The time required for water attack at the phosphorus atom of simple phosphodiesters and of DNA - Wikidata - awgldk - TriplyDB

The time required for water attack at the phosphorus atom of simple phosphodiesters and of DNA

The time required for water attack at the phosphorus atom of simple phosphodiesters and of DNA

http://www.wikidata.org/entity/Q34572901

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DNA-catalyzed sequence-specific hydrolysis of DNA Biological phosphoryl-transfer reactions: understanding mechanism and catalysis Atomic details of near-transition state conformers for enzyme phosphoryl transfer revealed by Formula rather than by phosphoranes Human Flap Endonuclease Structures, DNA Double-Base Flipping, and a Unified Understanding of the FEN1 Superfamily Pursuing DNA catalysts for protein modification Chain and conformation stability of solid-state DNA: implications for room temperature storage Catalytic DNA with phosphatase activity Quantum mechanical analysis of nonenzymatic nucleotidyl transfer reactions: kinetic and thermodynamic effects of β-γ bridging groups of dNTP substrates The hydrolysis of phosphate diesters in cyclohexane and acetone Impact of temperature on the time required for the establishment of primordial biochemistry, and for the evolution of enzymes.Resolving apparent conflicts between theoretical and experimental models of phosphate monoester hydrolysis The energy landscape of adenylate kinase during catalysis.DNA as a versatile chemical component for catalysis, encoding, and stereocontrol Merely two mutations switch a DNA-hydrolyzing deoxyribozyme from heterobimetallic (Zn2+/Mn2+) to monometallic (Zn2+-only) behavior.Establishing broad generality of DNA catalysts for site-specific hydrolysis of single-stranded DNA A Bis(guanidinium)alcohol Attached to a Hairpin Polyamide: Synthesis, DNA Binding, and Plasmid Cleavage.Comparison of the catalytic parameters and reaction specificities of a phage and an archaeal flap endonuclease Promiscuity in the Enzymatic Catalysis of Phosphate and Sulfate Transfer.Probing enzyme phosphoester interactions by combining mutagenesis and chemical modification of phosphate ester oxygens.DNA catalysis of a normally disfavored RNA hydrolysis reaction.Orotic acid decarboxylation in water and nonpolar solvents: a potential role for desolvation in the action of OMP decarboxylase.An overview of chemical processes that damage cellular DNA: spontaneous hydrolysis, alkylation, and reactions with radicals.DNA-catalyzed hydrolysis of esters and aromatic amides.Excited state dynamics and catalytic mechanism of the light-driven enzyme protochlorophyllide oxidoreductase.The DNA and RNA sugar-phosphate backbone emerges as the key player. An overview of quantum-chemical, structural biology and simulation studies.Why nature really chose phosphate.Flexibility and reactivity in promiscuous enzymes.Generation and selection of ribozyme variants with potential application in protein engineering and synthetic biology.Nucleic acid catalysis: metals, nucleobases, and other cofactors.The cutting edges in DNA repair, licensing, and fidelity: DNA and RNA repair nucleases sculpt DNA to measure twice, cut once.Metallophosphoesterases: structural fidelity with functional promiscuity.Nucleic Acid Extraction from Synthetic Mars Analog Soils for in situ Life Detection.DNA Catalysis: The Chemical Repertoire of DNAzymes.Five water-soluble zwitterionic copper(II)-carboxylate polymers: role of dipyridyl coligands in enhancing the DNA-binding, cleaving and anticancer activities.Copper(II) and Zinc(II) Complexes of Conformationally Constrained Polyazamacrocycles as Efficient Catalysts for RNA Model Substrate Cleavage in Aqueous Solution at Physiological pH.Role of metal ions in catalysis by HIV integrase analyzed using a quantitative PCR disintegration assay.Functional identification of ligands for a catalytic metal ion in group I introns Stereochemistry and Mechanism of Enzymatic and Non-Enzymatic Hydrolysis of Benzylic sec-Sulfate Esters.Rates of spontaneous cleavage of glucose, fructose, sucrose, and trehalose in water, and the catalytic proficiencies of invertase and trehalas.Stronger and (now) longer synthetic collagen.

P2860

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P2860

The time required for water attack at the phosphorus atom of simple phosphodiesters and of DNA

http://www.wikidata.org/entity/Q34572901

description

2006 nî lūn-bûn

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2006 թուականի Մարտին հրատարակուած գիտական յօդուած

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2006 թվականի մարտին հրատարակված գիտական հոդված

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2006年の論文

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PNAS.0510879103

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Proceedings of the National Academy of Sciences of the United States of America

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P2093

Chetan Lad

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Gottfried K Schroeder

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Paul Wyman

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Richard Wolfenden

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P2860

A proficient enzyme

Some factors in the interpretation of protein denaturation

The rate of hydrolysis of phosphomonoester dianions and the exceptional catalytic proficiencies of protein and inositol phosphatases

The ionic hydrogen bond.

Kinetic and magnetic resonance studies of active-site mutants of staphylococcal nuclease: factors contributing to catalysis.

Staphylococcal nuclease: proposed mechanism of action based on structure of enzyme-thymidine 3',5'-bisphosphate-calcium ion complex at 1.5-A resolution.

Some Factors in the Interpretation of Protein Denaturation

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4052-4055

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10.1073/PNAS.0510879103

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11

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103

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Nicholas H Williams

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