(Q39019943)

8 September 2017

1 reference

title

The mechanisms of catalysis by metallo beta-lactamases (English)

1 reference

8 September 2017

Michael I Page

1

0 references

author name string

Adriana Badarau

series ordinal

2

1 reference

8 September 2017

1 January 2008

1 reference

Bioinorganic Chemistry and Applications

8 September 2017

1 reference

8 September 2017

576297

1 reference

Creative Commons Attribution 3.0 Unported

8 September 2017

start time

1 January 2008

1 reference

April 2022 Public Data File from Crossref

copyright status

copyrighted

1 reference

April 2022 Public Data File from Crossref

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9 September 2017

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Over-expression, purification, and characterization of metallo-beta-lactamase ImiS from Aeromonas veronii bv. sobria

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14 September 2017

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17 June 2018

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Crystal Structure of Pseudomonas aeruginosa SPM-1 Provides Insights into Variable Zinc Affinity of Metallo-β-lactamases

17 June 2018

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21 August 2018

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A metallo-beta-lactamase enzyme in action: crystal structures of the monozinc carbapenemase CphA and its complex with biapenem

21 August 2018

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Role of Cys221 and Asn116 in the zinc-binding sites of the Aeromonas hydrophila metallo-beta-lactamase

21 August 2018

1 reference

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Metal binding Asp-120 in metallo-beta-lactamase L1 from Stenotrophomonas maltophilia plays a crucial role in catalysis.

21 August 2018

1 reference

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The inhibitor thiomandelic acid binds to both metal ions in metallo-beta-lactamase and induces positive cooperativity in metal binding

21 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2422870

Antibiotic prescription rates vary markedly between 13 European countries

21 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2422870

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

21 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2422870

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

21 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2422870

Dynamics of mononuclear cadmium beta-lactamase revealed by the combination of NMR and PAC spectroscopy

21 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2422870

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

21 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2422870

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

21 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2422870

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

21 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2422870

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

21 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2422870

The mechanism of catalysis and the inhibition of the Bacillus cereus zinc-dependent beta-lactamase

21 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2422870

Enzyme kinetics and biochemical analysis of ImiS, the metallo-beta-lactamase from Aeromonas sobria 163a.

21 August 2018

1 reference

Crossref

https://api.crossref.org/works/10.1155%2F2008%2F576297

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

21 January 2018

1 reference

12 December 2020

Production, purification and spectral properties of metal-dependent beta-lactamases of Bacillus cereus

1 reference

12 December 2020

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

1 reference

12 December 2020

Functional characterization of human carbonic anhydrase II variants with altered zinc binding sites

1 reference

12 December 2020

Metal ion binding and coordination geometry for wild type and mutants of metallo-beta -lactamase from Bacillus cereus 569/H/9 (BcII): a combined thermodynamic, kinetic, and spectroscopic approach

1 reference

12 December 2020

Evidence for a dinuclear active site in the metallo-beta-lactamase BcII with substoichiometric Co(II). A new model for metal uptake

1 reference

12 December 2020

Enzyme Deactivation Due to Metal-Ion Dissociation during Turnover of the Cobalt-β-Lactamase Catalyzed Hydrolysis of β-Lactams†

1 reference

12 December 2020

The Variation of Catalytic Efficiency ofBacilluscereusMetallo-β-lactamase with Different Active Site Metal Ions†

1 reference

12 December 2020

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

1 reference

12 December 2020

Identifiers

DOI

10.1155/2008/576297

1 reference

8 September 2017

1 reference

PMC publication ID

2422870

8 September 2017

PubMed publication ID

18551183

1 reference

PMC publication ID

2422870