(Q38325285)

2 September 2017

title

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

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2 September 2017

Paul-Soto R

1

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2 September 2017

Bauer R

2

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2 September 2017

Frère JM

3

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2 September 2017

Galleni M

4

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2 September 2017

Meyer-Klaucke W

5

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2 September 2017

Nolting H

6

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2 September 2017

Rossolini GM

7

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2 September 2017

de Seny D

8

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2 September 2017

Hernandez-Valladares M

9

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2 September 2017

Zeppezauer M

10

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2 September 2017

Adolph HW

11

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2 September 2017

language of work or name

English

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publication date

1 May 1999

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Journal of Biological Chemistry

2 September 2017

published in

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2 September 2017

volume

274

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2 September 2017

issue

19

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2 September 2017

page(s)

13242-13249

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Metallo-beta-lactamases--a new therapeutic challenge

2 September 2017

cites work

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.19.13242

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.274.19.13242

Characterization of the metal-binding sites of the beta-lactamase from Bacteroides fragilis

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.19.13242

Metal cofactor requirements of beta-lactamase II

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.19.13242

Histidine residues of zinc ligands in β-lactamase II

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.19.13242

A spectroscopic study of metal ion and ligand binding to beta-lactamase II.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.19.13242

Hyperexpression in Escherichia coli, purification, and characterization of the metallo-beta-lactamase of Bacillus cereus 5/B/6.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.19.13242

Mössbauer, electron-paramagnetic-resonance and X-ray-absorption fine-structure studies of the iron environment in recombinant human tyrosine hydroxylase.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.19.13242

Constrained and restrained refinement in EXAFS data analysis with curved wave theory

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.19.13242

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.274.19.13242

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.274.19.13242

New perspective on zinc biochemistry: cocatalytic sites in multi-zinc enzymes

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.19.13242

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.274.19.13242

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.19.13242

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.19.13242

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.19.13242

21 January 2018

Identifiers

DOI

10.1074/JBC.274.19.13242

1 reference

2 September 2017

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