Evaluating N-benzylgalactonoamidines as putative transition state analogs for β-galactoside hydrolysis
Document Type
Article - Abstract Only
Publication Date
2014
Keywords
Stability assays, kinetic assays, synthetic procedures
Abstract
Experimental evidence is provided for p-methylbenzyl-D-galactonoamidine to function as a true transition state analog for the enzymatic hydrolysis of aryl-β-D-galactopyranosides by β-galactosidase (A. oryzae). The compound exhibits inhibition constants in the low nanomolar concentration range (12–56 nM) for a selection of substrates. Along these lines, a streamlined synthetic method based on phase-transfer catalysis was optimized to afford the required variety of new aryl-β-D-galactopyranosides. Last, the stability of the galactonoamidines under the assay conditions was confirmed.
Citation
Fan, Q., Striegler, S., Langston, R., & Barnett, J. (2014). Evaluating N-benzylgalactonoamidines as putative transition state analogs for β-galactoside hydrolysis. Organic & Biomolecular Chemistry, 12 (17), 2792-2800. https://doi.org/10.1039/C4OB00153B
Comments
An undergraduate research fellowship of the University of Arkansas Honors College to R.G.L. and support by the National Science Foundation (CHE-1244755, CHE-1305543) to S. S. are gratefully acknowledged. This study was furthermore supported by Grant Number P30 GM103450 from the National Institute of General Medical Sciences (NIGMS) of the National Institutes of Health (NIH).