Inhibition of carboxypeptidase A by N-(4-t-butylbenzoyl)-2-hydroxy-1-naphthaldehyde hydrazone

Bioorganic and Medicinal Chemistry Letters

Volumn 7, Issue 12, 1997, Pages 1557-1562

  Lanthier, Christopher M ^a   Parniak, Michael A ^b   Dmitrienko, Gary I ^a  

^a UNIVERSITY OF WATERLOO   (Canada)

^b MCGILL UNIVERSITY   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

CARBOXYPEPTIDASE A; HYDRAZONE DERIVATIVE; PHENYLALANINE;

ARTICLE; BINDING SITE; ENZYME BINDING; ENZYME INHIBITION; IN VITRO STUDY; MOLECULAR MODEL; THERMODYNAMICS; ULTRAVIOLET SPECTROPHOTOMETRY; X RAY CRYSTALLOGRAPHY;

EID: 0030927294     PISSN: 0960894X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-894X(97)00267-9     Document Type: Article

References (27)

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16. +2 was assigned a charge of +2. The minimization involved Phe, 2 and residues within a 15 A radius around the active site and was conducted until the energy difference between iterations was less than 1 cal/mol.
17. +2 was assigned a charge of +2. The minimization involved Phe, 2 and residues within a 15 A radius around the active site and was conducted until the energy difference between iterations was less than 1 cal/mol.
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21. Kinetic data were analyzed using the software package Grafit 3.01® (©Erithacus Software Ltd.)
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27. a was determined spectrophotometrically (Albert, A; Sargeant, E. P. The Determination of Ionization Constants, 3rd ed; Chapman and Hall: New York, 1984; pp 70-101). Molecular modeling with the ionized form of 2 yielded a structure qualitatively very similar to the complex of non-ionized 2 with CPA which is described above.