Structural Evidence for Standard‐Mechanism Inhibition in Metallopeptidases from a Complex Poised to Resynthesize a Peptide Bond | Zendy

Arolas Joan L. | Zendy; Botelho Tiago O. | Zendy; Vilcinskas Andreas | Zendy; GomisRüth F. Xavier | Zendy

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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).

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