Kinetic isotope effects for alkaline phosphatase reactions: implications for the role of active-site metal ions in catalysis.
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Biological phosphoryl-transfer reactions: understanding mechanism and catalysisArginine Coordination in Enzymatic Phosphoryl Transfer: Evaluation of the Effect of Arg166 Mutations in Escherichia coli Alkaline Phosphatase † ‡Substrate-Promoted Formation of a Catalytically Competent Binuclear Center and Regulation of Reactivity in a Glycerophosphodiesterase from Enterobacter aerogenesComparative Enzymology in the Alkaline Phosphatase Superfamily to Determine the Catalytic Role of an Active-Site Metal IonInsights into the Reaction of Protein-tyrosine Phosphatase 1B: CRYSTAL STRUCTURES FOR TRANSITION STATE ANALOGS OF BOTH CATALYTIC STEPSStructural and Mechanistic Insights into C-P Bond Hydrolysis by Phosphonoacetate HydrolaseQM/MM analysis suggests that Alkaline Phosphatase (AP) and nucleotide pyrophosphatase/phosphodiesterase slightly tighten the transition state for phosphate diester hydrolysis relative to solution: implication for catalytic promiscuity in the AP supePromiscuity in the Enzymatic Catalysis of Phosphate and Sulfate Transfer.Mechanistic study of protein phosphatase-1 (PP1), a catalytically promiscuous enzymeExperimental and computational analysis of the transition state for ribonuclease A-catalyzed RNA 2'-O-transphosphorylation.Stabilization of different types of transition states in a single enzyme active site: QM/MM analysis of enzymes in the alkaline phosphatase superfamily.Experimental analyses of the chemical dynamics of ribozyme catalysisKinetic isotope effects in the characterization of catalysis by protein tyrosine phosphatases.Mechanistic and Evolutionary Insights from Comparative Enzymology of Phosphomonoesterases and Phosphodiesterases across the Alkaline Phosphatase SuperfamilyProbing the origin of the compromised catalysis of E. coli alkaline phosphatase in its promiscuous sulfatase reaction.Altered transition state for the reaction of an RNA model catalyzed by a dinuclear zinc(II) catalyst.Probing the origins of catalytic discrimination between phosphate and sulfate monoester hydrolysis: comparative analysis of alkaline phosphatase and protein tyrosine phosphatases.Isotope-edited FTIR of alkaline phosphatase resolves paradoxical ligand binding properties and suggests a role for ground-state destabilization.Leaving Group Ability Observably Affects Transition State Structure in a Single Enzyme Active Site.Substrate and Transition State Binding in Alkaline Phosphatase Analyzed by Computation of Oxygen Isotope Effects.Phosphate ester analogues as probes for understanding enzyme catalysed phosphoryl transfer
P2860
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P2860
Kinetic isotope effects for alkaline phosphatase reactions: implications for the role of active-site metal ions in catalysis.
description
2007 nî lūn-bûn
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2007年の論文
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2007年学术文章
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2007年学术文章
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name
Kinetic isotope effects for al ...... -site metal ions in catalysis.
@en
type
label
Kinetic isotope effects for al ...... -site metal ions in catalysis.
@en
prefLabel
Kinetic isotope effects for al ...... -site metal ions in catalysis.
@en
P2093
P2860
P356
P1476
Kinetic isotope effects for al ...... -site metal ions in catalysis.
@en
P2093
Daniel Herschlag
Irina Catrina
Patrick J O'brien
Piotr K Grzyska
Rebecca Mitchell
P2860
P304
P356
10.1021/JA072196+
P407
P577
2007-07-14T00:00:00Z