Accumulation of acyl-enzyme intermediates during turnover of penicillins by the class A beta-lactamase of Staphylococcus aureus PC1. (Q42817920)

7 November 2017

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

1 reference

7 November 2017

Staphylococcus aureus

1 reference

Pratt RF

1

1 reference

7 November 2017

McConnell TS

series ordinal

2

1 reference

7 November 2017

Murphy SJ

series ordinal

3

1 reference

7 November 2017

language of work or name

English

0 references

publication date

1 September 1988

1 reference

7 November 2017

1 reference

7 November 2017

254

1 reference

7 November 2017

3

1 reference

7 November 2017

919-922

1 reference

Pre-steady state beta-lactamase kinetics. Observation of a covalent intermediate during turnover of a fluorescent cephalosporin by the beta-lactamase of STaphylococcus aureus PC1.

7 November 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1135173

The acyl-enzyme mechanism of beta-lactamase action. The evidence for class C Beta-lactamases

27 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1135173

Inactivation of Bacillus cereus beta-lactamase I by 6 beta-bromopencillanic acid: mechanism

27 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1135173

Pre-steady state beta-lactamase kinetics. The trapping of a covalent intermediate and the interpretation of pH rate profiles.

27 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1135173

The active site of the P99 β-lactamase from Enterobacter cloacae

27 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1135173

Substrate-specific inactivation of staphylococcal penicillinase

27 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1135173

Single-turnover and steady-state kinetics of hydrolysis of cephalosporins by beta-lactamase I from Bacillus cereus

27 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1135173

Mechanism of inhibition of the PC1 beta-lactamase of Staphylococcus aureus by cephalosporins: importance of the 3'-leaving group

27 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1135173

Cryoenzymology of beta-lactamases

27 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1135173

Kinetics and mechanism of the serine beta-lactamase catalyzed hydrolysis of depsipeptides

27 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1135173

Acquisition of substrate-specific parameters during the catalytic reaction of penicillinase

27 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1135173

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

27 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1135173

Penicillinase active sites: Labelling of serine-44 in β-lactamase I by 6β-bromopenicillanic acid

27 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1135173

Inactivation of staphylococcal penicillinase by reaction with resistant penicillins.

27 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1135173

Kinetics of beta-lactamase inactivation of penicillins. II. Effect of competitive inhibitors.

27 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1135173

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

27 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1135173

STUDIES ON PENICILLINASE PRODUCED BY A STRAIN OF STAPHYLOCOCCUS AUREUS.

27 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1135173

Behaviour of some derivatives of 7-aminocephalosporanic acid and 6-aminopenicillanic acidas substrates, inhibitors and inducers of penicillinases

16 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1135173

Identification of the active site of Citrobacter freundii beta-lactamase using dansyl-penicillin

16 August 2018

1 reference

12 December 2020

Oxygenation-linked subunit interactions in human hemoglobin: analysis of linkage functions for constituent energy terms

1 reference

12 December 2020

Conformation of a stable intermediate on the folding pathway of Staphylococcus aureus penicillinase

1 reference

12 December 2020

beta-Lactamase proceeds via an acyl-enzyme intermediate. Interaction of the Escherichia coli RTEM enzyme with cefoxitin

1 reference

12 December 2020

Isolation of a covalent intermediate in beta -lactamase I catalysis

1 reference

12 December 2020

Identifiers

DOI

10.1042/BJ2540919

1 reference

7 November 2017

1 reference

7 November 2017

PubMed publication ID

3264153

1 reference