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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1984-3-5
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pubmed:databankReference |
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pubmed:abstractText |
A mutant of Escherichia coli has been described that produces an altered form of penicillin-binding protein 5 which still binds penicillin but is unable to catalyse the release of the bound penicilloyl moiety. We show that the mutation is caused by a single nucleotide transition that results in a change from glycine at residue 105 of the wild-type sequence of penicillin-binding protein 5 to aspartate in the mutant.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0014-5793
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pubmed:author |
|
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pubmed:issnType |
Print
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pubmed:day |
9
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pubmed:volume |
165
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
185-9
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:6319180-Acylation,
pubmed-meshheading:6319180-Amino Acid Sequence,
pubmed-meshheading:6319180-Bacterial Proteins,
pubmed-meshheading:6319180-Base Sequence,
pubmed-meshheading:6319180-Carrier Proteins,
pubmed-meshheading:6319180-DNA, Bacterial,
pubmed-meshheading:6319180-DNA Restriction Enzymes,
pubmed-meshheading:6319180-Escherichia coli,
pubmed-meshheading:6319180-Hexosyltransferases,
pubmed-meshheading:6319180-Muramoylpentapeptide Carboxypeptidase,
pubmed-meshheading:6319180-Mutation,
pubmed-meshheading:6319180-Penicillin G,
pubmed-meshheading:6319180-Penicillin-Binding Proteins,
pubmed-meshheading:6319180-Peptidyl Transferases,
pubmed-meshheading:6319180-Structure-Activity Relationship
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pubmed:year |
1984
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pubmed:articleTitle |
An amino acid substitution that blocks the deacylation step in the enzyme mechanism of penicillin-binding protein 5 of Escherichia coli.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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