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

被引:23
作者
Arolas, Joan L. [1 ]
Botelho, Tiago O. [1 ]
Vilcinskas, Andreas [2 ]
Xavier Gomis-Rueth, F. [1 ]
机构
[1] CSIC, Mol Biol Inst Barcelona, Proteolysis Lab, E-08028 Barcelona, Spain
[2] Univ Giessen, Inst Phytopathol & Angew Zool, D-35392 Giessen, Germany
关键词
enzymes; metallopeptidases; protein inhibitors; structure elucidation; thermolysin; METALLOPROTEINASE INHIBITOR; REACTIVE-SITE; THERMOLYSIN;
D O I
10.1002/anie.201103262
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
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 Asn56-Ile57 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). Copyright © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
引用
收藏
页码:10357 / 10360
页数:4
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