Ontology highlight
ABSTRACT:
SUBMITTER: Toplak A
PROVIDER: S-EPMC7921005 | biostudies-literature | 2021
REPOSITORIES: biostudies-literature
Toplak Ana A Teixeira de Oliveira Eduardo F EF Schmidt Marcel M Rozeboom Henriëtte J HJ Wijma Hein J HJ Meekels Linda K M LKM de Visser Rowin R Janssen Dick B DB Nuijens Timo T
Computational and structural biotechnology journal 20210209
Omniligase-1 is a broadly applicable enzyme for peptide bond formation between an activated acyl donor peptide and a non-protected acyl acceptor peptide. The enzyme is derived from an earlier subtilisin variant called peptiligase by several rounds of protein engineering aimed at increasing synthetic yields and substrate range. To examine the contribution of individual mutations on S/H ratio and substrate scope in peptide synthesis, we selected peptiligase variant M222P/L217H as a starting enzyme ...[more]