The organophosphate-degrading enzyme from Agrobacterium radiobacter displays mechanistic flexibility for catalysis
about
Asymmetric zinc(II) complexes as functional and structural models for phosphoesterases.The role of Zn-OR and Zn-OH nucleophiles and the influence of para-substituents in the reactions of binuclear phosphatase mimetics.Product release is rate-limiting for catalytic processing by the Dengue virus proteaseCatalytic mechanisms for phosphotriesterasesSpectroscopic and mechanistic studies of dinuclear metallohydrolases and their biomimetic complexes.Use of magnetic circular dichroism to study dinuclear metallohydrolases and the corresponding biomimetics.Characterization of a highly efficient antibiotic-degrading metallo-β-lactamase obtained from an uncultured member of a permafrost community.Reaction mechanism of the metallohydrolase CpsB from Streptococcus pneumoniae, a promising target for novel antimicrobial agents.Engineering and introduction of de novo disulphide bridges in organophosphorus hydrolase enzyme for thermostability improvement.Ca(II) Binding Regulates and Dominates the Reactivity of a Transition-Metal-Ion-Dependent Diesterase from Mycobacterium tuberculosis.An efficient thermostable organophosphate hydrolase and its application in pesticide decontamination.Biochemical characterization of a new nicotinamidase from an unclassified bacterium thriving in a geothermal water stream microbial mat community.Identification and characterization of an unusual metallo-β-lactamase from Serratia proteamaculans.Trimethylphosphate and Dimethylphosphate Hydrolysis by Binuclear CdII , MnII , and ZnII -FeII Promiscuous Organophosphate-Degrading Enzyme: Reaction Mechanisms.AIM-1: An Antibiotic-Degrading Metallohydrolase That Displays Mechanistic Flexibility.Is CuII Coordinated to Patellamides inside Prochloron Cells?Determination of the catalytic activity of binuclear metallohydrolases using isothermal titration calorimetry.Metallohydrolase biomimetics with catalytic and structural flexibility.Triesterase and promiscuous diesterase activities of a di-Co(II)-containing organophosphate degrading enzyme reaction mechanisms.
P2860
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P2860
The organophosphate-degrading enzyme from Agrobacterium radiobacter displays mechanistic flexibility for catalysis
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2010 nî lūn-bûn
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2010 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի դեկտեմբերին հրատարակված գիտական հոդված
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2010年の論文
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2010年学术文章
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The organophosphate-degrading ...... stic flexibility for catalysis
@ast
The organophosphate-degrading ...... stic flexibility for catalysis
@en
The organophosphate-degrading ...... stic flexibility for catalysis
@nl
type
label
The organophosphate-degrading ...... stic flexibility for catalysis
@ast
The organophosphate-degrading ...... stic flexibility for catalysis
@en
The organophosphate-degrading ...... stic flexibility for catalysis
@nl
prefLabel
The organophosphate-degrading ...... stic flexibility for catalysis
@ast
The organophosphate-degrading ...... stic flexibility for catalysis
@en
The organophosphate-degrading ...... stic flexibility for catalysis
@nl
P2093
P2860
P50
P356
P1433
P1476
The organophosphate-degrading ...... stic flexibility for catalysis
@en
P2093
David L Ollis
Kieran S Hadler
Lawrence R Gahan
P2860
P304
P356
10.1042/BJ20101054
P407
P577
2010-12-01T00:00:00Z