EC Number   |
Subunits |
Reference |
|---|
   3.4.24.25 | ? |
x * 45000, pro-vibriolysin, SDS-PAGE, x * 35000, vibriolysin, SDS-PAGE |
718364 |
| 3.4.24.25 | monomer |
1 * 35000 (about), Aeromonas proteolytica, sedimentation equilibrium in presence of guanidine-HCl |
31109 |
| 3.4.24.25 | More |
alpha and beta secondary structure analysis, circular dichroism, overview |
718364 |
| 3.4.24.25 | More |
comparative sequence-structure analysis and molecular dynamics simulations to reveal the molecula features of cold adaptation of enzyme. Enzyme has fewer arginines, a lower Arg/(Lys+Arg) ratio, a lower fraction of large aliphatic residues, more methionines, more serines, and more of the thermolabile amino acid asparagine than other thermolysin enzymes. Additionally, the enzyme has fewer intramolecular cation-pi electron interactions and fewer hydrogen bonds than its pseudolysin or thermolysin counterparts |
670843 |
| 3.4.24.25 | More |
gene encodes a signal sequence, an N-terminal propeptide, a mature peptidase domain and a C-terminal propeptide |
701377 |
