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On the mechanism of the metallo-β-lactamase from Bacteroides fragilis
Zhigang Wang
, Walter Fast
,
Stephen J. Benkovic
Chemistry
Research output
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Contribution to journal
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Article
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peer-review
202
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Keyphrases
Metallo-β-lactamase
100%
Zn(II)
75%
Anions
50%
Catalytic Mechanism
50%
Negatively Charged
50%
Dinuclear
50%
Nucleophile
50%
Nitrocefin
50%
Absorbance
25%
Stopped Flow
25%
Hydrolysis
25%
Active Sites
25%
Hydroxide
25%
Acyl
25%
Electrostatic Interaction
25%
Positively Charged
25%
Kinetic Mechanism
25%
Catalytic Reaction
25%
Amines
25%
Protonation
25%
Hydrolases
25%
Kinetic Parameters
25%
Leaving Group
25%
Flow Studies
25%
Anionic Species
25%
Rapid Scan
25%
Lactams
25%
Catalytic Cycle
25%
Hydrolysis Mechanism
25%
Single-wavelength
25%
Chemistry
Nucleophile
100%
Enzymatic Hydrolysis
100%
Catalytic Reaction
50%
Electrostatic Interaction
50%
Pharmacokinetics
50%
catalytic cycle
50%
Antibiotic Resistance
50%
protonation
50%
Lactam
50%
Biochemistry, Genetics and Molecular Biology
Enzyme
100%
Bacteroides fragilis
100%
Catalytic Mechanism
40%
Enzymatic Hydrolysis
40%
Active Site
20%
Kinetics
20%
Gene Linkage
20%
Protonation
20%
Hydrolase
20%
Static Electricity
20%
Catalysis
20%
Kinetic Parameter
20%
Antibiotic Resistance
20%
Material Science
Hydrolase
50%