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

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

inferred from title

exact match

0 references

cites work

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

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

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28 September 2017

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

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Resisting resistance: new chemical strategies for battling superbugs

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Metallo-beta-lactamase: structure and mechanism

28 September 2017

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28 September 2017

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28 September 2017

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28 September 2017

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28 September 2017

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28 September 2017

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28 September 2017

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28 September 2017

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28 September 2017

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28 September 2017

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28 September 2017

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28 September 2017

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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

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30 May 2018

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

30 May 2018

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30 May 2018

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30 May 2018

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

28 November 2018

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

28 November 2018

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

28 November 2018

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

28 November 2018

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

28 November 2018

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12 December 2020

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

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12 December 2020

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

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12 December 2020

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

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12 December 2020

beta -Lactamases: which ones are clinically important?

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12 December 2020

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

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12 December 2020

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

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12 December 2020

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

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12 December 2020

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

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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

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12 December 2020