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VyOpt1

Host Organism

Type

PAL

Sequence

MLQLPSEAAKFFHNDNSTNDDDSIGTRWAVLIAGSKGYHNYRHQADVCHMYQILRKGGVKDENIIVFMYDDIAYNESNPFPGIIINKPGGENVYKGVPKDYTGEDINNVNFLAAILGNKSAIIGGSGKVLDTSPNDHIFIYYADHGAPGKIGMPSKPYLYADDLVDTLKQKAATGTYKSMVFYVEACNAGSMFEGLLPEGTNIYAMAASNSTEGSWVTYCPGTPDFPPEFDVCLGDLWSITFLEDCDAHNLRTETVHQQFELVKKKIAYASTVSQYGDIPISKDSLSVYMGTDPANDNRTFVDENSLRPPLKVIHQHDADLYHLWCKYQKAPEGSSKKIEAQKQLLELMSHRAHVDNSITLIGKLLFGVEKASKVLNTVRPVGQPLVDDWQCLKDMIRTFETHCGSLSEYGMKHTLSFANMCNAGIQKEQLAEAAAQACVTFPLEHHHHHH

External Links

PDB ID: -
EC: 3.4.22.34
MEROPS: C13 legumain
UniProt ID: -
NCBI: -

Substrate Specificity

P1
P1'
P2'
N/D
X
L/I/F/Y/W/M

Functions

  • Intermolecular backbone terminal ligation
  • Backbone terminal cyclization, max. kcat/Km: 3.4 x 10^5 M-1s-1
  • Specificity strigency: Prime-low, Nonprime-high

Expression Platform:

  • E. coli

Mutations:

  • Expression level increased over 24-fold to 12 mg/L in E. coli: I351L/N356Q/M357K/N397E/A422D

Other Properties:

-

References:

  1. [1] (Engineering) Du, W., Qi, S., Zhen, M., Liao, M., Zhao, Y., Ma, J., Hao, Y., Jiang, H., Lu, G., Liew, C. W., Chua, N., Chen, H., Hu, G., Hemu, X. (2025). Mining of natural diversity enables efficient and expressible peptide asparaginyl ligases, bioRxiv, DOI: 10.64898/2025.12.16.694575