Activation of R235A mutant orotidine 5'-monophosphate decarboxylase by the guanidinium cation: effective molarity of the cationic side chain of Arg-235
about
Ground state destabilization by anionic nucleophiles contributes to the activity of phosphoryl transfer enzymesSubstrate Distortion Contributes to the Catalysis of Orotidine 5′-Monophosphate DecarboxylaseEnzymatic Catalysis of Proton Transfer and Decarboxylation Reactions.Product deuterium isotope effects for orotidine 5'-monophosphate decarboxylase: effect of changing substrate and enzyme structure on the partitioning of the vinyl carbanion reaction intermediate.Rescue of K12G triosephosphate isomerase by ammonium cations: the reaction of an enzyme in pieces.On catalytic preorganization in oxyanion holes: highlighting the problems with the gas-phase modeling of oxyanion holes and illustrating the need for complete enzyme models.Modification of residue 42 of the active site loop with a lysine-mimetic side chain rescues isochorismate-pyruvate lyase activity in Pseudomonas aeruginosa PchB.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.Enzyme architecture: optimization of transition state stabilization from a cation-phosphodianion pair.Orotidine 5'-monophosphate decarboxylase: transition state stabilization from remote protein-phosphodianion interactions.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.The use of reaction timecourses to determine the level of minor contaminants in enzyme preparations.A role for flexible loops in enzyme catalysis.Enzyme activation through the utilization of intrinsic dianion binding energy.Enzyme Architecture: Self-Assembly of Enzyme and Substrate Pieces of Glycerol-3-Phosphate Dehydrogenase into a Robust Catalyst of Hydride Transfer.A reevaluation of the origin of the rate acceleration for enzyme-catalyzed hydride transfer.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.Primary Deuterium Kinetic Isotope Effects: A Probe for the Origin of the Rate Acceleration for Hydride Transfer Catalyzed by Glycerol-3-Phosphate Dehydrogenase
P2860
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P2860
Activation of R235A mutant orotidine 5'-monophosphate decarboxylase by the guanidinium cation: effective molarity of the cationic side chain of Arg-235
description
2010 nî lūn-bûn
@nan
2010 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Activation of R235A mutant oro ...... cationic side chain of Arg-235
@ast
Activation of R235A mutant oro ...... cationic side chain of Arg-235
@en
type
label
Activation of R235A mutant oro ...... cationic side chain of Arg-235
@ast
Activation of R235A mutant oro ...... cationic side chain of Arg-235
@en
prefLabel
Activation of R235A mutant oro ...... cationic side chain of Arg-235
@ast
Activation of R235A mutant oro ...... cationic side chain of Arg-235
@en
P2093
P2860
P356
P1433
P1476
Activation of R235A mutant oro ...... cationic side chain of Arg-235
@en
P2093
B McKay Wood
John A Gerlt
Shonoi A Barnett
Tina L Amyes
P2860
P304
P356
10.1021/BI902174Q
P407
P577
2010-02-01T00:00:00Z