Magnitude and origin of the enhanced basicity of the catalytic glutamate of triosephosphate isomerase
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Enzyme Architecture: The Effect of Replacement and Deletion Mutations of Loop 6 on Catalysis by Triosephosphate IsomeraseReflections on the catalytic power of a TIM-barrel.Triosephosphate isomerase I170V alters catalytic site, enhances stability and induces pathology in a Drosophila model of TPI deficiency.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.Role of Loop-Clamping Side Chains in Catalysis by Triosephosphate Isomerase.Enzyme Architecture: A Startling Role for Asn270 in Glycerol 3-Phosphate Dehydrogenase-Catalyzed Hydride TransferStructure-Function Studies of Hydrophobic Residues That Clamp a Basic Glutamate Side Chain during Catalysis by Triosephosphate IsomeraseStructural 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.Enzyme architecture: the activating oxydianion binding domain for orotidine 5'-monophophate decarboxylase.Mechanistic Imperatives for Deprotonation of Carbon Catalyzed by Triosephosphate Isomerase: Enzyme-Activation by Phosphite Dianion.Enzyme architecture: remarkably similar transition states for triosephosphate isomerase-catalyzed reactions of the whole substrate and the substrate in piecesEnzyme architecture: on the importance of being in a protein cage.Enzyme activation through the utilization of intrinsic dianion binding energy.Enzyme Architecture: Modeling the Operation of a Hydrophobic Clamp in Catalysis by Triosephosphate Isomerase.A reevaluation of the origin of the rate acceleration for enzyme-catalyzed hydride transfer.Enzyme 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
Magnitude and origin of the enhanced basicity of the catalytic glutamate of triosephosphate isomerase
description
2013 nî lūn-bûn
@nan
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
2013年论文
@zh
2013年论文
@zh-cn
name
Magnitude and origin of the en ...... e of triosephosphate isomerase
@en
type
label
Magnitude and origin of the en ...... e of triosephosphate isomerase
@en
prefLabel
Magnitude and origin of the en ...... e of triosephosphate isomerase
@en
P2093
P2860
P356
P1476
Magnitude and origin of the en ...... e of triosephosphate isomerase
@en
P2093
Lucia Nitsch-Velasquez
M Merced Malabanan
Tina L Amyes
P2860
P304
P356
10.1021/JA401504W
P407
P577
2013-04-10T00:00:00Z