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Disclosing New Inhibitors by Finding Similarities in Three‐Dimensional Active‐Site Architectures of Polynuclear Zinc Phospholipases and Aminopeptidases
Author(s) -
GonzálezRoura Albert,
Navarro Isabel,
Delgado Antonio,
Llebaria Amadeu,
Casas Josefina
Publication year - 2004
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200352241
Subject(s) - active site , aminopeptidase , phospholipase , enzyme , zinc , identification (biology) , biochemistry , sequence (biology) , hydrolase , phospholipase a2 , chemistry , stereochemistry , biology , amino acid , organic chemistry , leucine , botany
Shaping up for inhibition : Identification of three‐dimensional structural similarities (see picture) between the active sites of zinc dinuclear aminopeptidases and trinuclear phospholipase C hydrolytic enzymes that are not related by sequence or tertiary structure led to the discovery of phospholipase C inhibition by α‐aminohydroxamic acids, a typical family of aminopeptidase inhibitors.