Allosteric properties of inosine monophosphate dehydrogenase revealed through the thermodynamics of binding of inosine 5'-monophosphate and mycophenolic acid. Temperature dependent heat capacity of binding as a signature of ligand-coupled conformational equilibria

Biochemistry

Volumn 36, Issue 34, 1997, Pages 10428-10438

  Bruzzese, Frank J ^a   Connelly, Patrick R ^a,b  

^a VERTEX PHARMACEUTICALS   (United States)

^b Connelly Scientific ^*  (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME INHIBITOR; INOSINATE DEHYDROGENASE; INOSINE PHOSPHATE; LIGAND; MYCOPHENOLIC ACID;

ARTICLE; BINDING AFFINITY; CONFORMATIONAL TRANSITION; ENTHALPY; ENTROPY; ENZYME ACTIVITY; HEAT; IMMUNOSUPPRESSIVE TREATMENT; MICROCALORIMETRY; MODEL; NONHUMAN; PRIORITY JOURNAL; TEMPERATURE DEPENDENCE; THERMODYNAMICS;

ALLOSTERIC REGULATION; ANIMALS; CALORIMETRY; CRICETINAE; DRUG DESIGN; IMP DEHYDROGENASE; INOSINE MONOPHOSPHATE; LIGANDS; MYCOPHENOLIC ACID; PROTEIN BINDING; PROTEIN CONFORMATION; TEMPERATURE; THERMODYNAMICS;

EID: 0030868374     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9708040     Document Type: Article

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