CATH Classification

Domain Context

CATH Clusters

Superfamily 3.10.450.490
Functional Family

Enzyme Information

3.4.24.25
Vibriolysin.
based on mapping to UniProt A1DRD5
Preferential cleavage of bonds with bulky hydrophobic groups in P2 and P1'. Phe at P1' is the most favored residue, which distinguished this enzyme from thermolysin.
-!- Thermostable enzyme from Vibrio proteolyticus (formerly Aeromonas proteolytica). -!- Specificity related to, but distinct from, those of the thermolysin and Bacillus subtilis endopeptidase. -!- Belongs to peptidase family M4. -!- Formerly EC 3.4.24.4.

UniProtKB Entries (1)

A1DRD5
A1DRD5_PSEU9
Pseudoalteromonas sp. SM9913
Secreted metalloprotease Mcp02

PDB Structure

PDB 3NQY
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Structural basis for the autoprocessing of zinc metalloproteases in the thermolysin family
Gao, X., Wang, J., Yu, D.-Q., Bian, F., Xie, B.-B., Chen, X.-L., Zhou, B.-C., Lai, L.-H., Wang, Z.-X., Wu, J.-W., Zhang, Y.-Z.
Proc.Natl.Acad.Sci.USA