Disclosing New Inhibitors by Finding Similarities in Three‐Dimensional Active‐Site Architectures of Polynuclear Zinc Phospholipases and Aminopeptidases | Zendy

GonzálezRoura Albert | Zendy; Navarro Isabel | Zendy; Delgado Antonio | Zendy; Llebaria Amadeu | Zendy; Casas Josefina | Zendy

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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.

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