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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
24
|
| pubmed:dateCreated |
1990-9-27
|
| pubmed:databankReference | |
| pubmed:abstractText |
UDP-GlcNAc:dolichol phosphate N-acetylglucosamine-1-phosphate transferase (GPT) catalyzes the initial reaction required for synthesis of dolichol-P-P-oligosaccharides. We report here on the sequence and expression of a full-length cDNA clone encoding hamster GPT. The cDNA predicts a protein of 408 amino acid residues including 10 hydrophobic segments. Several portions of the hamster GPT sequence constituting one-third of the protein have 60% or greater identity with yeast GPT, and one-half of the conserved sequence falls within the hydrophobic segments. In addition, hamster GPT has two copies of a putative dolichol recognition sequence recently identified in three yeast enzymes that interact with dolichol. The protein lacks KDEL or DEKKMP-type carboxyl-terminal ER sorting sequences. When expressed in COS-1 cells, the cDNA causes a 5-7-fold increase of GPT activity in membrane fractions. The activity was completely inhibitable by tunicamycin, and the primary product was shown to be GlcNAc-pyrophosphoryldolichol. This cDNA represents the first enzyme of the dolichol-oligosaccharide biosynthetic pathway to be cloned from a vertebrate source and demonstrates structural homology between the enzymes of the yeast and mammalian pathways.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphotransferases,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Transferases (Other Substituted...,
http://linkedlifedata.com/resource/pubmed/chemical/UDPacetylglucosamine-dolichyl-phosph...
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Aug
|
| pubmed:issn |
0021-9258
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
25
|
| pubmed:volume |
265
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
14250-5
|
| pubmed:dateRevised |
2007-11-14
|
| pubmed:meshHeading |
pubmed-meshheading:2167312-Amino Acid Sequence,
pubmed-meshheading:2167312-Animals,
pubmed-meshheading:2167312-Base Sequence,
pubmed-meshheading:2167312-Cell Line,
pubmed-meshheading:2167312-Cloning, Molecular,
pubmed-meshheading:2167312-Cricetinae,
pubmed-meshheading:2167312-DNA,
pubmed-meshheading:2167312-Gene Library,
pubmed-meshheading:2167312-Models, Structural,
pubmed-meshheading:2167312-Molecular Sequence Data,
pubmed-meshheading:2167312-Phosphotransferases,
pubmed-meshheading:2167312-Protein Conformation,
pubmed-meshheading:2167312-RNA, Messenger,
pubmed-meshheading:2167312-Restriction Mapping,
pubmed-meshheading:2167312-Saccharomyces cerevisiae,
pubmed-meshheading:2167312-Sequence Homology, Nucleic Acid,
pubmed-meshheading:2167312-Transfection,
pubmed-meshheading:2167312-Transferases (Other Substituted Phosphate Groups)
|
| pubmed:year |
1990
|
| pubmed:articleTitle |
Cloning, sequence, and expression of a cDNA encoding hamster UDP-GlcNAc:dolichol phosphate N-acetylglucosamine-1-phosphate transferase.
|
| pubmed:affiliation |
Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas 75235.
|
| pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|