| Study of nucleophile binding in the penicillin acylase active center. Kinetic analysis. | |
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MedLine Citation:
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PMID: 12733976 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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. |
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Authors:
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M I Youshko; A L Bukhanov; V K Svedas |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Biochemistry. Biokhimii͡a Volume: 68 ISSN: 0006-2979 ISO Abbreviation: Biochemistry Mosc. Publication Date: 2003 Mar |
Date Detail:
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Created Date: 2003-05-07 Completed Date: 2004-01-06 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 0376536 Medline TA: Biochemistry (Mosc) Country: United States |
Other Details:
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Languages: eng Pagination: 334-8 Citation Subset: IM |
Affiliation:
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Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow, 119992 Russia. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Aminobenzoic Acids
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chemistry,
metabolism Binding Sites Catalysis Escherichia coli Proteins / chemistry, metabolism Hydrolysis Kinetics Penicillanic Acid / analogs & derivatives*, metabolism*, pharmacology Penicillin Amidase / chemistry, metabolism* Reproducibility of Results Substrate Specificity |
| Chemical | |
Reg. No./Substance:
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0/Aminobenzoic Acids; 0/Escherichia coli Proteins; 551-16-6/aminopenicillanic acid; 87-53-6/Penicillanic Acid; EC 3.5.1.11/Penicillin Amidase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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