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Structural Evidence for Standard‐Mechanism Inhibition in Metallopeptidases from a Complex Poised to Resynthesize a Peptide Bond
Author(s) -
Arolas Joan L.,
Botelho Tiago O.,
Vilcinskas Andreas,
GomisRüth F. Xavier
Publication year - 2011
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.201103262
Subject(s) - thermolysin , peptide bond , mechanism (biology) , peptide , chemistry , bond , stereochemistry , biochemistry , enzyme , philosophy , business , trypsin , epistemology , finance
It goes both ways : An unprecedented mechanism of metalloendopeptidase inhibition has been identified for the insect metalloproteinase inhibitor, which is both cleaved and rejoined at bond Asn56Ile57 by thermolysin under appropriate conditions. A two‐product complex is formed after hydrolysis and, simultaneously, a Michaelis complex is poised for synthesis of a peptide bond (see crystal structure).