Chemical synthesis and enzymatic properties of RNase A analogues designed to enhance second-step catalytic activity
Author:
Affiliation:
1. Department of Biochemistry & Molecular Biology
2. University of Chicago
3. Chicago
4. USA
5. Institute for Biophysical Dynamics
6. Department of Chemistry
Abstract
Adenine covalently attached to the RNase A enzyme molecule decreased the rate of transphosphorylation and increased the rate of hydrolysis.
Publisher
Royal Society of Chemistry (RSC)
Subject
Organic Chemistry,Physical and Theoretical Chemistry,Biochemistry
Link
http://pubs.rsc.org/en/content/articlepdf/2016/OB/C6OB01163B
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1. Bovine Pancreatic Ribonuclease: Fifty Years of the First Enzymatic Reaction Mechanism
2. Ribonuclease A
3. The role of 2', 3'-cyclic phosphodiesters in the bovine pancreatic ribonuclease A catalysed cleavage of RNA: intermediates or products?
4. Hydrolysis and Exchange in Esters of Phosphoric Acid1a,b
5. On the origins of enhanced reactivity of five-membered cyclic phosphate esters. The relative contributions of enthalpic and entropic factors
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