Alternating Sites Reactivity Is a Common Feature of Thiamin Diphosphate-Dependent Enzymes As Evidenced by Isothermal Titration Calorimetry Studies of Substrate Binding-Reference-Cited by-同舟云学术

Alternating Sites Reactivity Is a Common Feature of Thiamin Diphosphate-Dependent Enzymes As Evidenced by Isothermal Titration Calorimetry Studies of Substrate Binding

Published:2013-04-01 Issue:15 Volume:52 Page:2505-2507
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Schröder-Tittmann Kathrin¹,Meyer Danilo¹,Arens Johannes¹,Wechsler Cindy¹,Tietzel Michael¹,Golbik Ralph²,Tittmann Kai¹

Affiliation:

1. Göttingen Center for Molecular Biosciences, Georg-August-University Göttingen, Ernst-Caspari-Haus, Justus-von-Liebig-Weg 11, 37077 Göttingen, Germany

2. Martin-Luther University Halle-Wittenberg, 06120 Halle/Salle, Germany

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi301591e

Reference26 articles.

1. Domain Relationships in Thiamine Diphosphate-Dependent Enzymes

2. Evolutionary Analysis of the TPP-Dependent Enzyme Family

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

4. Three-dimensional structure of transketolase, a thiamine diphosphate dependent enzyme, at 2.5 A resolution.

5. Three-dimensional structure of apotransketolase flexible loops at the active site enable cofactor binding

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