Catalytic Accelerations of 10 12 -Fold by an Enzyme-Like Synthetic Polymer
- 1 August 1972
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 69 (8) , 2155-2159
- https://doi.org/10.1073/pnas.69.8.2155
Abstract
A synthetic polymer, polyethyleneimine containing dodecyl (C(12)H(25))-chains for binding sites and imidazole moieties for functional catalytic groups, catalyzes the hydrolysis of phenolic sulfate esters by a two-step mechanism resembling that of the corresponding natural enzyme. Quantitative rate studies give kinetic parameters that show that the polymer (synzyme) accelerates the rate 10(12)-fold compared to unbound imidazole, and 10(2)-fold compared to a type IIA aryl sulfatase enzyme.Keywords
This publication has 10 references indexed in Scilit:
- Macromolecule-small molecule interactions. Strong binding by intramolecularly cross-linked polylysineBiochemistry, 1971
- Synthetic Derivatives of Polyethyleneimine with Enzyme-Like Catalytic Activity (Synzymes)Proceedings of the National Academy of Sciences, 1971
- The type II arylsulphatases of the red kangarooBiochimica et Biophysica Acta (BBA) - Enzymology, 1971
- Macromolecule-small molecule interactions. Strong binding and cooperativity in a model synthetic polymerBiochemistry, 1969
- The sulphatase of ox liver XII. The effect of tyrosine and histidine reagents on the activity of sulphatase ABiochimica et Biophysica Acta (BBA) - Protein Structure, 1969
- Structure of crystalline α-chymotrypsinJournal of Molecular Biology, 1968
- Mechanism of Action of Proteolytic EnzymesAnnual Review of Biochemistry, 1965
- The Kinetics of the α-Chymotrypsin-Catalyzed Hydrolysis of p-Nitrophenyl Acetate*Biochemistry, 1962
- The ultramicro determination of inorganic sulphateBiochemical Journal, 1960
- Studies in detoxication. 43. A study of the arylsulphatase activity of takadiastase towards some phenolic ethereal sulphatesBiochemical Journal, 1952