Back to All Enzymes

Omniligase-1

Host Organism

Bacillus amyloliquefaciens

Type

Sequence

AKCVSYGVAQIKAPALHSQGYTGSNVKVAVLDSGIDSSHPDLNVAGGASFVPSETNPFQDNNSHGTHVAGTVLAVAPSASLYAVKVLGADGSGQYSWVINGIEWAIANNMDVINMSLGGPSGSAALKAAVDKAVASGVVVVAAAGNSGTSGSSSTVSYPAKYPSVIAVGAVDSSNQRAPFSSVGPELDVMAPGVSICSTLPGGKYGAHSGTCPASNHVAGAAALILSKHPNWTNTQVRSSLENTATKLGDSFYYGKGLINVEAAAQHHHHHH

External Links

PDB ID: 7AM8
EC: 3.4.21.62
MEROPS: S8 subtilase
UniProt ID: -
NCBI: -

Substrate Specificity

-

Functions

  • Intermolecular backbone terminal ligation
  • Backbone terminal cyclization
  • Specificity stringency: Prime-low, Nonprime-low, only stringent to the C-terminal active ester/thioester served as a leaving group

Expression Platform:

  • E. coli

Mutations:

  • Improve S/H ratio: 22 mutants compared with subtilisin BPN'

Other Properties:

-

References:

  1. [1] (Engineering) Schmidt, M.; Toplak, A.; Quaedflieg, P. J. L. M.; Ippel, H.; Richelle, G. J. J.; Hackeng, T. M.; van?Maarseveen, J. H.; Nuijens, T. Omniligase-1: A Powerful Tool for Peptide Head-to-Tail Cyclization. Advanced Synthesis & Catalysis 2017, 359 (12), 2050-2055. DOI: https://doi.org/10.1002/adsc.201700314
  2. [2] () (Structure) Toplak, A.; Teixeira de Oliveira, E. F.; Schmidt, M.; Rozeboom, H. J.; Wijma, H. J.; Meekels, L. K. M.; de Visser, R.; Janssen, D. B.; Nuijens, T. From thiol-subtilisin to omniligase: Design and structure of a broadly applicable peptide ligase. Comput Struct Biotechnol J 2021, 19, 1277-1287. DOI: 10.1016/j.csbj.2021.02.002