Dissecting the total transition state stabilization provided by amino acid side chains at orotidine 5'-monophosphate decarboxylase: a two-part substrate approach.
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Uroporphyrinogen decarboxylation as a benchmark for the catalytic proficiency of enzymesMechanism of the Orotidine 5′-Monophosphate Decarboxylase-Catalyzed Reaction: Evidence for Substrate Destabilization ,Conformational Changes in Orotidine 5′-Monophosphate Decarboxylase: “Remote” Residues That Stabilize the Active ConformationMechanism of the Orotidine 5′-Monophosphate Decarboxylase-Catalyzed Reaction: Importance of Residues in the Orotate Binding SiteConformational Changes in Orotidine 5′-Monophosphate Decarboxylase: A Structure-Based Explanation for How the 5′-Phosphate Group Activates the EnzymeProton transfer from C-6 of uridine 5'-monophosphate catalyzed by orotidine 5'-monophosphate decarboxylase: formation and stability of a vinyl carbanion intermediate and the effect of a 5-fluoro substituentActivation of R235A mutant orotidine 5'-monophosphate decarboxylase by the guanidinium cation: effective molarity of the cationic side chain of Arg-235Product deuterium isotope effects for orotidine 5'-monophosphate decarboxylase: effect of changing substrate and enzyme structure on the partitioning of the vinyl carbanion reaction intermediate.Role of Lys-12 in catalysis by triosephosphate isomerase: a two-part substrate approach.Determination of the amino acid sequence requirements for catalysis by the highly proficient orotidine monophosphate decarboxylase.Enzyme architecture: deconstruction of the enzyme-activating phosphodianion interactions of orotidine 5'-monophosphate decarboxylase.The activating oxydianion binding domain for enzyme-catalyzed proton transfer, hydride transfer, and decarboxylation: specificity and enzyme architecture.Rate and Equilibrium Constants for an Enzyme Conformational Change during Catalysis by Orotidine 5'-Monophosphate DecarboxylaseOrotidine 5'-monophosphate decarboxylase: transition state stabilization from remote protein-phosphodianion interactions.Using catalytic atom maps to predict the catalytic functions present in enzyme active sites.Catalysis by orotidine 5'-monophosphate decarboxylase: effect of 5-fluoro and 4'-substituents on the decarboxylation of two-part substrates.Enzyme Architecture: A Startling Role for Asn270 in Glycerol 3-Phosphate Dehydrogenase-Catalyzed Hydride TransferStructural mutations that probe the interactions between the catalytic and dianion activation sites of triosephosphate isomerase.Role of a guanidinium cation-phosphodianion pair in stabilizing the vinyl carbanion intermediate of orotidine 5'-phosphate decarboxylase-catalyzed reactions.Orotic acid decarboxylation in water and nonpolar solvents: a potential role for desolvation in the action of OMP decarboxylase.An examination of the relationship between active site loop size and thermodynamic activation parameters for orotidine 5'-monophosphate decarboxylase from mesophilic and thermophilic organismsEnzyme architecture: the activating oxydianion binding domain for orotidine 5'-monophophate decarboxylase.The use of reaction timecourses to determine the level of minor contaminants in enzyme preparations.Mechanism of the orotidine 5'-monophosphate decarboxylase-catalyzed reaction: effect of solvent viscosity on kinetic constants.Primary Deuterium Kinetic Isotope Effects From Product Yields: Rationale, Implementation, and Interpretation.Orotidine 5'-Monophosphate Decarboxylase: Probing the Limits of the Possible for Enzyme Catalysis.
P2860
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P2860
Dissecting the total transition state stabilization provided by amino acid side chains at orotidine 5'-monophosphate decarboxylase: a two-part substrate approach.
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article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 04 July 2008
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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Dissecting the total transitio ...... a two-part substrate approach.
@en
Dissecting the total transitio ...... a two-part substrate approach.
@nl
type
label
Dissecting the total transitio ...... a two-part substrate approach.
@en
Dissecting the total transitio ...... a two-part substrate approach.
@nl
prefLabel
Dissecting the total transitio ...... a two-part substrate approach.
@en
Dissecting the total transitio ...... a two-part substrate approach.
@nl
P2093
P2860
P356
P1433
P1476
Dissecting the total transitio ...... a two-part substrate approach.
@en
P2093
Bryant M Wood
John A Gerlt
Shonoi A Barnett
Tina L Amyes
P2860
P304
P356
10.1021/BI800939K
P407
P577
2008-07-04T00:00:00Z