Literature DB >> 308803

Reversible inhibition of penicillinase by quinacillin: evaluation of mechanisms involving two conformational states of the enzyme.

R Virden, A F Bristow, R H Pain.   

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Year:  1978        PMID: 308803     DOI: 10.1016/0006-291x(78)90875-6

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


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  7 in total

1.  Beta-lactamases as fully efficient enzymes. Determination of all the rate constants in the acyl-enzyme mechanism.

Authors:  H Christensen; M T Martin; S G Waley
Journal:  Biochem J       Date:  1990-03-15       Impact factor: 3.857

2.  The crystal structure of beta-lactamase from Staphylococcus aureus at 0.5 nm resolution.

Authors:  J Moult; L Sawyer; O Herzberg; C L Jones; A F Coulson; D W Green; M M Harding; R P Ambler
Journal:  Biochem J       Date:  1985-01-01       Impact factor: 3.857

3.  Accumulation of acyl-enzyme intermediates during turnover of penicillins by the class A beta-lactamase of Staphylococcus aureus PC1.

Authors:  R F Pratt; T S McConnell; S J Murphy
Journal:  Biochem J       Date:  1988-09-15       Impact factor: 3.857

4.  Substrate-induced inactivation of the OXA2 beta-lactamase.

Authors:  P Ledent; J M Frère
Journal:  Biochem J       Date:  1993-11-01       Impact factor: 3.857

5.  Identification of the site of covalent attachment of nafcillin, a reversible suicide inhibitor of beta-lactamase.

Authors:  A K Tan; A L Fink
Journal:  Biochem J       Date:  1992-01-01       Impact factor: 3.857

6.  Reversible deactivation of beta-lactamase by quinacillin. Extent of the conformational change in the isolated transitory complex.

Authors:  K C Persaud; R H Pain; R Virden
Journal:  Biochem J       Date:  1986-08-01       Impact factor: 3.857

7.  Interactions between active-site-serine beta-lactamases and mechanism-based inactivators: a kinetic study and an overview.

Authors:  A Matagne; M F Ghuysen; J M Frère
Journal:  Biochem J       Date:  1993-11-01       Impact factor: 3.857

  7 in total

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