Small-Angle X-ray Solution-Scattering Studies on Ligand-Induced Subunit Interactions of the Thiamine Diphosphate Dependent Enzyme Pyruvate Decarboxylase from Different Organisms-Reference-Cited by-同舟云学术

Small-Angle X-ray Solution-Scattering Studies on Ligand-Induced Subunit Interactions of the Thiamine Diphosphate Dependent Enzyme Pyruvate Decarboxylase from Different Organisms

Published:1998-03-24 Issue:15 Volume:37 Page:5329-5334
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

König Stephan¹,Svergun Dmitri I.¹,Volkov Vladimir V.¹,Feigin Lev A.¹,Koch Michel H. J.¹

Affiliation:

1. Fachbereich Biochemie/Biotechnologie, Institut für Biochemie, Martin-Luther-Univerität HalleWittenberg, Halle/Saale, Germany, European Molecular Biology Laboratory (EMBL c/o DESY), Hamburg Outstation, Germany, and Institute of Crystallography, Russian Academy of Sciences, Moscow, Russia

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi972125v

Reference34 articles.

1. The influence of the effectors of yeast pyruvate decarboxylase (PDC) on the conformation of the dimers and tetramers and their pH-dependent equilibrium

2. Crystal Structure of the Thiamin Diphosphate-dependent Enzyme Pyruvate Decarboxylase from the YeastSaccharomyces cerevisiaeat 2.3 Å Resolution

3. A thiamin diphosphate binding fold revealed by comparison of the crystal structures of transketolase, pyruvate oxidase and pyruvate decarboxylase

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