Probing the origin of the compromised catalysis of E. coli alkaline phosphatase in its promiscuous sulfatase reaction.
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Comparative Enzymology in the Alkaline Phosphatase Superfamily to Determine the Catalytic Role of an Active-Site Metal IonGround state destabilization by anionic nucleophiles contributes to the activity of phosphoryl transfer enzymesSpectroscopic studies on the [4Fe-4S] cluster in adenosine 5'-phosphosulfate reductase from Mycobacterium tuberculosis.Active site detection by spatial conformity and electrostatic analysis--unravelling a proteolytic function in shrimp alkaline phosphatase.Resolving apparent conflicts between theoretical and experimental models of phosphate monoester hydrolysisGeometric and electrostatic study of the [4Fe-4S] cluster of adenosine-5'-phosphosulfate reductase from broken symmetry density functional calculations and extended X-ray absorption fine structure spectroscopy.Promiscuity in the Enzymatic Catalysis of Phosphate and Sulfate Transfer.Cohesion group approach for evolutionary analysis of TyrA, a protein family with wide-ranging substrate specificities.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.Experimental analyses of the chemical dynamics of ribozyme catalysisWhy nature really chose phosphate.Kinetic isotope effects for alkaline phosphatase reactions: implications for the role of active-site metal ions in catalysis.Computational and biological evaluation of quinazolinone prodrug for targeting pancreatic cancer.Modeling catalytic promiscuity in the alkaline phosphatase superfamily.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.Exploring the tunable excitation of QDs to maximize the overlap with the absorber for inner filter effect-based phosphorescence sensing of alkaline phosphatase.Catalytic mechanism of the arylsulfatase promiscuous enzyme from Pseudomonas aeruginosa.A phosphoarginine containing peptide as an artificial SH2 ligand.
P2860
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P2860
Probing the origin of the compromised catalysis of E. coli alkaline phosphatase in its promiscuous sulfatase reaction.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
2007年论文
@zh
2007年论文
@zh-cn
name
Probing the origin of the comp ...... romiscuous sulfatase reaction.
@en
type
label
Probing the origin of the comp ...... romiscuous sulfatase reaction.
@en
prefLabel
Probing the origin of the comp ...... romiscuous sulfatase reaction.
@en
P2093
P2860
P50
P356
P1476
Probing the origin of the comp ...... romiscuous sulfatase reaction.
@en
P2093
Daniel Herschlag
Ivana Nikolic-Hughes
Jamie Purcell
Patrick J O'Brien
P2860
P304
P356
10.1021/JA069111+
P407
P577
2007-04-06T00:00:00Z