Precomplexation and Activation of Carboxylate and Phosphate Esters,
Abstract
The hydrolyses of unactivated esters and amides (both carboxylic and phosphoryl) are exceptionally slow, yet subject to efficient catalysis by enzymes. Because these reactions are key to metabolic processes and to the CW agents designed to interfere with them, the abiotic duplication of transacylase activity remains an eagerly sought-after target. Desirable properties for one class of ideal synthetic transacylase, biotic or abiotic, might include: rapid reaction in totally aqueous solution near neutral pH; activity towards unactivated substrates with turnover behavior; selectivity coupled with a practical ability to bind substrates of widely diverse structural types; an ability to produce the pure catalyst on usefully large scale. To date, no catalyst type meets all of these design criteria. Nevertheless, the past five years has seen such progress that artificial transacylases can no longer be characterized as 'pipe dreams'.
Document Details
- Document Type
- Technical Report
- Publication Date
- May 31, 1992
- Accession Number
- ADA251846
Entities
People
- Anthony W. Czarnik
Organizations
- Ohio State University