(Q44426206)

2 December 2017

title

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

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2 December 2017

5

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1

Catherine Moali

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author name string

Catherine Moali

1

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2 December 2017

Christine Anne

2

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2 December 2017

Josette Lamotte-Brasseur

3

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2 December 2017

Sylvie Groslambert

4

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2 December 2017

Jozef Van Beeumen

6

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2 December 2017

Moreno Galleni

7

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2 December 2017

Jean Marie Frère

8

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2 December 2017

publication date

1 April 2003

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2 December 2017

published in

Chemistry and Biology

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2 December 2017

volume

10

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2 December 2017

issue

4

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2 December 2017

page(s)

319-329

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Some properties of two extracellular beta-lactamases from Bacillus cereus 569/H

2 December 2017

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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

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

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

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

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

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Kinetic properties and metal content of the metallo-beta-lactamase CcrA harboring selective amino acid substitutions

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

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Biochemical characterization of the Pseudomonas aeruginosa 101/1477 metallo-beta-lactamase IMP-1 produced by Escherichia coli.

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Crystal structure of the IMP-1 metallo beta-lactamase from Pseudomonas aeruginosa and its complex with a mercaptocarboxylate inhibitor: binding determinants of a potent, broad-spectrum inhibitor

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Functional analysis of the active site of a metallo-beta-lactamase proliferating in Japan

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Zn(II) Dependence of theAeromonas hydrophilaAE036 Metallo-β-lactamase Activity and Stability†

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Overexpression, purification, and characterization of the cloned metallo-beta-lactamase L1 from Stenotrophomonas maltophilia

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7 January 2021

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

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7 January 2021

Biochemical characterization of the FEZ-1 metallo-beta-lactamase of Legionella gormanii ATCC 33297T produced in Escherichia coli

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7 January 2021

X-ray structure of the ZnII beta-lactamase from Bacteroides fragilis in an orthorhombic crystal form

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7 January 2021

1.85 A resolution structure of the zinc (II) beta-lactamase from Bacillus cereus

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7 January 2021

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

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7 January 2021

The 3-D structure of a zinc metallo-beta-lactamase from Bacillus cereus reveals a new type of protein fold

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7 January 2021

Metallo-beta-lactamase: structure and mechanism

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Kinetic mechanism of metallo-beta-lactamase L1 from Stenotrophomonas maltophilia

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7 January 2021

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

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7 January 2021

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

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7 January 2021

Substrate binding and catalytic mechanism of class B beta-lactamases: a molecular modelling study

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7 January 2021

Standard numbering scheme for class B beta-lactamases

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7 January 2021

NMR characterization of the metallo-beta-lactamase from Bacteroides fragilis and its interaction with a tight-binding inhibitor: role of an active-site loop

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7 January 2021

Modeling of the metallo-beta-lactamase from B. fragilis: structural and dynamic effects of inhibitor binding.

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7 January 2021

Dynamics of the metallo-beta-lactamase from Bacteroides fragilis in the presence and absence of a tight-binding inhibitor

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7 January 2021

Thiomandelic acid, a broad spectrum inhibitor of zinc beta-lactamases: kinetic and spectroscopic studies

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7 January 2021

Cryoenzymology of Bacillus cereus beta-lactamase II.

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7 January 2021

Kinetic study of interaction between BRL 42715, beta-lactamases, and D-alanyl-D-alanine peptidases

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7 January 2021

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

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7 January 2021

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

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7 January 2021

On functional and structural heterogeneity of VIM-type metallo-beta-lactamases.

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7 January 2021

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

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7 January 2021

Automated analysis of enzyme inactivation phenomena. Application to beta-lactamases and DD-peptidases

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7 January 2021

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Identifiers

DOI

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2 December 2017

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