Enzymes for the removal of N-carbobenzyloxy protecting groups from N-carbobenzyloxy-d- and l-amino acids

Biocatalytic processes to selectively hydrolyze the N-carbobenzyloxy (CBz) group from CBz-protected d- or l-amino acids have been developed. The substrate specificities of the CBz-deprotecting enzymes from Burkholderia phenazinium SC 16530, and Sphingomonas paucimobilis expressed into Escherichia coli SC 16501 were evaluated on CBz-protected amino acids and structurally related compounds. Modifications of various structural components and their effects on enzyme activity and enantioselectivity provided a greater understanding of the two CBz-deprotecting enzymes.

Graphical abstractFigure optionsDownload full-size imageDownload as PowerPoint slideHighlights► Enzymes for the hydrolysis of N-carbobenzyloxy amino acids. ► Selective deprotection of N-CBz d- or l-amino acids. ► Enzymatic resolution of dl-amino acid by enantioselective CBz deprotection. ► Effect of varying the structures on the activity and enantioselectivity.