Photo-stimulated leaving group isomerization of acyl donor esters in protease-catalyzed hydrolysis reactions. Issue 6 (2nd November 2018)

• Record Type: Journal Article
• Authors: Elsner, Christian; Lohan, Marcus; Griebel, Jan; Decker, Ulrich
• Is Part Of: Biocatalysis and biotransformation. Volume 36:Issue 6(2018)
• Page Start: 444
• Page End: 449
• Publication Date: 2018-11-02
• Subjects: Trypsin -- chymotrypsin -- photoswitch -- azobenzene -- substrate isomerization; Enzymes -- Biotechnology -- Periodicals; Enzymes -- Industrial applications -- Periodicals; Biotransformation (Metabolism) -- Periodicals; 660.63
• DOI: 10.1080/10242422.2018.1427739
• Languages: English
• ISSNs: 1024-2422

Abstract

Abstract: Hydrolysis studies of photo-switchable N -maleyl-amino acid-(4-phenylazophenyl) esters of Ala, Gly, Met, Phe, and Pro were performed using the proteases trypsin and chymotrypsin. It has been found out that the cis -isomers were hydrolyzed faster than the trans -isomers. In dependence of the amino acid in the P1 position the velocity graduation is Phe > Met > Ala > Gly > Pro for trypsin and Phe ≫ Met > Ala > Gly > Pro for chymotrypsin for both isomers.