Catalytic role of the metal ion in the metallo-beta-lactamase GOB. (Q39541312)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:20007696%20AND%20SRC:MED&resulttype=core&format=json

15 January 2020

title

Catalytic role of the metal ion in the metallo-beta-lactamase GOB (English)

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15 January 2020

1

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15 January 2020

Lars Hemmingsen

series ordinal

2

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15 January 2020

author name string

Alejandro J Vila

series ordinal

3

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language of work or name

English

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publication date

10 December 2009

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Journal of Biological Chemistry

15 January 2020

published in

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15 January 2020

volume

285

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15 January 2020

issue

7

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15 January 2020

page(s)

4570-4577

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Common mechanistic features among metallo-beta-lactamases: a computational study of Aeromonas hydrophila CphA enzyme

15 January 2020

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

13 September 2017

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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

13 September 2017

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13 September 2017

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

13 September 2017

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13 September 2017

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13 September 2017

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13 September 2017

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

13 September 2017

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

13 September 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

13 September 2017

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13 September 2017

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13 September 2017

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13 September 2017

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13 September 2017

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14 September 2017

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14 September 2017

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14 September 2017

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25 September 2017

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25 September 2017

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17 June 2018

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The metallo-beta-lactamase GOB is a mono-Zn(II) enzyme with a novel active site.

17 June 2018

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21 August 2018

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Antibiotic recognition by binuclear metallo-beta-lactamases revealed by X-ray crystallography

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Hybrid QM/MM and DFT investigations of the catalytic mechanism and inhibition of the dinuclear zinc metallo-beta-lactamase CcrA from Bacteroides fragilis.

21 August 2018

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21 August 2018

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21 August 2018

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21 August 2018

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21 August 2018

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Cd-substituted horse liver alcohol dehydrogenase: catalytic site metal coordination geometry and protein conformation.

21 August 2018

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Metallo-β-lactamases: does it take two to tango?

21 August 2018

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Crossref

https://api.crossref.org/works/10.1074%2FJBC.M109.063743

Nuclear magnetic resonance of paramagnetic metalloproteins

21 January 2018

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Crossref

https://api.crossref.org/works/10.1074%2FJBC.M109.063743

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

21 January 2018

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12 December 2020

On the coordination of inhibitors to the metal ion of carboxypeptidase A. A 113Cd and 31P NMR study

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12 December 2020

Is it necessary to change the classification of {beta}-lactamases?

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12 December 2020

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

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12 December 2020

Mutational analysis of metallo-beta-lactamase CcrA from Bacteroides fragilis

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12 December 2020

Recent Advances in Zinc Enzymology

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12 December 2020

Metal content and localization during turnover in B. cereus metallo-beta-lactamase

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12 December 2020

Identifiers

DOI

10.1074/JBC.M109.063743

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:20007696%20AND%20SRC:MED&resulttype=core&format=json

15 January 2020

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:20007696%20AND%20SRC:MED&resulttype=core&format=json

15 January 2020

PubMed publication ID

20007696

1 reference