EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
3.4.21.B55 | azocasein + H2O |
- |
Pyrococcus furiosus |
? |
- |
? |
3.4.21.B55 | beta-casein + H2O |
- |
Pyrococcus furiosus |
? |
- |
? |
3.4.21.B55 | casein + H2O |
- |
Pyrococcus furiosus |
? |
- |
? |
3.4.21.B55 | D-Val-Leu-Lys-4-nitroanilide + H2O |
41% of the activity compared to succinyl-Ala-Ala-Pro-Lys-4-nitroanilide |
Pyrococcus furiosus |
D-Val-Leu-Lys + 4-nitroaniline |
- |
? |
3.4.21.B55 | kappa-casein + H2O |
- |
Pyrococcus furiosus |
? |
- |
? |
3.4.21.B55 | methoxysuccinyl-Arg-Pro-Tyr-4-nitroanilide + H2O |
52% of the activity compared to succinyl-Ala-Ala-Pro-Lys-4-nitroanilide |
Pyrococcus furiosus |
methoxysuccinyl-Arg-Pro-Tyr + 4-nitroaniline |
- |
? |
3.4.21.B55 | more |
no activity with Ala-Ala-Phe-4-nitroanilide or pyroglutamyl-Pro-Val-4-nitroanilide |
Pyrococcus furiosus |
? |
- |
? |
3.4.21.B55 | RPKHPIKHQGLPQEVLNENLLRF + H2O |
i.e. alphaS1-casein-(123) can be completely degraded by pyrolysin resulting in the appearance of four new peptides that are identified based on their retention time. Prolonged incubation shows a decrease of the peptides 116 and 1023 and the appearance of new cleavage products. Pyrolysin is an endopeptidase with two preferential cleavage sites in alphaS1-casein, at bonds 910 and 1617 |
Pyrococcus furiosus |
RPKHPIKHQ + GLPQEVL + NENLLRF |
- |
? |
3.4.21.B55 | succinyl-AAPK-4-nitroanilide + H2O |
- |
Pyrococcus furiosus |
succinyl-AAPK + 4-nitroaniline |
- |
? |
3.4.21.B55 | succinyl-Ala-Ala-Pro-Arg-4-nitroanilide + H2O |
32% of the activity compared to succinyl-Ala-Ala-Pro-Lys-4-nitroanilide |
Pyrococcus furiosus |
succinyl-Ala-Ala-Pro-Arg + 4-nitroaniline |
- |
? |