Degrees of difficulty of water-consuming reactions in the absence of enzymes.
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Uroporphyrinogen decarboxylation as a benchmark for the catalytic proficiency of enzymesDihydrofolate reductase as a model for studies of enzyme dynamics and catalysisAn efficient, multiply promiscuous hydrolase in the alkaline phosphatase superfamilyNerve agent hydrolysis activity designed into a human drug metabolism enzymeStructural Snapshots for Mechanism-Based Inactivation of a Glycoside Hydrolase by Cyclopropyl CarbasugarsStatistical Mechanics of Allosteric Enzymes.How the Same Core Catalytic Machinery Catalyzes 17 Different Reactions: the Serine-Histidine-Aspartate Catalytic Triad of α/β-Hydrolase Fold Enzymes.Hydrogen tunneling links protein dynamics to enzyme catalysisEnhancement of the rate of pyrophosphate hydrolysis by nonenzymatic catalysts and by inorganic pyrophosphatase.Impact of temperature on the time required for the establishment of primordial biochemistry, and for the evolution of enzymes.Quantitating the specificity and selectivity of Gcn5-mediated acetylation of histone H3.Role of dynamics in enzyme catalysis: substantial versus semantic controversies.Monoalkyl sulfates as alkylating agents in water, alkylsulfatase rate enhancements, and the "energy-rich" nature of sulfate half-esters.Hydrolysis of N-alkyl sulfamates and the catalytic efficiency of an S-N cleaving sulfamidase.Proton-in-flight mechanism for the spontaneous hydrolysis of N-methyl O-phenyl sulfamate: implications for the design of steroid sulfatase inhibitors.Catalysis by a de novo zinc-mediated protein interface: implications for natural enzyme evolution and rational enzyme engineering.Promiscuity in the Enzymatic Catalysis of Phosphate and Sulfate Transfer.Kinetic Detection of Orthogonal Protein and Chemical Coordinates in Enzyme Catalysis: Double Mutants of Soybean Lipoxygenase.Amide bond cleavage: acceleration due to a 1,3-diaxial interaction with a carboxylic acidComputation of kinetic isotope effects for enzymatic reactions.Cytosine deamination and the precipitous decline of spontaneous mutation during Earth's history.Constant enthalpy change value during pyrophosphate hydrolysis within the physiological limits of NaCl.Why nature really chose phosphate.Flexibility and reactivity in promiscuous enzymes.Linking protein motion to enzyme catalysis.The guanidinium unit in the catalysis of phosphoryl transfer reactions: from molecular spacers to nanostructured supports.Prediction of the maximum temperature for life based on the stability of metabolites to decomposition in water.Determination of concentration and activity of immobilized enzymes.Rates of spontaneous cleavage of glucose, fructose, sucrose, and trehalose in water, and the catalytic proficiencies of invertase and trehalas.The rate of spontaneous cleavage of the glycosidic bond of adenosine.Energy flows, metabolism and translation.DNA hydrolytic cleavage catalyzed by synthetic multinuclear metallonucleases.Guanidine-based polymer brushes grafted onto silica nanoparticles as efficient artificial phosphodiesterases.Structural and Mechanistic Analysis of the Choline Sulfatase from Sinorhizobium melliloti: A Class I Sulfatase Specific for an Alkyl Sulfate Ester.Simulating the reactions of substituted pyridinio-N-phosphonates with pyridine as a model for biological phosphoryl transfer.Catalytic promiscuity in Pseudomonas aeruginosa arylsulfatase as an example of chemistry-driven protein evolution.Role of Conformational Motions in Enzyme Function: Selected Methodologies and Case Studies.Ligand-Induced Variations in Structural and Dynamical Properties Within an Enzyme Superfamily.Fluorogenic structure activity library pinpoints molecular variations in substrate specificity of structurally homologous esterasesRevealing the mechanism for covalent inhibition of glycoside hydrolases by carbasugars at an atomic level
P2860
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P2860
Degrees of difficulty of water-consuming reactions in the absence of enzymes.
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
2006年论文
@zh
2006年论文
@zh-cn
name
Degrees of difficulty of water-consuming reactions in the absence of enzymes.
@ast
Degrees of difficulty of water-consuming reactions in the absence of enzymes.
@en
type
label
Degrees of difficulty of water-consuming reactions in the absence of enzymes.
@ast
Degrees of difficulty of water-consuming reactions in the absence of enzymes.
@en
prefLabel
Degrees of difficulty of water-consuming reactions in the absence of enzymes.
@ast
Degrees of difficulty of water-consuming reactions in the absence of enzymes.
@en
P356
P1433
P1476
Degrees of difficulty of water-consuming reactions in the absence of enzymes.
@en
P2093
Richard Wolfenden
P304
P356
10.1021/CR050311Y
P577
2006-08-01T00:00:00Z