Comparative Enzymology in the Alkaline Phosphatase Superfamily to Determine the Catalytic Role of an Active-Site Metal Ion
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High-resolution analysis of Zn(2+) coordination in the alkaline phosphatase superfamily by EXAFS and x-ray crystallographyBiological phosphoryl-transfer reactions: understanding mechanism and catalysisComparative genomics of defense systems in archaea and bacteriaCoordination sphere of the third metal site is essential to the activity and metal selectivity of alkaline phosphatasesX-Ray Structure Reveals a New Class and Provides Insight into Evolution of Alkaline PhosphatasesStructural and Mechanistic Insights into C-P Bond Hydrolysis by Phosphonoacetate HydrolaseGround state destabilization by anionic nucleophiles contributes to the activity of phosphoryl transfer enzymesTungstate as a Transition State Analog for Catalysis by Alkaline PhosphataseIdentification and characterization of a novel phosphodiesterase from the metagenome of an Indian coalbedRepurposing Suzuki Coupling Reagents as a Directed Fragment Library Targeting Serine Hydrolases and Related EnzymesCellular function and molecular structure of ecto-nucleotidases.Active site detection by spatial conformity and electrostatic analysis--unravelling a proteolytic function in shrimp alkaline phosphatase.QM/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 supeResolving apparent conflicts between theoretical and experimental models of phosphate monoester hydrolysisDefense islands in bacterial and archaeal genomes and prediction of novel defense systemsSite-directed mutagenesis maps interactions that enhance cognate and limit promiscuous catalysis by an alkaline phosphatase superfamily phosphodiesterase.Extensive site-directed mutagenesis reveals interconnected functional units in the alkaline phosphatase active site.Cooperative Electrostatic Interactions Drive Functional Evolution in the Alkaline Phosphatase Superfamily.High-throughput analysis and protein engineering using microcapillary arrays.Promiscuity in the Enzymatic Catalysis of Phosphate and Sulfate Transfer.Tuned by metals: the TET peptidase activity is controlled by 3 metal binding sites.Stabilization of different types of transition states in a single enzyme active site: QM/MM analysis of enzymes in the alkaline phosphatase superfamily.Nucleases: diversity of structure, function and mechanism.Recombinant production and characterization of a highly active alkaline phosphatase from marine bacterium Cobetia marina.Evolutionary Genomics of Defense Systems in Archaea and Bacteria.Distinct metal ion requirements for the phosphomonoesterase and phosphodiesterase activities of calf intestinal alkaline phosphataseMonitoring the heat-induced structural changes of alkaline phosphatase by molecular modeling, fluorescence spectroscopy and inactivation kinetics investigationsMechanistic and Evolutionary Insights from Comparative Enzymology of Phosphomonoesterases and Phosphodiesterases across the Alkaline Phosphatase SuperfamilyFerrocene-Based Bioactive Bimetallic Thiourea Complexes: Synthesis and Spectroscopic Studies.Modeling catalytic promiscuity in the alkaline phosphatase superfamily.Divergence of chemical function in the alkaline phosphatase superfamily: structure and mechanism of the P-C bond cleaving enzyme phosphonoacetate hydrolase.Probing the origins of catalytic discrimination between phosphate and sulfate monoester hydrolysis: comparative analysis of alkaline phosphatase and protein tyrosine phosphatases.Chronic Cadmium Exposure Lead to Inhibition of Serum and Hepatic Alkaline Phosphatase Activity in Wistar Rats.Isotope-edited FTIR of alkaline phosphatase resolves paradoxical ligand binding properties and suggests a role for ground-state destabilization.Kinetic and computational evidence for an intermediate in the hydrolysis of sulfonate esters.QM/MM Analysis of Transition States and Transition State Analogues in Metalloenzymes.Leaving Group Ability Observably Affects Transition State Structure in a Single Enzyme Active Site.Differential catalytic promiscuity of the alkaline phosphatase superfamily bimetallo core reveals mechanistic features underlying enzyme evolution.
P2860
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P2860
Comparative Enzymology in the Alkaline Phosphatase Superfamily to Determine the Catalytic Role of an Active-Site Metal Ion
description
2008 nî lūn-bûn
@nan
2008 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2008年の論文
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2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
Comparative Enzymology in the ...... le of an Active-Site Metal Ion
@ast
Comparative Enzymology in the ...... le of an Active-Site Metal Ion
@en
Comparative Enzymology in the ...... le of an Active-Site Metal Ion
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type
label
Comparative Enzymology in the ...... le of an Active-Site Metal Ion
@ast
Comparative Enzymology in the ...... le of an Active-Site Metal Ion
@en
Comparative Enzymology in the ...... le of an Active-Site Metal Ion
@nl
prefLabel
Comparative Enzymology in the ...... le of an Active-Site Metal Ion
@ast
Comparative Enzymology in the ...... le of an Active-Site Metal Ion
@en
Comparative Enzymology in the ...... le of an Active-Site Metal Ion
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P2860
P3181
P1476
Comparative Enzymology in the ...... le of an Active-Site Metal Ion
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P2093
Timothy D Fenn
P2860
P304
P3181
P356
10.1016/J.JMB.2008.09.059
P407
P577
2008-12-31T00:00:00Z