Abstract
Penicillin-binding proteins (PBPs) and b-lactamases are related enzymes, the former are the targets for b-lactam antibiotics and the latter are resistance enzyme to these antibiotics. The two families of enzymes share structural topologies and certain mechanistic features. However, these classes of enzymes have diversified substantially and have broadened the reaction repertoire for their catalytic properties. This report addresses the issues of the evolution of function of these proteins.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
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Review
MeSH terms
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Acylation
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Anti-Bacterial Agents / pharmacology*
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Bacterial Proteins*
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Binding Sites
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Carrier Proteins / metabolism*
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Hexosyltransferases*
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Muramoylpentapeptide Carboxypeptidase / metabolism*
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Penicillin-Binding Proteins
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Penicillins / metabolism*
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Peptidyl Transferases*
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Phylogeny
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beta-Lactam Resistance / physiology
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beta-Lactamases / chemistry*
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beta-Lactamases / metabolism
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beta-Lactams
Substances
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Anti-Bacterial Agents
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Bacterial Proteins
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Carrier Proteins
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Penicillin-Binding Proteins
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Penicillins
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beta-Lactams
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Peptidyl Transferases
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Hexosyltransferases
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Muramoylpentapeptide Carboxypeptidase
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beta-Lactamases