Stages of the formation of nonequivalence of active centers of transketolase from baker’s yeast-Reference-Cited by-同舟云学术

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Stages of the formation of nonequivalence of active centers of transketolase from baker’s yeast

Published:2019-04 Issue: Volume:466 Page:122-129
ISSN:2468-8231
Container-title:Molecular Catalysis
language:en
Short-container-title:Molecular Catalysis

Author:

Solovjeva Olga N.,Selivanov Vitaly A.^ORCID,Orlov Victor N.,Kochetov German A.

Publisher

Elsevier BV

Subject

Physical and Theoretical Chemistry,Process Chemistry and Technology,Catalysis

Reference43 articles.

1. Studies on thiamine diphosphate-dependent enzymes

2. Domain Relationships in Thiamine Diphosphate-Dependent Enzymes

3. Aspartate 155 of human transketolase is essential for thiamine diphosphate–magnesium binding, and cofactor binding is required for dimer formation

4. Structure, mechanism and catalytic duality of thiamine-dependent enzymes

Cited by 5 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. New Role of Water in Transketolase Catalysis;International Journal of Molecular Sciences;2023-01-20

2. Regulation of enzymes with identical subunits on the example of Transketolase;Open Journal of Analytical and Bioanalytical Chemistry;2022-03-07

3. The mechanism of a one-substrate transketolase reaction. Part II;Analytical Biochemistry;2021-01

4. Triosephosphate isomerase from baker’s yeast – ribozyme versus protein;Open Journal of Analytical and Bioanalytical Chemistry;2020-08-18

5. The Two-Species Model of transketolase explains donor substrate-binding, inhibition and heat-activation;Scientific Reports;2020-03-05

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