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Peptiligase

Host Organism

Bacillus amyloliquefaciens

Type

Sequence

AKCVSYGVSQIKAPALHSQGYTGSNVKVAVIDSGIDSSHPDLNVAGGASFVPSETNPFQDNNSHGTHVAGTVLAVAPSASLYAVKVLGADGSGQYSWIINGIEWAIANNMDVINMSLGGPSGSAALKAAVDKAVASGVVVVAAAGNSGTSGSSSTVSYPAKYPSVIAVGAVDSSNQRAPFSSVGPELDVMAPGVSICSTLPGNKYGALSGTCMASAHVAGAAALILSKHPNWTNTQVRSSLENTATKLGDSFYYGKGLINVEAAAQHHHHHH

External Links

PDB ID: 7AM3, 7AM4, 7AM5, 7AM6, 7AM7
EC: 3.4.21.62
MEROPS: S8 subtilase
UniProt ID: P00782
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 stability, Calcium-indepenency: a deleted calcium binding domain (deletion of 9 amino acids, number 75 to 83) and additional 18 stabilizing mutations, including one disulfide bridge

Other Properties:

-

References:

  1. [1] (Engineering, Sequence) Toplak, A.; Nuijens, T.; Quaedflieg, P. J. L. M.; Wu, B.; Janssen, D. B. Peptiligase, an Enzyme for Efficient Chemoenzymatic Peptide Synthesis and Cyclization in Water. Advanced Synthesis & Catalysis 2016, 358 (13), 2140-2147. DOI: https://doi.org/10.1002/adsc.201600017