Saturation mutagenesis reveals the importance of residues αR145 and αF146 of penicillin acylase in the synthesis of β-lactam antibiotics-Reference-Cited by-同舟云学术

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Saturation mutagenesis reveals the importance of residues αR145 and αF146 of penicillin acylase in the synthesis of β-lactam antibiotics

Published:2008-01 Issue:1 Volume:133 Page:18-26
ISSN:0168-1656
Container-title:Journal of Biotechnology
language:en
Short-container-title:Journal of Biotechnology

Author:

Jager Simon A.W.,Shapovalova Irina V.,Jekel Peter A.,Alkema Wynand B.L.,Švedas Vytas K.,Janssen Dick B.

Publisher

Elsevier BV

Subject

Applied Microbiology and Biotechnology,General Medicine,Biotechnology,Bioengineering

Reference34 articles.

1. The use of chromogenic reference substrates for the kinetic analysis of penicillin acylases;Alkema;Anal. Biochem.,1999

2. Characterization of the beta-lactam binding site of penicillin acylase of Escherichia coli by structural and site-directed mutagenesis studies;Alkema;Protein Eng.,2000

3. The role of hydrophobic active-site residues in substrate specificity and acyl transfer activity of penicillin acylase;Alkema;Eur. J. Biochem.,2002

4. Role of αArg145 and βArg263 in the active site of penicillin acylase of Escherichia coli;Alkema;Biochem. J.,2002

5. Pharmacokinetics of β-lactam antibiotics;Bergan;Scand. J. Infect. Dis. Suppl.,1984

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