Enzyme Architecture: Amino Acid Side-Chains That Function To Optimize the Basicity of the Active Site Glutamate of Triosephosphate Isomerase

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Enzyme Architecture: Amino Acid Side-Chains That Function To Optimize the Basicity of the Active Site Glutamate of Triosephosphate Isomerase

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im Juli 2018 veröffentlichter wissenschaftlicher Artikel

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wetenschappelijk artikel

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наукова стаття, опублікована в липні 2018

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Enzyme Architecture: Amino Aci ...... e of Triosephosphate Isomerase

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Enzyme Architecture: Amino Aci ...... e of Triosephosphate Isomerase

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Enzyme Architecture: Amino Aci ...... e of Triosephosphate Isomerase

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Enzyme Architecture: Amino Aci ...... e of Triosephosphate Isomerase

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Enzyme Architecture: Amino Aci ...... e of Triosephosphate Isomerase

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Enzyme Architecture: Amino Aci ...... e of Triosephosphate Isomerase

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P1476

Enzyme Architecture: Amino Aci ...... e of Triosephosphate Isomerase

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P2093

M Merced Malabanan

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Tina L Amyes

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Optimal alignment for enzymatic proton transfer: structure of the Michaelis complex of triosephosphate isomerase at 1.2-A resolution.

Crystal structure of triosephosphate isomerase complexed with 2-phosphoglycolate at 0.83-A resolution

Functional role of the conserved active site proline of triosephosphate isomerase

Refined 1.83 A structure of trypanosomal triosephosphate isomerase crystallized in the presence of 2.4 M-ammonium sulphate. A comparison with the structure of the trypanosomal triosephosphate isomerase-glycerol-3-phosphate complex

Electrophilic catalysis in triosephosphate isomerase: the role of histidine-95

Crystallographic analysis of the complex between triosephosphate isomerase and 2-phosphoglycolate at 2.5-A resolution: implications for catalysis

Triosephosphate isomerase requires a positively charged active site: the role of lysine-12

The influence of pH on the interaction of inhibitors with triosephosphate isomerase and determination of the pKa of the active-site carboxyl group.

Hydron transfer catalyzed by triosephosphate isomerase. Products of isomerization of (R)-glyceraldehyde 3-phosphate in D2O.

Wildtype and engineered monomeric triosephosphate isomerase from Trypanosoma brucei: partitioning of reaction intermediates in D2O and activation by phosphite dianion.

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8277-8286

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scholarly article

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10.1021/JACS.8B04367

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English

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140

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John P. Richard

Christopher J Reinhardt

Xiang Zhai

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2018-07-05T00:00:00Z

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29862813

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catalysis

general chemistry

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6037162

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