EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
   3.4.24.B26 | bovine elastin + H2O |
myroilysin preferentially cleaves peptide bonds of bovine elastin with hydrophobic residues at the P1' and/or P1 positions |
Myroides profundi |
? |
- |
? |
| 3.4.24.B26 | bovine elastin + H2O |
myroilysin preferentially cleaves peptide bonds of bovine elastin with hydrophobic residues at the P1' and/or P1 positions |
Myroides profundi D25 |
? |
- |
? |
| 3.4.24.B26 | casein + H2O |
- |
Myroides profundi |
? |
- |
? |
| 3.4.24.B26 | casein + H2O |
- |
Myroides profundi D25 |
? |
- |
? |
| 3.4.24.B26 | Collagen + H2O |
insoluble type I collagen fibre. Although it displays very low activity with collagen, myroilysin has strong collagen-swelling ability and plays a synergistic role with collagenase in collagen hydrolysis |
Myroides profundi |
? |
- |
? |
| 3.4.24.B26 | Collagen + H2O |
insoluble type I collagen fibre. Although it displays very low activity with collagen, myroilysin has strong collagen-swelling ability and plays a synergistic role with collagenase in collagen hydrolysis |
Myroides profundi D25 |
? |
- |
? |
| 3.4.24.B26 | Elastin + H2O |
the enzyme shows much higher elastinolytic activity than the bacterial elastinase pseudolysin (EC 3.4.24.26). It has 6.78 U/mg elastinolytic activity in artificial seawater at 4°C, suggesting that it probably can degrade elastin in the deep sea |
Myroides profundi |
? |
- |
? |
| 3.4.24.B26 | elastinorcein + H2O |
- |
Myroides profundi |
? |
- |
? |
| 3.4.24.B26 | Fibrin + H2O |
hydrolyzes alpha, beta and gamma fibrin. Cleavage sites on fibrinogen and fibrin are different from those of pseudolysin |
Myroides profundi |
? |
- |
? |
| 3.4.24.B26 | Fibrinogen + H2O |
hydrolyzes Aalpha and Bbeta fibrinogen. Cleavage sites on fibrinogen and fibrin are different from those of pseudolysin |
Myroides profundi |
? |
- |
? |
