(Q38299801)

English

Substitution of Asp for Asn at position 132 in the active site of TEM beta-lactamase. Activity toward different substrates and effects of neighboring residues

scientific article published on January 1995

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scholarly article

1 reference

Europe PubMed Central

1 September 2017

Substitution of Asp for Asn at position 132 in the active site of TEM beta-lactamase. Activity toward different substrates and effects of neighboring residues (English)

1 reference

Europe PubMed Central

1 September 2017

author name string

Osuna J

1

1 reference

Europe PubMed Central

1 September 2017

Viadiu H

2

1 reference

Europe PubMed Central

1 September 2017

Fink AL

3

1 reference

Europe PubMed Central

1 September 2017

Soberón X

4

1 reference

Europe PubMed Central

1 September 2017

language of work or name

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publication date

1 January 1995

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Europe PubMed Central

1 September 2017

Journal of Biological Chemistry

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Europe PubMed Central

1 September 2017

270

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Europe PubMed Central

1 September 2017

775-780

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Europe PubMed Central

1 September 2017

2

1 reference

Europe PubMed Central

1 September 2017

A standard numbering scheme for the class A beta-lactamases

1 reference

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21 January 2018

Structure of a phosphonate-inhibited beta-lactamase. An analog of the tetrahedral transition state/intermediate of beta-lactam hydrolysis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.2.781

21 January 2018

Phylogeny of LCR-1 and OXA-5 with class A and class D beta-lactamases

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.2.781

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.2.781

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.2.781

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.2.781

21 January 2018

A means to reduce the complexity of oligonucleotides encoding degenerate peptides

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.2.781

21 January 2018

More extended-spectrum beta-lactamases

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.2.781

21 January 2018

Crystal structure of Escherichia coli TEM1 beta-lactamase at 1.8 A resolution

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.2.781

21 January 2018

Site-saturation mutagenesis and three-dimensional modelling of ROB-1 define a substrate binding role of Ser130 in class A beta-lactamases

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.2.781

21 January 2018

A catalytically-impaired class A beta-lactamase: 2 A crystal structure and kinetics of the Bacillus licheniformis E166A mutant

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.2.781

21 January 2018

Gly-238-Ser substitution changes the substrate specificity of the SHV class A beta-lactamases.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.2.781

21 January 2018

Beta-lactamase of Bacillus licheniformis 749/C at 2 A resolution

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.2.781

21 January 2018

Substitution of lysine at position 104 or 240 of TEM-1pTZ18R beta-lactamase enhances the effect of serine-164 substitution on hydrolysis or affinity for cephalosporins and the monobactam aztreonam.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.2.781

21 January 2018

Molecular structure of the acyl-enzyme intermediate in beta-lactam hydrolysis at 1.7 A resolution

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.2.781

21 January 2018

A spectrophotometric assay of beta-lactamase action on penicillins

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.2.781

21 January 2018

Identifiers

10.1074/JBC.270.2.781

1 reference

Europe PubMed Central

1 September 2017

1 reference

Europe PubMed Central

1 September 2017

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