The active site and mechanism of action of bovine pancreatic ribonuclease. 7. The catalytic mechanism
- 1 October 1962
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 85 (1), 152-153
- https://doi.org/10.1042/bj0850152
Abstract
An hypothesis for the active site and mechanism of action of ribonuclease is presented. In the hydrolysis of cytidine 2[image],3[image]-phosphate a histidine in the acid form transfers a proton to the 2[image]-oxygen atom of the nucleotide and a proton from water (or an alcohol) is transferred to another histidine. In the cyclization of an ester of cytidine 3[image]-phosphate, such as ribo-nucleic acid, the function of these two histidines is reversed.This publication has 6 references indexed in Scilit:
- The active site and mechanism of action of bovine pancreatic ribonuclease. 4. The activity in inert organic solvents and alcoholsBiochemical Journal, 1962
- The active site and mechanism of action of bovine pancreatic ribonuclease. 6. Kinetic and spectrophotometric investigation of the interaction of the enzyme with inhibitors and p-nitrophenyl acetateBiochemical Journal, 1962
- The active site and mechanism of action of bovine pancreatic ribonuclease. 3. The pH-dependence of the kinetic parameters for the hydrolysis of cytidine 2′,3′-phosphateBiochemical Journal, 1962
- The Active Site and Mechanism of Action of Bovine Pancreatic RibonucleaseNature, 1961
- The preparation and purification of cytidine 2′:3′-phosphateBiochemical Journal, 1960
- Spectrophotometric assay of bovine pancreatic ribonuclease by the use of cytidine 2′:3′-phosphateBiochemical Journal, 1960