Document Detail

Mutational analysis of the carboxy-terminal region of UDP-glucuronosyltransferase 2B1.
MedLine Citation:
PMID:  8672245     Owner:  NLM     Status:  MEDLINE    
UDP-glucuronosyltransferases (UGTs) are membrane-bound glycoproteins that are resident in the endoplasmic reticulum with a type I topology. The roles of the membrane-spanning and membrane-proximal cytoplasmic domains in UGT activity were investigated. Site-directed and deletional mutagenesis techniques were used to generate truncated forms of the enzyme, forms with altered residues, or forms with heterologous tails appended to the carboxyl terminus. The presence of the transmembrane domain was a critical requirement for UGT activity whereas the cytoplasmic domain seemed to be a modulator of activity but was not essential. Truncation of the protein did not appear to lead to scavenging and degradation, although appending long heterologous tails to the cytoplasmic domain did seem to trigger proteolysis. Analysis of enzyme kinetic parameters and enzyme latency allowed us to discount substrate binding or substrate transport defects as the cause of ameliorated UGT activity in the mutants.
R Meech; G Yogalingam; P I Mackenzie
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  DNA and cell biology     Volume:  15     ISSN:  1044-5498     ISO Abbreviation:  DNA Cell Biol.     Publication Date:  1996 Jun 
Date Detail:
Created Date:  1996-08-12     Completed Date:  1996-08-12     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  9004522     Medline TA:  DNA Cell Biol     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  489-94     Citation Subset:  IM    
Department of Clinical Pharmacology, Flinders Medical Centre, Bedford Park, South Australia.
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MeSH Terms
Amino Acid Sequence
Cell Line
Cell Membrane / chemistry
Cercopithecus aethiops
Cytoplasm / chemistry
Glucuronosyltransferase / chemistry*,  genetics,  metabolism*
Molecular Sequence Data
Reg. No./Substance:

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