Hydroxamate based inhibitors of adenylyl cyclase. Part 2: The effect of cyclic linkers on P-site binding

Bioorganic and Medicinal Chemistry Letters

Volumn 12, Issue 21, 2002, Pages 3089-3092

  Levy, Daniel E ^a   Bao, Ming ^a   Tomlinson, James E ^a   Scarborough, Robert M ^a  

^a MILLENNIUM PHARMACEUTICALS INC   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENINE; ADENOSINE TRIPHOSPHATE; ADENYLATE CYCLASE; CYCLIC AMP; ENZYME INHIBITOR; HYDROXAMIC ACID DERIVATIVE; LINK PROTEIN; METAL ION; PURINE; PYROPHOSPHATE;

ARTICLE; BINDING AFFINITY; BINDING SITE; CATALYSIS; CONTROLLED STUDY; CYCLIZATION; DRUG STRUCTURE; ENTROPY; ENZYME ACTIVITY; ENZYME BINDING; ENZYME INHIBITION; ENZYME METABOLISM; ENZYME STRUCTURE; HUMAN; HUMAN CELL; SIGNAL TRANSDUCTION; STEREOCHEMISTRY; STRUCTURE ACTIVITY RELATION;

ADENYLATE CYCLASE; BINDING SITES; CELL LINE; CRYSTALLOGRAPHY, X-RAY; CYCLOPENTANES; ENZYME INHIBITORS; HUMANS; HYDROGEN BONDING; HYDROXAMIC ACIDS; INDICATORS AND REAGENTS; ISOENZYMES; KIDNEY; MAGNESIUM; PROTEIN CONFORMATION; RECEPTORS, PURINERGIC; STEREOISOMERISM; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 0037020720     PISSN: 0960894X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-894X(02)00654-6     Document Type: Article

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12. 2. Compounds were added to the mixture and the reaction was run for 30 min at 30°C. Terminated reactions were evaluated for the enzymatic product, cAMP, using a commercially available New England Nuclear flash plate system. The degree of inhibition was determined by comparing the measured cAMP concentrations to those measured in control reactions containing no compound.