Crystallography and mutagenesis of transketolase: mechanistic implications for enzymatic thiamin catalysis
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics,Structural Biology
Reference42 articles.
1. Three-dimensional structure of transketolase, a thiamine diphosphate dependent enzyme, at 2.5 A resolution.
2. Refined Structure of Transketolase from Saccharomyces cerevisiae at 2·0 Å Resolution
3. Structure of the Thiamine- and Flavin-Dependent Enzyme Pyruvate Oxidase
4. Catalytic centers in the thiamin diphosphate dependent enzyme pyruvate decarboxylase at 2.4-.ANG. resolution
5. Thiamin diphosphate dependent enzymes: transketolase, pyruvate oxidase and pyruvate decarboxylase
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1. In Salmonella enterica, the pathogenicity island 2 (SPI‐2) regulator PagR regulates its own expression and the expression of a five‐gene operon that encodes transketolase C;Molecular Microbiology;2023-08-24
2. Ambient temperature structure of phosphoketolase from Bifidobacterium longum determined by serial femtosecond X-ray crystallography;Acta Crystallographica Section D Structural Biology;2023-03-28
3. New Role of Water in Transketolase Catalysis;International Journal of Molecular Sciences;2023-01-20
4. Regulation of enzymes with identical subunits on the example of Transketolase;Open Journal of Analytical and Bioanalytical Chemistry;2022-03-07
5. QM/MM Study of Human Transketolase: Thiamine Diphosphate Activation Mechanism and Complete Catalytic Cycle;Journal of Chemical Information and Modeling;2021-06-23
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