(Q44894410)

7 December 2017

Structural determinants of substrate binding to Bacillus cereus metallo-beta-lactamase (English)

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7 December 2017

Bacillus cereus

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1

1 reference

7 December 2017

Alejandro J Vila

2

1 reference

PubMed ID

15140877

7 December 2017

language of work or name

English

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publication date

31 March 2004

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Journal of Biological Chemistry

7 December 2017

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7 December 2017

279

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7 December 2017

26046-26051

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7 December 2017

25

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Beta-lactamases and bacterial resistance to antibiotics

7 December 2017

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311373200

Metallo-beta-lactamase: structure and mechanism

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311373200

Standard numbering scheme for class B beta-lactamases

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311373200

An overview of the kinetic parameters of class B beta-lactamases

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311373200

Kinetic analysis of extension of substrate specificity with Xanthomonas maltophilia, Aeromonas hydrophila, and Bacillus cereus metallo-beta-lactamases

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311373200

Characterization and sequence of the Chryseobacterium (Flavobacterium) meningosepticum carbapenemase: a new molecular class B beta-lactamase showing a broad substrate profile

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311373200

Purification, characterization, and kinetic studies of a soluble Bacteroides fragilis metallo-beta-lactamase that provides multiple antibiotic resistance

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311373200

Spectroscopic characterization of a binuclear metal site in Bacillus cereus beta-lactamase II.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311373200

Mono- and binuclear Zn2+-beta-lactamase. Role of the conserved cysteine in the catalytic mechanism

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311373200

Exploring the role and the binding affinity of a second zinc equivalent in B. cereus metallo-beta-lactamase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311373200

Mono- and binuclear Zn-beta-lactamase from Bacteroides fragilis: catalytic and structural roles of the zinc ions.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311373200

IMP-1 metallo-beta-lactamase: effect of chelators and assessment of metal requirement by electrospray mass spectrometry.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311373200

Familial mutations and zinc stoichiometry determine the rate-limiting step of nitrocefin hydrolysis by metallo-beta-lactamase from Bacteroides fragilis

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311373200

Crystal structure of the wide-spectrum binuclear zinc beta-lactamase from Bacteroides fragilis

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311373200

Crystal structure of the zinc-dependent beta-lactamase from Bacillus cereus at 1.9 A resolution: binuclear active site with features of a mononuclear enzyme

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311373200

The crystal structure of the L1 metallo-beta-lactamase from Stenotrophomonas maltophilia at 1.7 A resolution

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311373200

Three-dimensional structure of FEZ-1, a monomeric subclass B3 metallo-beta-lactamase from Fluoribacter gormanii, in native form and in complex with D-captopril

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311373200

Antibiotic sensitization using biphenyl tetrazoles as potent inhibitors of Bacteroides fragilis metallo-beta-lactamase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311373200

Unanticipated inhibition of the metallo-beta-lactamase from Bacteroides fragilis by 4-morpholineethanesulfonic acid (MES): a crystallographic study at 1.85-A resolution

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311373200

Succinic acids as potent inhibitors of plasmid-borne IMP-1 metallo-beta-lactamase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311373200

The 1.5-A structure of Chryseobacterium meningosepticum zinc beta-lactamase in complex with the inhibitor, D-captopril

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311373200

Molecular dynamics simulations of the mononuclear zinc-beta-lactamase from Bacillus cereus complexed with benzylpenicillin and a quantum chemical study of the reaction mechanism

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311373200

Molecular dynamics simulations of the dinuclear zinc-beta-lactamase from Bacteroides fragilis complexed with imipenem

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311373200

Substrate binding to mononuclear metallo-beta-lactamase from Bacillus cereus

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311373200

On the mechanism of the metallo-beta-lactamase from Bacteroides fragilis

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311373200

Analysis of the importance of the metallo-beta-lactamase active site loop in substrate binding and catalysis

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311373200

Novel mechanism of hydrolysis of therapeutic beta-lactams by Stenotrophomonas maltophilia L1 metallo-beta-lactamase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311373200

Cryoenzymology of Bacillus cereus beta-lactamase II.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311373200

Program DYNAFIT for the analysis of enzyme kinetic data: application to HIV proteinase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311373200

Approach to inhibition kinetics. Measurement of enzyme-substrate complexes by electronic energy transfer

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311373200

Comparison of beta-lactamase II from Bacillus cereus 569/H/9 with a beta-lactamase from Bacillus cereus 5/B/6

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311373200

Mutational analysis of the two zinc-binding sites of the Bacillus cereus 569/H/9 metallo-beta-lactamase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311373200

Active-site mutants of class B beta-lactamases: substrate binding and mechanistic study

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311373200

Intermediate in beta-lactam hydrolysis catalyzed by a dinuclear zinc(II) complex: relevance to the mechanism of metallo-beta-lactamase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311373200

Probing substrate binding to metallo-beta-lactamase L1 from Stenotrophomonas maltophilia by using site-directed mutagenesis

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311373200

Carboxypeptidase A. Differences in the mechanisms of ester and peptide hydrolysis

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311373200

Kinetic and microcalorimetric analysis of substrate and cofactor interactions in epoxyalkane:CoM transferase, a zinc-dependent epoxidase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311373200

Substrate-activated zinc binding of metallo-beta -lactamases: physiological importance of mononuclear enzymes.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311373200

Methanolysis of nitrocefin catalyzed by one and two Zn(2+) ions. A simplified model for class B beta-lactamases

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311373200

21 January 2018

Identifiers

DOI

10.1074/JBC.M311373200

1 reference

7 December 2017

1 reference

PubMed ID

15140877