The interplay of electrostatic and binding interactions determining active centre chemistry and catalytic activity in actinidin and papain
- 1 January 1989
- journal article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 257 (1) , 309-310
- https://doi.org/10.1042/bj2570309
Abstract
No abstract availableThis publication has 16 references indexed in Scilit:
- Supracrystallographic resolution of interactions contributing to enzyme catalysis by use of natural structural variants and reactivity-probe kineticsBiochemical Journal, 1988
- Substrate-derived two-protonic-state electrophiles as sensitive kinetic specificity probes for cysteine proteinases. Activation of 2-pyridyl disulphides by hydrogen-bondingBiochemical Journal, 1987
- Chemical evidence for the pH-dependent control of ion-pair geometry in cathepsin B. Benzofuroxan as a reactivity probe sensitive to differences in the mutual disposition of the thiolate and imidazolium components of cysteine proteinase catalytic sitesBiochemical Journal, 1986
- Cloning and sequencing of papain-encoding cDNAGene, 1985
- Thiol proteasesJournal of Molecular Biology, 1985
- Effects of conformational selectivity and of overlapping kinetically influential ionizations on the characteristics of pH-dependent enzyme kinetics. Implications of free-enzyme pKa variability in reactions of papain for its catalytic mechanismBiochemical Journal, 1983
- Calculation of the electric potential in the active site cleft due to α-helix dipolesJournal of Molecular Biology, 1982
- Structure of actinidin, after refinement at 1.7 Å resolutionJournal of Molecular Biology, 1980
- Kinetics of papain-catalyzed hydrolysis of α-N-benzoyl-L-arginine-p-nitroanilideBiochemistry, 1973
- Ionization behavior of the catalytic carboxyls of lysozymeBiochemical and Biophysical Research Communications, 1970