Two inhibitor molecules bound in the active site of Pseudomonas sedolisin: a model for the bi-product complex following cleavage of a peptide substrate-Reference-Cited by-同舟云学术

Two inhibitor molecules bound in the active site of Pseudomonas sedolisin: a model for the bi-product complex following cleavage of a peptide substrate

Published:2004-02 Issue:2 Volume:314 Page:638-645
ISSN:0006-291X
Container-title:Biochemical and Biophysical Research Communications
language:en
Short-container-title:Biochemical and Biophysical Research Communications

Author:

Wlodawer Alexander,Li Mi,Gustchina Alla,Oyama Hiroshi,Oda Kohei,Beyer Bret B,Clemente Jose,Dunn Ben M

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry,Biophysics

Reference24 articles.

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2. Carboxyl proteinase from Pseudomonas defines a novel family of subtilisin-like enzymes;Wlodawer;Nat. Struct. Biol.,2001

3. Inhibitor complexes of the Pseudomonas serine-carboxyl proteinase;Wlodawer;Biochemistry,2001

4. The 1.4Å crystal structure of kumamolysin: a thermostable serine-carboxyl-type proteinase;Comellas-Bigler;Structure,2002

5. Structural and enzymatic properties of the sedolisin family of serine-carboxyl peptidases;Wlodawer;Acta Biochim. Pol.,2003

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1. Serine-Carboxyl Peptidases, Sedolisins: From Discovery to Evolution;Biochemistry;2022-07-21

2. QM/MM and free-energy simulations of deacylation reaction catalysed by sedolisin, a serine-carboxyl peptidase;Molecular Simulation;2013-03

3. Sedolisin;Handbook of Proteolytic Enzymes;2013

4. Narrowing the gap in understanding protein structure and function through computer simulations;AIP Conference Proceedings;2012

5. New families of carboxyl peptidases: serine-carboxyl peptidases and glutamic peptidases;Journal of Biochemistry;2011-10-19