Glutamate 270 plays an essential role in K+-activation and domain closure of Thermus thermophilus isopropylmalate dehydrogenase

FEBS Letters

Volumn 589, Issue 2, 2015, Pages 240-245

  Gráczer, Éva ^a   Palló, Anna ^a,f,g,h   Oláh, Julianna ^b   Szimler, Tamás ^a   Konarev, Petr V ^c,i   Svergun, Dmitri I ^c   Merli, Angelo ^d   Závodszky, Péter ^a   Weiss, Manfred S ^e   Vas, Mária ^a  

^a INSTITUTE OF EXPERIMENTAL MEDICINE   (Hungary)

^b BUDAPEST UNIVERSITY OF TECHNOLOGY AND ECONOMICS   (Hungary)

^c EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

^d UNIVERSITY OF PARMA   (Italy)

^e HAHN MEITNER INSTITUT   (Germany)

^f DEPARTMENT OF PLANT SYSTEMS BIOLOGY   (Belgium)

^g Brussels Center for Redox Biology   (Belgium)

^h VRIJE UNIVERSITEIT BRUSSEL   (Belgium)

ⁱ SHUBNIKOV INSTITUTE OF CRYSTALLOGRAPHY   (Russian Federation)

Author keywords

Activation by K+; Fluorescence resonance energy transfer; Isopropylmalate dehydrogenase; Site directed mutagenesis; Small angle X ray scattering; X ray crystallography

Indexed keywords

3 ISOPROPYLMALATE DEHYDROGENASE; GLUTAMIC ACID; NICOTINAMIDE ADENINE DINUCLEOTIDE; POTASSIUM ION;

ARTICLE; CATALYSIS; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME CONFORMATION; GENE MUTATION; MUTANT; NONHUMAN; PROTEIN DOMAIN; THERMUS THERMOPHILUS; WILD TYPE; CHEMICAL STRUCTURE; CHEMISTRY; ENZYMOLOGY; GENETICS; KINETICS; METABOLISM; MUTATION; PROTEIN TERTIARY STRUCTURE;

THERMUS THERMOPHILUS;

3-ISOPROPYLMALATE DEHYDROGENASE; ENZYME ACTIVATION; GLUTAMIC ACID; KINETICS; MODELS, MOLECULAR; MUTATION; PROTEIN STRUCTURE, TERTIARY; THERMUS THERMOPHILUS;

EID: 84920734436     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2014.12.005     Document Type: Article

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