RGD Reference Report - Cloning and characterization of mammalian UDP-glucose glycoprotein: glucosyltransferase and the development of a specific substrate for this enzyme. - Rat Genome Database

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Cloning and characterization of mammalian UDP-glucose glycoprotein: glucosyltransferase and the development of a specific substrate for this enzyme.

Authors: Tessier, DC  Dignard, D  Zapun, A  Radominska-Pandya, A  Parodi, AJ  Bergeron, JJ  Thomas, DY 
Citation: Tessier DC, etal., Glycobiology 2000 Apr;10(4):403-12.
RGD ID: 634448
Pubmed: PMID:10764828   (View Abstract at PubMed)

The endoplasmic reticulum enzyme UDP-glucose glycoprotein:glucosyltransferase (UGGT) has the unique property of recognizing incompletely folded glycoproteins and, if they carry an N -linked Man(9)GlcNAc(2)oligosaccharide, of catalyzing the addition of a glucose residue from UDP-glucose. Using peptide sequence information, we have isolated the complete cDNA of rat liver UGGT and expressed it in insect cells. The cDNA specifies an open reading frame which codes for a protein of 1527 residues including an 18 amino acid signal peptide. The protein has a C-terminal tetrapeptide (HEEL) characteristic of endoplasmic reticulum luminal proteins. The purified recombinant enzyme shows the same preference for unfolded polypeptides with N -linked Man(9)GlcNAc(2)glycans as the enzyme purified from rat liver. A genetically engineered Saccharomyces cerevisiae strain capable of producing glyco-proteins with Man(9)GlcNAc(2)core oligosaccharides was constructed and secreted acid phosphatase (G0-AcP) was purified. G0-AcP was used as an acceptor glycoprotein for UGGT and found to be a better substrate than the previously used soybean agglutinin and thyroglobulin. Recombinant rat UGGT has a K (m) of 44 microM for UDP-glucose. A proteolytic fragment of UGGT was found to retain enzymatic activity thus localizing the catalytic site of the enzyme to the C-terminal 37 kDa of the protein. Using site-directed mutagenesis and photoaffinity labeling, we have identified residues D1334, D1336, Q1429, and N1433 to be necessary for the catalytic activity of the enzyme.



Gene Ontology Annotations    Click to see Annotation Detail View

Biological Process

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Uggt1Rat'de novo' post-translational protein folding involved_inTAS PMID:10764828UniProt 

Molecular Function

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Uggt1Ratprotein binding enablesIPIUniProtKB:Q923V8PMID:10764828UniProt 
Uggt1RatUDP-glucose:glycoprotein glucosyltransferase activity enablesIDA PMID:10764828UniProt 
Uggt1RatUDP-glucose:glycoprotein glucosyltransferase activity  TAS  RGD 
Uggt1Ratunfolded protein binding enablesIDA PMID:10764828UniProt 

Objects Annotated

Genes (Rattus norvegicus)
Uggt1  (UDP-glucose glycoprotein glucosyltransferase 1)


Additional Information