Abstract
In Streptococcus faecium inhibition by both benzylpenicillin and cefotaxime of cells growing at maximal and at reduced rates was associated with saturation of different penicillin-binding proteins. Cells growing at reduced rates were not inhibited by benzylpenicillin concentrations that saturated all penicillin-binding proteins except penicillin-binding protein 5, but did stop growing when this protein was saturated.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Bacterial Proteins*
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Binding, Competitive
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Carboxypeptidases / physiology*
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Carrier Proteins / metabolism
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Carrier Proteins / physiology*
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Cefotaxime / pharmacology
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Hexosyltransferases*
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Kinetics
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Muramoylpentapeptide Carboxypeptidase / metabolism
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Muramoylpentapeptide Carboxypeptidase / physiology*
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Penicillin G / pharmacology
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Penicillin-Binding Proteins
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Peptidyl Transferases*
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Streptococcus / drug effects
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Streptococcus / growth & development*
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Temperature
Substances
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Bacterial Proteins
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Carrier Proteins
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Penicillin-Binding Proteins
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Peptidyl Transferases
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Hexosyltransferases
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Carboxypeptidases
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Muramoylpentapeptide Carboxypeptidase
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Cefotaxime
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Penicillin G