Thionesters as a probe for electrophilic catalysis in the serine protease mechanism.-Reference-Cited by-同舟云学术

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Thionesters as a probe for electrophilic catalysis in the serine protease mechanism.

Published:1983-01 Issue:1 Volume:258 Page:59-66
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Campbell P,Nashed N T,Lapinskas B A,Gurrieri J

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference85 articles.

1. Serine Proteases: Structure and Mechanism of Catalysis

2. Structure of crystalline α-chymotrypsin

3. Structure of crystalline α-chymotrypsin

4. Subtilisin. Stereochemical mechanism involving transition-state stabilization

5. X-ray crystallographic study of boronic acid adducts with subtilisin BPN' (Novo). A model for the catalytic transition state.

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2. metal ion (electrophilic) catalysis;Catalysis from A to Z;2020-04-18

3. Cysteinyl Proteinases and Their Selective Inactivation;Advances in Enzymology - and Related Areas of Molecular Biology;2006-11-22

4. Benzotriazole-Assisted Thioacylation;The Journal of Organic Chemistry;2005-08-26

5. The role of a β-proton transfer donor in the degradation of benzylpenicillin;Journal of Molecular Catalysis A: Chemical;2001-10

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