rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
2
|
pubmed:dateCreated |
1996-10-21
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pubmed:databankReference |
|
pubmed:abstractText |
Using conserved fingerprints in the glycosyltransferase (GTase) domain of high-molecular-weight penicillin-binding proteins (PBP), a gene (mgt) encoding a putative monofunctional glycosyltransferase has been identified in Haemophilus influenzae and in other bacteria] species. Here we report the cloning of the homologous Escherichia coli gene and show that the solubilised membrane fraction of E. coli cells overexpressing the mgt gene contain a significantly increased peptidoglycan synthesis activity. In contrast to the high-molecular-weight PBPs, this activity is not inhibited by Flavomycin.
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pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Aug
|
pubmed:issn |
0014-5793
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
26
|
pubmed:volume |
392
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
184-8
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:8772200-Amino Acid Sequence,
pubmed-meshheading:8772200-Base Sequence,
pubmed-meshheading:8772200-DNA Primers,
pubmed-meshheading:8772200-Escherichia coli,
pubmed-meshheading:8772200-Glycosyltransferases,
pubmed-meshheading:8772200-Membrane Proteins,
pubmed-meshheading:8772200-Molecular Sequence Data,
pubmed-meshheading:8772200-Peptidoglycan,
pubmed-meshheading:8772200-Recombinant Proteins,
pubmed-meshheading:8772200-Sequence Homology, Amino Acid,
pubmed-meshheading:8772200-Species Specificity
|
pubmed:year |
1996
|
pubmed:articleTitle |
The monofunctional glycosyltransferase of Escherichia coli is a member of a new class of peptidoglycan-synthesising enzymes.
|
pubmed:affiliation |
Pharma Research Department, F. Hoffman-La Roche Ltd., Basel, Switzerland.
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pubmed:publicationType |
Journal Article
|