Literature DB >> 15358003

Improved beta-lactam acylases and their use as industrial biocatalysts.

Charles F Sio1, Wim J Quax.   

Abstract

Whereas the beta-lactam acylases are traditionally used for the hydrolytic processing of penicillin G and cephalosporin C, new and mutated acylases can be used for the hydrolysis of alternative fermentation products as well as for the synthesis of semisynthetic beta-lactam antibiotics. Three-dimensional structural analyses and site-directed mutagenesis studies have increased the understanding of the catalytic mechanism of these enzymes. The yield of hydrolysis and synthesis has been greatly improved by process design, including immobilization of the enzyme and the use of alternative reaction media. Significant advances have also been made in the resolution of racemic mixtures by means of stereoselective acylation/hydrolysis using beta-lactam acylases.

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Year:  2004        PMID: 15358003     DOI: 10.1016/j.copbio.2004.06.006

Source DB:  PubMed          Journal:  Curr Opin Biotechnol        ISSN: 0958-1669            Impact factor:   9.740


  9 in total

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2.  Genetic modification of the penicillin G acylase surface to improve its reversible immobilization on ionic exchangers.

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Journal:  Infect Immun       Date:  2006-03       Impact factor: 3.441

4.  Autoproteolytic activation of ThnT results in structural reorganization necessary for substrate binding and catalysis.

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6.  Computational design of catalytic dyads and oxyanion holes for ester hydrolysis.

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Journal:  J Am Chem Soc       Date:  2012-09-21       Impact factor: 15.419

7.  New active site oriented glyoxyl-agarose derivatives of Escherichia coli penicillin G acylase.

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Review 8.  Deciphering Physiological Functions of AHL Quorum Quenching Acylases.

Authors:  Putri D Utari; Jan Vogel; Wim J Quax
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  9 in total

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