Intramolecular Inhibition by Enzyme of Site-Specific Modification Reactions can Mask pKa Values Characteristic of the Reaction Pathway: Do the Side Chains of Aspartic Acid-158 and Lysine-156 of Papain Form an Ion-Pair?-Reference-Cited by-同舟云学术

Intramolecular Inhibition by Enzyme of Site-Specific Modification Reactions can Mask pKa Values Characteristic of the Reaction Pathway: Do the Side Chains of Aspartic Acid-158 and Lysine-156 of Papain Form an Ion-Pair?

Published:1978-02-01 Issue:1 Volume:6 Page:250-252
ISSN:0300-5127
Container-title:Biochemical Society Transactions
language:en
Short-container-title:

Author:

MALTHOUSE J. PAUL G.¹,BROCKLEHURST KEITH²

Affiliation:

1. 1Department of Biochemistry and Chemistry, St. Bartholomew's Hospital Medical College, University of London, Charterhouse Square, London EC1M 6BQ, U.K.

2. 2Department of Biochemistry and Chemistry, St. Bartholomew's Hospital Medical College, University of London, Charterhouse Square, London EC1M 6BQ, U.K.

Publisher

Portland Press Ltd.

Subject

Biochemistry

Link

https://portlandpress.com/biochemsoctrans/article-pdf/6/1/250/555870/bst0060250.pdf

Cited by 11 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. References;Enzyme Kinetics: Catalysis & Control;2010

2. Synthesis and biological activity of a squalenoid maleimide and other classes of squalene derivatives as irreversible inhibitors of 2,3-oxidosqualene cyclase;European Journal of Medicinal Chemistry;1994-01

3. The interplay of electrostatic fields and binding interactions determining catalytic-site reactivity in actinidin. A possible origin of differences in the behaviour of actinidin and papain;Biochemical Journal;1989-04-15

4. Chapter 2 Cysteine proteinases;Hydrolytic Enzymes;1987

5. [24] Two-protonic-state electrophiles as probes of enzyme mechanism;Methods in Enzymology;1982