Enzymatic mechanisms for catalysis of enolization: ketosteroid isomerase.
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Testing electrostatic complementarity in enzyme catalysis: hydrogen bonding in the ketosteroid isomerase oxyanion holeFundamental challenges in mechanistic enzymology: progress toward understanding the rate enhancements of enzymesHydrogen Bond Coupling in the Ketosteroid Isomerase Active SiteAn aspartate and a water molecule mediate efficient acid-base catalysis in a tailored antibody pocketEvaluating the Catalytic Contribution from the Oxyanion Hole in Ketosteroid IsomeraseRescue of deleterious mutations by the compensatory Y30F mutation in ketosteroid isomeraseA Double-Hotdog with a New Trick: Structure and Mechanism of the trans -Acyltransferase Polyketide Synthase Enoyl-isomeraseUncovering the determinants of a highly perturbed tyrosine pKa in the active site of ketosteroid isomerase.Enzymatic catalysis of proton transfer at carbon: activation of triosephosphate isomerase by phosphite dianion.Using unnatural amino acids to probe the energetics of oxyanion hole hydrogen bonds in the ketosteroid isomerase active site.Kemp Eliminase Activity of Ketosteroid Isomerase.Proton affinity of the oxyanion hole in the active site of ketosteroid isomerase.Solvation response along the reaction coordinate in the active site of ketosteroid isomerase.Water in the active site of ketosteroid isomerase.Hydrogen bonding in the active site of ketosteroid isomerase: electronic inductive effects and hydrogen bond couplingExtreme electric fields power catalysis in the active site of ketosteroid isomeraseA Critical Test of the Electrostatic Contribution to Catalysis with Noncanonical Amino Acids in Ketosteroid IsomeraseTM6SF2 and MAC30, new enzyme homologs in sterol metabolism and common metabolic diseaseQuantum delocalization of protons in the hydrogen-bond network of an enzyme active site.Common enzymological experiments allow free energy profile determination.Determining the catalytic role of remote substrate binding interactions in ketosteroid isomerase.Direct measurement of the protein response to an electrostatic perturbation that mimics the catalytic cycle in ketosteroid isomeraseContribution of a low-barrier hydrogen bond to catalysis is not significant in ketosteroid isomerase.Site-specific measurement of water dynamics in the substrate pocket of ketosteroid isomerase using time-resolved vibrational spectroscopyAsymmetric approach toward chiral cyclohex-2-enones from anisoles via an enantioselective isomerization by a new chiral diamine catalystRole of Loop-Clamping Side Chains in Catalysis by Triosephosphate Isomerase.Short Hydrogen Bonds and Proton Delocalization in Green Fluorescent Protein (GFP)Ground state destabilization from a positioned general base in the ketosteroid isomerase active site.Thermodynamic framework for identifying free energy inventories of enzyme catalytic cycles.Experimental and computational mutagenesis to investigate the positioning of a general base within an enzyme active site.Catalytic efficiency of enzymes: a theoretical analysisSpecificity in transition state binding: the Pauling model revisited.(15)N and (1)H Solid-State NMR Investigation of a Canonical Low-Barrier Hydrogen-Bond Compound: 1,8-Bis(dimethylamino)naphthalene.Electric Fields and Enzyme Catalysis.Evaluation of the energetics of the concerted acid-base mechanism in enzymatic catalysis: the case of ketosteroid isomerase.Calculation of vibrational shifts of nitrile probes in the active site of ketosteroid isomerase upon ligand binding.Evaluating the potential for halogen bonding in the oxyanion hole of ketosteroid isomerase using unnatural amino acid mutagenesisHybrid quantum/classical molecular dynamics simulations of the proton transfer reactions catalyzed by ketosteroid isomerase: analysis of hydrogen bonding, conformational motions, and electrostatics.Electric Fields and Fast Protein Dynamics in Enzymes.Theoretical study of enzymatically catalyzed tautomerization of carbon acids in aqueous solution: quantum calculations and steered molecular dynamics simulations.
P2860
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P2860
Enzymatic mechanisms for catalysis of enolization: ketosteroid isomerase.
description
2004 nî lūn-bûn
@nan
2004 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
Enzymatic mechanisms for catalysis of enolization: ketosteroid isomerase.
@ast
Enzymatic mechanisms for catalysis of enolization: ketosteroid isomerase.
@en
Enzymatic mechanisms for catalysis of enolization: ketosteroid isomerase.
@nl
type
label
Enzymatic mechanisms for catalysis of enolization: ketosteroid isomerase.
@ast
Enzymatic mechanisms for catalysis of enolization: ketosteroid isomerase.
@en
Enzymatic mechanisms for catalysis of enolization: ketosteroid isomerase.
@nl
prefLabel
Enzymatic mechanisms for catalysis of enolization: ketosteroid isomerase.
@ast
Enzymatic mechanisms for catalysis of enolization: ketosteroid isomerase.
@en
Enzymatic mechanisms for catalysis of enolization: ketosteroid isomerase.
@nl
P1433
P1476
Enzymatic mechanisms for catalysis of enolization: ketosteroid isomerase.
@en
P2093
Ralph M Pollack
P304
P356
10.1016/J.BIOORG.2004.06.005
P577
2004-10-01T00:00:00Z