Bovine pancreatic ribonuclease: fifty years of the first enzymatic reaction mechanism.
نویسندگان
چکیده
Fifty years ago, the group of Tony Mathias and Bob Rabin at University College London deduced the first mechanism for catalysis by an enzyme, ribonuclease [Findlay, D., Herries, D. G., Mathias, A. P., Rabin, B. R., and Ross, C. A. (1961) Nature 190, 781-784]. Here, we celebrate this historic accomplishment by surveying knowledge of enzymology and protein science at that time, facts that led to the formulation of the mechanism, criticisms and alternative mechanisms, data that supported the proposed mechanism, and some of the refinements that have since provided a more precise picture of catalysis of RNA cleavage by ribonucleases. The Mathias and Rabin mechanism has appeared in numerous textbooks, monographs, and reviews and continues to have a profound impact on biochemistry.
منابع مشابه
Ribonuclease A: from Model System to Cancer Chemotherapeutic
Ribonuclease A has been the most studied enzyme of the twentieth century. Work on ribonuclease A has endowed enzymology, as well as protein science, with many paradigms. This work continues to provide a framework for understanding protein structure – function relationships in atomic detail. In addition, knowledge gained by basic research is enabling the rapid deployment of ribonuclease A homolo...
متن کاملThe Interaction of Metal Ions with Polynucleotides and Related Compounds XIII. THE EFFECT OF METAL IONS ON THE ENZYMATIC DEGRADATION OF RIBONUCLEIC ACID BY BOVINE PANCREATIC RIBONUCLEASE AND OF DEOXYRIBONUCLEIC ACID BY BOVINE PANCREATIC DEOXYRIBONUCLEASE
The activity of ribonuclease increases with increasing concentration of added divalent metal ions until the attainment of an optimal metal concentration, beyond which the addition of further metal ions inhibits the reaction. When either the optimal metal concentration or the enzymatic activity at that concentration is plotted versus the atomic number of the transition metals, the resulting curv...
متن کاملReaction of Bovine Pancreatic Ribonuclease a with 1,5-difluoro-2,4-dinitrobenzene. I. Preparation of Monomeric Intramolecularly Bridged Derivatives.
Bifunctional reagents have recently been used in several studies (l-4) concerned with the stereochemistry of proteins in solution. The objective was to link proximal pairs of functional groups of a protein molecule by means of bifunctional reagents in order to introduce artificial cross-links stable enough to withstand chemical and enzymatic degradative procedures. The expectation was that only...
متن کاملبررسی فعالیت مهارکننده ریبونوکلئاز جفتی بر روی آنزیم ریبونوکلئاز
Ribonuclease inhibitor is an acidic protein, soluble in cytoplasm. It is abundantly present in human placenta. It could be extracted from this organ to the extent of 1mg/placenta using chemical ion exchange and affinity techniques. Molecular weight of this protein is estimated by electophoresis or SDS-PAG electrophoresis using standards of known proteins. Molecular weight has been found to be 4...
متن کاملReaction of Bovine Pancreatic Ribonuclease A with 1, S-Diflworo=2,4=dinitrobenzene II. STRUCTURE OF AN INTRAMOLECULARLY BRIDGED DERIVATIVE*
In the previous communication (1) it was reported that the reaction of ribonuclease A with the bifunctional reagent, 1,5difluoro-2,4-dinitrobenzene leads to the formation of three major cross-linked derivatives. Each of them was shown to contain one N , N’-2,4-dinitrophenylene 1,5-cross-link per mole of the derivative. In this communication we are describing the structure of one of these deriva...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
- Biochemistry
دوره 50 37 شماره
صفحات -
تاریخ انتشار 2011