The Cys319 Loop modulates the transition between dehydrogenase and hydrolase conformations in inosine 5′-monophosphate dehydrogenase

Biochemistry

Volumn 49, Issue 50, 2010, Pages 10674-10681

  Josephine, Helen R ^a   Ravichandran, Kanchana R ^a,b   Hedstrom, Lizbeth ^a  

^a BRANDEIS UNIVERSITY   (United States)

^b MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYTIC CYCLES; CONFORMATION CHANGE; CONFORMATIONAL CHANGE; ENZYME-LIGAND COMPLEX; HYDRIDE TRANSFERS; HYDROLASES; INHIBITOR COMPLEX; INOSINE; MICROSCOPIC RATE CONSTANTS; MINIMAL EFFECTS; MONOPHOSPHATES; X RAY CRYSTAL STRUCTURES;

COMPLEXATION; ENZYMES; EQUILIBRIUM CONSTANTS; RATE CONSTANTS;

CONFORMATIONS;

ALANINE; ARGININE; CYSTEINE; GLUTAMIC ACID; GLUTAMINE; HYDROLASE; INOSINATE DEHYDROGENASE; OXIDOREDUCTASE;

AMINO ACID SUBSTITUTION; ARTICLE; CRYSTAL STRUCTURE; ENZYME CONFORMATION; ENZYME MECHANISM; ENZYME STRUCTURE; EQUILIBRIUM CONSTANT; HYDROLYSIS; NONHUMAN; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS;

CRYSTALLOGRAPHY, X-RAY; HYDROLASES; IMP DEHYDROGENASE; OXIDOREDUCTASES; PROTEIN STRUCTURE, SECONDARY; TRITRICHOMONAS FOETUS;

TRITRICHOMONAS FOETUS;

EID: 78650323744     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi101590c     Document Type: Article

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