Linked Life Data

11985586

Source:http://linkedlifedata.com/resource/pubmed/id/11985586

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pubmed-article:11985586pubmed:abstractTextPenicillin acylase of Escherichia coli catalyses the hydrolysis and synthesis of beta-lactam antibiotics. To study the role of hydrophobic residues in these reactions, we have mutated three active-site phenylalanines. Mutation of alphaF146, betaF24 and betaF57 to Tyr, Trp, Ala or Leu yielded mutants that were still capable of hydrolysing the chromogenic substrate 2-nitro-5-[(phenylacetyl)amino]-benzoic acid. Mutations on positions alphaF146 and betaF24 influenced both the hydrolytic and acyl transfer activity. This caused changes in the transferase/hydrolase ratios, ranging from a 40-fold decrease for alphaF146Y and alphaF146W to a threefold increase for alphaF146L and betaF24A, using 6-aminopenicillanic acid as the nucleophile. Further analysis of the betaF24A mutant showed that it had specificity constants (kcat/Km) for p-hydroxyphenylglycine methyl ester and phenylglycine methyl ester that were similar to the wild-type values, whereas the specificity constants for p-hydroxyphenylglycine amide and phenylglycine amide had decreased 10-fold, due to a decreased kcat value. A low amidase activity was also observed for the semisynthetic penicillins amoxicillin and ampicillin and the cephalosporins cefadroxil and cephalexin, for which the kcat values were fivefold to 10-fold lower than the wild-type values. The reduced specificity for the product and the high initial transferase/hydrolase ratio of betaF24A resulted in high yields in acyl transfer reactions.lld:pubmed
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pubmed-article:11985586pubmed:authorpubmed-author:JanssenDick...lld:pubmed
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pubmed-article:11985586pubmed:volume269lld:pubmed
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pubmed-article:11985586pubmed:pagination2093-100lld:pubmed
pubmed-article:11985586pubmed:dateRevised2007-7-23lld:pubmed
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pubmed-article:11985586pubmed:year2002lld:pubmed
pubmed-article:11985586pubmed:articleTitleThe role of hydrophobic active-site residues in substrate specificity and acyl transfer activity of penicillin acylase.lld:pubmed
pubmed-article:11985586pubmed:affiliationDepartment of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, the Netherlands.lld:pubmed
pubmed-article:11985586pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:11985586pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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