Chemical modification of one carboxyl-group of papain abolishes the catalytic activity of the enzyme
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(74)80815-X/fullpdf
Reference11 articles.
1. Active Site of Papain and Covalent “High Energy” Bonds of Proteins
2. The structure and mechanism of action of papain
3. IV. Cysteine proteinases
4. Normal apparent pK a value for the ionization of the histidine residue of papain and stem bromelain as determined by photooxidation reaction
5. Ionization of a nitrophenol-containing reporter group at the active site of papain
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1. Protein immobilization to alumina supports: II. Papain immobilization to alumina via organophosphate linkers;Biotechnology and Bioengineering;1992-12-20
2. Importance of hydrogen-bonding interactions involving the side chain of Asp158 in the catalytic mechanism of papain;Biochemistry;1991-06-01
3. A protein engineering study of the role of aspartate 158 in the catalytic mechanism of papain;Biochemistry;1990-07
4. Isosteric and non-isosteric modification of car☐yl groups of papain;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1989-07
5. Chapter 2 Cysteine proteinases;Hydrolytic Enzymes;1987
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