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. 1972 Aug;69(8):2155–2159. doi: 10.1073/pnas.69.8.2155

Catalytic Accelerations of 1012-Fold by an Enzyme-Like Synthetic Polymer

Helen C Kiefer 1, Wayne I Congdon 1, Ioannis S Scarpa 1, Irving M Klotz 1
PMCID: PMC426890  PMID: 16592004

Abstract

A synthetic polymer, polyethyleneimine containing dodecyl (C12H25)-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 1012-fold compared to unbound imidazole, and 102-fold compared to a type IIA aryl sulfatase enzyme.

Keywords: Michaelis-Menten kinetics, aryl sulfatase, nitrocatechol sulfate

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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