Probing substrate binding to metallo-beta-lactamase L1 from Stenotrophomonas maltophilia by using site-directed mutagenesis (Q24802987)

2

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Gopal Periyannan

3

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Robert B Yates

4

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Michael W Crowder

describes a project that uses

5

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language of work or name

English

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publication date

2002

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published in

BMC Biochemistry

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volume

3

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issue

1

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page(s)

4

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site-directed mutagenesis

1 reference

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

inferred from title

cites work

1 reference

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

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Energetic, structural, and antimicrobial analyses of beta-lactam side chain recognition by beta-lactamases

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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

7 April 2017

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

7 April 2017

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

7 April 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

7 April 2017

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

7 April 2017

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

7 April 2017

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

7 April 2017

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How to measure and predict the molar absorption coefficient of a protein

7 April 2017

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Site-directed mutagenesis by overlap extension using the polymerase chain reaction

7 April 2017

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Enzyme catalysis: removing chemically 'essential' residues by site-directed mutagenesis.

7 April 2017

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New beta-lactamases in gram-negative bacteria: diversity and impact on the selection of antimicrobial therapy

28 September 2017

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The problem of a solvent exposable disulfide when preparing Co(II)-substituted metallo-beta-lactamase L1 from Stenotrophomonas maltophilia

28 September 2017

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Standard numbering scheme for class B beta-lactamases

28 September 2017

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beta-Lactamase epidemiology and the utility of established and novel beta-lactamase inhibitors

28 September 2017

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Resisting resistance: new chemical strategies for battling superbugs

28 September 2017

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Convenient test for screening metallo-beta-lactamase-producing gram-negative bacteria by using thiol compounds

28 September 2017

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How beta-lactamases have driven pharmaceutical drug discovery. From mechanistic knowledge to clinical circumvention

28 September 2017

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Class B beta-lactamases: the importance of being metallic.

28 September 2017

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Beta-lactamases and beta-lactamase inhibitors

28 September 2017

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Metallo-beta-lactamase: structure and mechanism

28 September 2017

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Carbapenem derivatives as potential inhibitors of various beta-lactamases, including class B metallo-beta-lactamases.

28 September 2017

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Mechanistic and clinical aspects of beta-lactam antibiotics and beta-lactamases.

28 September 2017

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Inhibition studies on the metallo-beta-lactamase L1 from Stenotrophomonas maltophilia

28 September 2017

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The beta-lactamase cycle: a tale of selective pressure and bacterial ingenuity

28 September 2017

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

28 September 2017

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Crystal structures of the cadmium- and mercury-substituted metallo-beta-lactamase from Bacteroides fragilis

28 September 2017

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Carbapenem-hydrolyzing beta-lactamases

28 September 2017

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Inhibition of metallo-beta-lactamases by a series of mercaptoacetic acid thiol ester derivatives

28 September 2017

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Metallo-beta-lactamases--a new therapeutic challenge

28 September 2017

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Critical hydrogen bonding by serine 235 for cephalosporinase activity of TEM-1 beta-lactamase

28 September 2017

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Interactions of biapenem with active-site serine and metallo-beta-lactamases

28 September 2017

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The structure of β-lactamases

28 September 2017

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Classification of beta-lactamases: groups 2c, 2d, 2e, 3, and 4.

28 September 2017

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Classification of beta-lactamases: groups 1, 2a, 2b, and 2b'.

28 September 2017

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Characterization of beta-lactamases

28 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=77373

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

28 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=77373

Metallo-beta-lactamases: a class apart.

30 May 2018

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Analysis of protein circular dichroism spectra for secondary structure using a simple matrix multiplication

30 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=77373

Infections caused by Pseudomonas maltophilia. Expanding clinical spectrum.

30 May 2018

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=77373

Purification, crystallization and preliminary X-ray analysis of Bacteroides fragilis Zn2+ beta-lactamase.

30 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=77373

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

28 November 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=77373

Molecular dynamics simulations of the mononuclear zinc-beta-lactamase from Bacillus cereus

28 November 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=77373

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

28 November 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=77373

Sequence analysis of the L1 metallo-beta-lactamase from Xanthomonas maltophilia

28 November 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=77373

On the importance of a methyl group in beta-lactamase evolution: free energy profiles and molecular modeling

28 November 2018

1 reference

12 December 2020

Structure-activity relationships of biphenyl tetrazoles as metallo-beta-lactamase inhibitors

1 reference

12 December 2020

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

1 reference

12 December 2020

Arabidopsis glyoxalase II contains a zinc/iron binuclear metal center that is essential for substrate binding and catalysis

1 reference

12 December 2020

beta -Lactamases: which ones are clinically important?

1 reference

12 December 2020

Elucidation of the role of arginine-244 in the turnover processes of class A beta-lactamases

1 reference

12 December 2020

Risk factors for epidemic Xanthomonas maltophilia infection/colonization in intensive care unit patients

1 reference

12 December 2020

Nosocomial infections due to Xanthomonas maltophilia (Pseudomonas maltophilia) in patients with cancer

1 reference

12 December 2020

Outer membrane permeability and beta-lactamase content in Pseudomonas maltophilia clinical isolates and laboratory mutants

1 reference

12 December 2020

Isolation and structure determination of two novel phenazines from a Streptomyces with inhibitory activity against metallo-enzymes, including metallo-beta-lactamase

1 reference

12 December 2020

Sequence analysis and enzyme kinetics of the L2 serine beta-lactamase from Stenotrophomonas maltophilia

1 reference

12 December 2020

Inhibition of metallo-beta-lactamases by a series of thiol ester derivatives of mercaptophenylacetic acid

1 reference

12 December 2020

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

1 reference

12 December 2020

Interaction between class B beta-lactamases and suicide substrates of active-site serine beta-lactamases

1 reference

12 December 2020

Dimensions Publication ID

Identifiers

DOI

10.1186/1471-2091-3-4

0 references

1 reference

https://scigraph.springernature.com/pub.10.1186/1471-2091-3-4