Glutamate 270 plays an essential role in K+-activation and domain closure ofThermus thermophilusisopropylmalate dehydrogenase-Reference-Cited by-同舟云学术

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Glutamate 270 plays an essential role in K+-activation and domain closure ofThermus thermophilusisopropylmalate dehydrogenase

Published:2014-12-10 Issue:2 Volume:589 Page:240-245
ISSN:0014-5793
Container-title:FEBS Letters
language:en
Short-container-title:

Author:

Gráczer Éva,Palló Anna,Oláh Julianna,Szimler Tamás,Konarev Petr V.,Svergun Dmitri I.,Merli Angelo,Závodszky Péter,Weiss Manfred S.,Vas Mária

Funder

OTKA

European Community’s Seventh Framework Programme

German Ministry of Education and Science

Publisher

Wiley

Subject

Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics

Reference20 articles.

1. Purification and characterization of recombinant 3-isopropylmalate dehydrogenases from Thermus thermophilus and other microorganisms;Hayashi-Iwasaki;Methods Enzymol.,2000

2. A lysine-tyrosine pair carries out acid-base chemistry in the metal ion-dependent pyridine dinucleotide-linked beta-hydroxyacid oxidative decarboxylases;Aktas;Biochemistry,2009

3. Cloning of beta-isopropylmalate dehydrogenase gene from Bacillus coagulans in Escherichia coli and purification and properties of the enzyme;Sekiguchi;Biochim. Biophys. Acta,1984

4. Purification, catalytic properties, and thermal stability of threo-Ds-3-isopropylmalate dehydrogenase coded by leuB gene from an extreme thermophile, Thermus thermophilus strain HB8;Yamada;J. Biochem. (Tokyo),1990

5. Substrate determinants of the course of tartrate dehydrogenase-catalyzed reactions;Serfozo;Biochemistry,1995

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3. Characterization of 3-isopropylmalate dehydrogenase from extremely halophilic archaeon Haloarcula japonica;Bioscience, Biotechnology, and Biochemistry;2021-07-02

4. Dynamic Description of the Catalytic Cycle of Malate Enzyme: Stereoselective Recognition of Substrate, Chemical Reaction, and Ligand Release;The Journal of Physical Chemistry B;2018-11-30

5. Determinants of dual substrate specificity revealed by the crystal structure of homoisocitrate dehydrogenase from Thermus thermophilus in complex with homoisocitrate·Mg2+·NADH;Biochemical and Biophysical Research Communications;2016-09

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