The activating oxydianion binding domain for enzyme-catalyzed proton transfer, hydride transfer, and decarboxylation: specificity and enzyme architecture.
about
Enzyme architecture: optimization of transition state stabilization from a cation-phosphodianion pair.Rate and Equilibrium Constants for an Enzyme Conformational Change during Catalysis by Orotidine 5'-Monophosphate DecarboxylaseRole of Loop-Clamping Side Chains in Catalysis by Triosephosphate Isomerase.Enzyme Architecture: A Startling Role for Asn270 in Glycerol 3-Phosphate Dehydrogenase-Catalyzed Hydride TransferEnzyme activation through the utilization of intrinsic dianion binding energy.Enzyme Architecture: Modeling the Operation of a Hydrophobic Clamp in Catalysis by Triosephosphate Isomerase.Structure-Reactivity Effects on Intrinsic Primary Kinetic Isotope Effects for Hydride Transfer Catalyzed by Glycerol-3-phosphate Dehydrogenase.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.Enzyme Architecture: The Role of a Flexible Loop in Activation of Glycerol-3-phosphate Dehydrogenase for Catalysis of Hydride Transfer.Enzyme Architecture: Erection of Active Orotidine 5'-Monophosphate Decarboxylase by Substrate-Induced Conformational Changes.Orotidine 5'-Monophosphate Decarboxylase: Probing the Limits of the Possible for Enzyme Catalysis.Linking coupled motions and entropic effects to the catalytic activity of 2-deoxyribose-5-phosphate aldolase (DERA)† †Electronic supplementary information (ESI) available: Further experimental and computational data. See DOI: 10.1039/c5sc03666f.Primary Deuterium Kinetic Isotope Effects: A Probe for the Origin of the Rate Acceleration for Hydride Transfer Catalyzed by Glycerol-3-Phosphate DehydrogenaseEnzyme Architecture: Amino Acid Side-Chains That Function To Optimize the Basicity of the Active Site Glutamate of Triosephosphate Isomerase
P2860
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P2860
The activating oxydianion binding domain for enzyme-catalyzed proton transfer, hydride transfer, and decarboxylation: specificity and enzyme architecture.
description
2015 nî lūn-bûn
@nan
2015 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2015 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2015年の論文
@ja
2015年論文
@yue
2015年論文
@zh-hant
2015年論文
@zh-hk
2015年論文
@zh-mo
2015年論文
@zh-tw
2015年论文
@wuu
name
The activating oxydianion bind ...... icity and enzyme architecture.
@ast
The activating oxydianion bind ...... icity and enzyme architecture.
@en
type
label
The activating oxydianion bind ...... icity and enzyme architecture.
@ast
The activating oxydianion bind ...... icity and enzyme architecture.
@en
prefLabel
The activating oxydianion bind ...... icity and enzyme architecture.
@ast
The activating oxydianion bind ...... icity and enzyme architecture.
@en
P2860
P50
P356
P1476
The activating oxydianion bind ...... icity and enzyme architecture.
@en
P2093
Archie C Reyes
Tina L Amyes
P2860
P304
P356
10.1021/JA5123842
P407
P577
2015-01-20T00:00:00Z