Kinetic Control of Thiamin Diphosphate Activation in Enzymes Studied by Proton−Nitrogen Correlated NMR Spectroscopy-Reference-Cited by-同舟云学术

Kinetic Control of Thiamin Diphosphate Activation in Enzymes Studied by Proton−Nitrogen Correlated NMR Spectroscopy

Published:2005-05-26 Issue:24 Volume:44 Page:8697-8700
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Tittmann Kai¹,Neef Holger¹,Golbik Ralph¹,Hübner Gerhard¹,Kern Dorothee¹

Affiliation:

1. Institut für Biochemie, Fachbereich Biochemie/Biotechnologie, Martin-Luther-Universität Halle-Wittenberg, Kurt-Mothes-Strasse 3, D-06120 Halle, Germany, and Department of Biochemistry, Brandeis University, 415 South Street, Waltham, Massachusetts 02454

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi050522x

Reference20 articles.

1. How Thiamine Diphosphate Is Activated in Enzymes

2. The Replacement of Trp392 by Alanine Influences the Decarboxylase/Carboligase Activity and Stability of Pyruvate Decarboxylase from Zymomonas mobilis

3. Analysis of an invariant cofactor-protein interaction in thiamin diphosphate-dependent enzymes by site-directed mutagenesis. Glutamic acid 418 in transketolase is essential for catalysis.

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