3.  A knowledge base for predicting protein localization sites in eukaryotic cells.

Authors:  K Nakai; M Kanehisa
Journal:  Genomics       Date:  1992-12       Impact factor: 5.736

  3 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.