Document Detail

Study of nucleophile binding in the penicillin acylase active center. Kinetic analysis.
MedLine Citation:
PMID:  12733976     Owner:  NLM     Status:  MEDLINE    
The influence of the external nucleophile (6-aminopenicillanic acid) on the kinetics of the penicillin acylase-catalyzed acyl transfer reactions was studied using a highly sensitive spectrophotometric assay. An adequate kinetic scheme is suggested based on kinetic analysis of the experimental dependencies of the k(cat) and K(m) values on the nucleophile concentration. The proposed kinetic scheme has been verified by a quantitative description of the above-mentioned experimental dependencies using the set of kinetic parameters obtained from independent experiments. Such an approach can be used for modeling of different penicillin acylase-catalyzed acyl transfer reactions.
M I Youshko; A L Bukhanov; V K Svedas
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Biochemistry. Biokhimii͡a     Volume:  68     ISSN:  0006-2979     ISO Abbreviation:  Biochemistry Mosc.     Publication Date:  2003 Mar 
Date Detail:
Created Date:  2003-05-07     Completed Date:  2004-01-06     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0376536     Medline TA:  Biochemistry (Mosc)     Country:  United States    
Other Details:
Languages:  eng     Pagination:  334-8     Citation Subset:  IM    
Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow, 119992 Russia.
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MeSH Terms
Aminobenzoic Acids / chemistry,  metabolism
Binding Sites
Escherichia coli Proteins / chemistry,  metabolism
Penicillanic Acid / analogs & derivatives*,  metabolism*,  pharmacology
Penicillin Amidase / chemistry,  metabolism*
Reproducibility of Results
Substrate Specificity
Reg. No./Substance:
0/Aminobenzoic Acids; 0/Escherichia coli Proteins; 551-16-6/aminopenicillanic acid; 87-53-6/Penicillanic Acid; EC Amidase

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