Side-chain interactions in the regulatory domain of human glutamate dehydrogenase determine basal activity and regulation

Journal of Neurochemistry

Volumn 133, Issue 1, 2015, Pages 73-82

  Mastorodemos, Vasileios ^a   Kanavouras, Konstantinos ^a   Sundaram, Shobana ^b   Providaki, Maria ^c   Petraki, Zoe ^a   Kokkinidis, Michael ^c   Zaganas, Ioannis ^a   Logothetis, Diomedes E ^b   Plaitakis, Andreas ^a  

^a UNIVERSITY OF CRETE   (Greece)

^b VIRGINIA COMMONWEALTH UNIVERSITY   (United States)

^c UNIVERSITY OF CRETE   (Greece)

Author keywords

allosteric regulation; circular dichroism; glutamate dehydrogenase; molecular dynamics simulation; molecular modeling; site directed mutagenesis

Indexed keywords

ARGININE; GLUTAMATE DEHYDROGENASE; GLUTAMIC ACID; MUTANT PROTEIN; RECOMBINANT PROTEIN; SERINE; GLUD1 PROTEIN, HUMAN; ISOENZYME;

ALLOSTERISM; AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; CATALYSIS; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME INACTIVATION; ENZYME REGULATION; ENZYME STRUCTURE; GENE MUTATION; MOLECULAR DYNAMICS; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL; REGULATORY DOMAIN; SIDE CHAIN INTERACTION; CHEMICAL STRUCTURE; CHEMISTRY; COMPUTER SIMULATION; GENETICS; HEAT; HUMAN; KINETICS; METABOLISM; MUTATION; PHYSIOLOGY; PROTEIN DENATURATION; SITE DIRECTED MUTAGENESIS;

MAMMALIA;

ALLOSTERIC REGULATION; AMINO ACID SUBSTITUTION; COMPUTER SIMULATION; GLUTAMATE DEHYDROGENASE; HOT TEMPERATURE; HUMANS; ISOENZYMES; KINETICS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; MUTATION; PROTEIN DENATURATION;

EID: 84924599163     PISSN: 00223042     EISSN: 14714159     Source Type: Journal    
DOI: 10.1111/jnc.13019     Document Type: Article

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