Transition state structure of purine nucleoside phosphorylase and principles of atomic motion in enzymatic catalysis - Wikidata - wikimedia - TriplyDB

Transition state structure of purine nucleoside phosphorylase and principles of atomic motion in enzymatic catalysis

Transition state structure of purine nucleoside phosphorylase and principles of atomic motion in enzymatic catalysis

http://www.wikidata.org/entity/Q27629392

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Fungal trehalose phosphorylase: kinetic mechanism, pH-dependence of the reaction and some structural properties of the enzyme from Schizophyllum commune Alpha-retaining glucosyl transfer catalysed by trehalose phosphorylase from Schizophyllum commune: mechanistic evidence obtained from steady-state kinetic studies with substrate analogues and inhibitors Dynamic dissociating homo-oligomers and the control of protein function Transition state analogue discrimination by related purine nucleoside phosphorylases Acetogenesis and the Wood-Ljungdahl pathway of CO(2) fixation Binding isotope effects: boon and bane Insights into the mechanism of bovine CD38/NAD+glycohydrolase from the X-ray structures of its Michaelis complex and covalently-trapped intermediates Catalysis by hen egg-white lysozyme proceeds via a covalent intermediate Closed site complexes of adenine phosphoribosyltransferase from Giardia lamblia reveal a mechanism of ribosyl migration Structure of Escherichia coli 5'-methylthioadenosine/ S-adenosylhomocysteine nucleosidase inhibitor complexes provide insight into the conformational changes required for substrate binding and catalysis Structural and Kinetic Evidence for an Extended Hydrogen-bonding Network in Catalysis of Methyl Group Transfer: ROLE OF AN ACTIVE SITE ASPARAGINE RESIDUE IN ACTIVATION OF METHYL TRANSFER BY METHYLTRANSFERASES Structural basis for substrate specificity of Escherichia coli purine nucleoside phosphorylase Crystal structure and snapshots along the reaction pathway of a family 51 -L-arabinofuranosidase Neighboring Group Participation in the Transition State of Human Purine Nucleoside Phosphorylase †Conservation of structure and activity in Plasmodium purine nucleoside phosphorylases l -Enantiomers of Transition State Analogue Inhibitors Bound to Human Purine Nucleoside Phosphorylase A phosphoenzyme mimic, overlapping catalytic sites and reaction coordinate motion for human NAMPT Structure and reaction mechanism of human nicotinamide phosphoribosyltransferase Structural and Mechanistic Studies on Klebsiella pneumoniae 2-Oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline Decarboxylase The Crystal Structure of Streptococcus pyogenes Uridine Phosphorylase Reveals a Distinct Subfamily of Nucleoside Phosphorylases Catalytic site conformations in human PNP by 19F-NMR and crystallography.Structure of Salmonella typhimurium OMP Synthase in a Complete Substrate Complex Catalysis of methyl group transfers involving tetrahydrofolate and B(12)Structural analyses reveal two distinct families of nucleoside phosphorylases Xanthosine and xanthine Atomic detail of chemical transformation at the transition state of an enzymatic reaction.Enzymatic transition states and dynamic motion in barrier crossing.Loop-tryptophan human purine nucleoside phosphorylase reveals submillisecond protein dynamics.Ribocation transition state capture and rebound in human purine nucleoside phosphorylase.Four generations of transition-state analogues for human purine nucleoside phosphorylase.Pyrophosphate activation in hypoxanthine--guanine phosphoribosyltransferase with transition state analogue A synchrotron radiation study of the one-dimensional complex of sodium with (1S)-N-carboxylato-1-(9-deazaadenin-9-yl)-1,4-dideoxy-1,4-imino-D-ribitol, a member of the 'immucillin' family Sirtuin chemical mechanisms Design and directed evolution of a dideoxy purine nucleoside phosphorylase.Loop residues and catalysis in OMP synthase.Insights into the serine protease mechanism from atomic resolution structures of trypsin reaction intermediates.Description of local and global shape properties of protein helices.Direct measurement of the protein response to an electrostatic perturbation that mimics the catalytic cycle in ketosteroid isomerase Immucillins as antibiotics for T-cell proliferation and malaria.Mass Modulation of Protein Dynamics Associated with Barrier Crossing in Purine Nucleoside Phosphorylase.

P2860

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P2860

Transition state structure of purine nucleoside phosphorylase and principles of atomic motion in enzymatic catalysis

http://www.wikidata.org/entity/Q27629392

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2001 nî lūn-bûn

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2001 թուականի Յունուարին հրատարակուած գիտական յօդուած

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2001 թվականի հունվարին հրատարակված գիտական հոդված

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2001年の論文

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A Fedorov

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G J Gainsford

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853-860

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10.1021/BI002499F

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11170405

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