Document Detail

Penicillin-binding protein 2x of Streptococcus pneumoniae: enzymic activities and interactions with beta-lactams.
MedLine Citation:
PMID:  8318005     Owner:  NLM     Status:  MEDLINE    
The high-molecular-mass penicillin-binding protein (PBP) 2x, one of the primary targets of beta-lactam antibiotics in Streptococcus pneumoniae, has been produced as a soluble form and purified in large amounts. It has been shown to catalyse hydrolysis and transfer reactions with different ester and thiolester substrates and its catalytic behaviour was often similar to that of the soluble DD-peptidase from Streptomyces R61. This provided an easy method to monitor the activity of the PBP. For the first time, a reliable kinetic study of the interaction between a lethal target and beta-lactam antibiotics has been performed. Characteristic kinetic parameters were obtained with different beta-lactam compounds. These results not only validated the mechanism established with non-essential extracellular enzymes, but will also constitute the basis for comparative studies of the low-affinity variants from penicillin-resistant strains.
M Jamin; C Damblon; S Millier; R Hakenbeck; J M Frère
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  The Biochemical journal     Volume:  292 ( Pt 3)     ISSN:  0264-6021     ISO Abbreviation:  Biochem. J.     Publication Date:  1993 Jun 
Date Detail:
Created Date:  1993-07-27     Completed Date:  1993-07-27     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  2984726R     Medline TA:  Biochem J     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  735-41     Citation Subset:  IM    
Laboratoire d'Enzymologie, Université de liège, Sart Tilman, Belgium.
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MeSH Terms
Amino Acids / metabolism*
Anti-Bacterial Agents / metabolism*
Bacterial Proteins*
Carrier Proteins / isolation & purification,  metabolism*
Cefotaxime / metabolism
Chromatography, Ion Exchange
Hexosyltransferases / isolation & purification,  metabolism*
Isoelectric Focusing
Multienzyme Complexes / isolation & purification,  metabolism*
Muramoylpentapeptide Carboxypeptidase*
Penicillin G / metabolism
Penicillin-Binding Proteins
Peptides / metabolism
Peptidyl Transferases / isolation & purification,  metabolism*
Streptococcus pneumoniae / enzymology*
Structure-Activity Relationship
Substrate Specificity
Reg. No./Substance:
0/Amino Acids; 0/Anti-Bacterial Agents; 0/Bacterial Proteins; 0/Carrier Proteins; 0/Multienzyme Complexes; 0/Penicillin-Binding Proteins; 0/Peptides; 128284-03-7/PBP 2x protein, Streptococcus; 61-33-6/Penicillin G; 63527-52-6/Cefotaxime; EC Transferases; EC 2.4.1.-/Hexosyltransferases; EC Carboxypeptidase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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