Synthetic Derivatives of Polyethyleneimine with Enzyme-Like Catalytic Activity (Synzymes)
- 1 February 1971
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 68 (2) , 263-264
- https://doi.org/10.1073/pnas.68.2.263
Abstract
A synthetic polymer has been prepared which contains dodecyl groups (to bind small substrate molecules) and methyleneimidazole side chains (as nucleophilic catalytic sites) linked to a polyethyleneimine framework. This macromolecule, with a high local concentration of binding and catalytic groups, catalyzes the hydrolysis of uncharged nitrophenyl esters in water at pH 7 with rates markedly greater than previously observed with any other synthetic substances under similar conditions.Keywords
This publication has 8 references indexed in Scilit:
- Macromolecule-small molecule interactions. Strong binding and cooperativity in a model synthetic polymerBiochemistry, 1969
- Macromolecule-small molecule interactions: A synthetic polymer with greater affinity than serum albumin for small moleculesBiochemical and Biophysical Research Communications, 1968
- Macromolecule-small molecule interactions. A synthetic macromolecule with high esterolytic activityJournal of the American Chemical Society, 1968
- alpha-Chymotrypsin: Enzyme concentration and kineticsJournal of Chemical Education, 1967
- Synthetic Peptide Models of Enzyme Active Sites. III. Stereoselective Esterase Models1Journal of the American Chemical Society, 1966
- States of amino acid residues in proteinsBiochimica et Biophysica Acta (BBA) - General Subjects, 1964
- The Kinetics of the α-Chymotrypsin-Catalyzed Hydrolysis of p-Nitrophenyl Acetate*Biochemistry, 1962
- IMIDAZOLE CATALYSIS .2. ACYL TRANSFER AND THE REACTIONS OF ACETYL IMIDAZOLE WITH WATER AND OXYGEN ANIONS1959