2D NOESY Spectra of a Synthetic Siloxane Oligomer with Selective Esterase Activity.
Abstract
An oligomer containing 4-(dialkylamino) pyridine groups incorporated within a bis(trimethylineamine)disiloxane backbone exhibits remarkable catalytic activity in the hydrolysis of p-nitrophenyl alkanoates. p-Nitrophenyl tetradecanoate is the optimum substrate in 1:1 methanol-water at pH 8, 30 deg C. The structure of the oligomer's catalytically active conformation was investigated by 2D NOESY experiments. The resultant structure parameters obtained with aggregates of catalyst or catalyst-myristoleic acid complex were used to model the intermolecular interactions of catalyst and substrate. This uniquely informative NOESY distance information may explain the enzyme-like, chain length specificity for catalysis of C-14 fatty acid esters. Enzyme-mimic, esterase, p-nitrophenyl alkanoates, oligomeric 4-(dialkylamino)pyridine, 2D NOESY spectra, catalyst-substrate complex model.
Document Details
- Document Type
- Technical Report
- Publication Date
- May 15, 1992
- Accession Number
- ADA250870
Entities
People
- David G. Gorenstein
- Martel Zeldin
- Patricia L. Jackson
- Slawomir Rubinsztajn
- Wilmer K. Fife
Organizations
- Purdue University