Efficient catalysis by beta-lactamase from Staphylococcus aureus PC1 accompanied by accumulation of an acyl-enzyme (Q41828188)

12 October 2017

Efficient catalysis by beta-lactamase from Staphylococcus aureus PC1 accompanied by accumulation of an acyl-enzyme (English)

1 reference

12 October 2017

Staphylococcus aureus

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Qi X

1

1 reference

PMCID

1217229

12 October 2017

Virden R

series ordinal

2

1 reference

PMCID

1217229

12 October 2017

language of work or name

English

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publication date

1 April 1996

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12 October 2017

5

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inferred from page(s)

published in

Biochemical Journal

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12 October 2017

315 ( Pt 2)

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12 October 2017

537-541

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Effects of site-specific mutagenesis of tyrosine 105 in a class A beta-lactamase

12 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1217229

The enigmatic catalytic mechanism of active-site serine beta-lactamases

6 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1217229

Evidence for two acyl group conformations in some furylacryloyl- and thienylacryloylchymotrypsins: resonance Raman studies of enzyme--substrate intermediates at pH 3.0.

6 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1217229

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

6 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1217229

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

6 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1217229

The analysis of enzyme progress curves by numerical differentiation, including competitive product inhibition and enzyme reactivation

6 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1217229

Bacterial resistance to beta-lactam antibiotics: crystal structure of beta-lactamase from Staphylococcus aureus PC1 at 2.5 A resolution.

6 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1217229

Trapping the acyl-enzyme intermediate in beta-lactamase I catalysis

6 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1217229

Kinetic parameters of the acyl-enzyme mechanism and conditions for quasi-equilibrium and for optimal catalytic characteristics

6 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1217229

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

6 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1217229

Cryoenzymology of staphylococcal beta-lactamase: trapping a serine-70-linked acyl-enzyme

6 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1217229

Refined crystal structure of beta-lactamase from Staphylococcus aureus PC1 at 2.0 A resolution

6 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1217229

Structural basis for the inactivation of the P54 mutant of beta-lactamase from Staphylococcus aureus PC1

6 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1217229

The mechanism of folding of globular proteins. Suitability of a penicillinase from Staphylococcus Aureus as a model for refolding studies

6 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1217229

N-(2-furyl) acryloyl penicillin: A novel compound for the spectrophotometric assay of .BETA.-lactamase I

6 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1217229

Diffusion-limited component of reactions catalyzed by Bacillus cereus beta-lactamase I.

6 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1217229

Correlations between reactivity and structure of some chromophoric acylchymotrypsins by resonance Raman spectroscopy

18 August 2018

1 reference

12 December 2020

Enzyme kinetics in solvents of increased viscosity. Dynamic aspects of carbonic anhydrase catalysis

1 reference

12 December 2020

Extent of accumulation of an acylenzyme during beta-lactamase catalysis

1 reference

12 December 2020

Inhibition of β-lactamase by clavulanate

1 reference

12 December 2020

Identifiers

DOI

10.1042/BJ3150537

1 reference

12 October 2017

1 reference

12 October 2017

1 reference

PMCID

1217229