Specificity of Penicillin Acylases in Deprotection of N-Benzyloxycarbonyl Derivatives of Amino Acids

I A Morozova; D T Guranda; N V Panin; V K Švedas

doi:10.32607/actanaturae.13703

Specificity of Penicillin Acylases in Deprotection of N-Benzyloxycarbonyl Derivatives of Amino Acids

Acta Naturae. 2023 Jan-Mar;15(1):69-73. doi: 10.32607/actanaturae.13703.

Authors

I A Morozova¹, D T Guranda¹, N V Panin^{1

2}, V K Švedas^{1

2

3}

Affiliations

¹ Lomonosov Moscow State University, Belozersky Institute of Physicochemical Biology, Moscow, 119234 Russian Federation.
² Lomonosov Moscow State University, Research Computing Center, Moscow, 119234 Russian Federation.
³ Lomonosov Moscow State University, Faculty of Bioengineering and Bioinformatics, Moscow, 119234 Russian Federation.

Abstract

Changes in the structure of the N-acyl group in N-acylated amino acid derivatives significantly affect both the recognition and activity of penicillin acylases on this series of substrates. However, penicillin acylases from both Alcaligenes faecalis and Escherichia coli are capable of removing the N-benzyloxycarbonyl protecting group in amino acid derivatives under mild conditions without the use of toxic reagents. Efficiency in using penicillin acylases in preparative organic synthesis can be improved by utilizing modern rational enzyme design methods.

Keywords: N-benzyloxycarbonyl derivatives of amino acids; enzymatic deprotection of functional groups; penicillin acylases; substrate specificity.