The nature of interaction between the carboxylate of substrates and the guanidinium moiety of Arg-145 in carboxypeptidase a probed by inhibitors of the enzyme

Bioorganic and Medicinal Chemistry Letters

Volumn 6, Issue 24, 1996, Pages 2967-2970

  Kim, Dong H ^a   Park, Jeong Il ^a  

^a Pohang University of Science and Technology (POSTECH)   (South Korea)

Author keywords

[No Author keywords available]

Indexed keywords

2 BENZYL 2 FLUORO 3 HYDROXYPROPIONIC ACID; 2 BENZYL 3 HYDROXYPROPIONIC ACID; CARBOXYPEPTIDASE; ENZYME INHIBITOR; PROPIONIC ACID DERIVATIVE; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; DRUG SYNTHESIS; ENZYME BINDING; ENZYME INHIBITION; IN VITRO STUDY; PKA; STRUCTURE ACTIVITY RELATION;

EID: 0030591846     PISSN: 0960894X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-894X(96)00541-0     Document Type: Article

References (26)

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3. 2. Other important binding forces involved in the enzyme-ligand complex formation are interactions of the hydrophobic side chain of the C-terminal amino acid residue with the primary recognition pocket and the coordination of scissile carbonyl oxygen to the active site zinc ion.
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24. 1b
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