title: Evaluating N-benzylgalactonoamidines as putative transition state analogs for β-galactoside hydrolysis.
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.
authors.affiliation: 119 Department of Chemistry and Biochemistry, University of Arkansas, Fayetteville, AR 72701, USA. susanne.striegler@uark.edu.
authors.forename: Qiu-Hua
authors.initials: QH
authors.lastname: Fan
authors.forename: Susanne
authors.initials: S
authors.lastname: Striegler
authors.forename: Rebekah G
authors.initials: RG
authors.lastname: Langston
authors.forename: James D
authors.initials: JD
authors.lastname: Barnett
mesh_terms: D000578:Amidines / Q000737:chemistry* / Q000378:metabolism; D002384:Catalysis; D005697:Galactosides / Q000378:metabolism*; D006868:Hydrolysis; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy; D013379:Substrate Specificity; D001616:beta-Galactosidase / Q000378:metabolism*
chemical_list: D000578:Amidines; D005697:Galactosides; C007816:beta-galactoside; D001616:beta-Galactosidase