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Literature summary extracted from
- Purification, molecular properties and specificity of a thermoactive and thermostable proteinase from Pyrococcus abyssi, strain st 549, hyperthermophilic archaea from deep-sea hydrothermal ecosystem (1998), FEBS Lett., 431, 279-284.
General Stability
| EC Number | General Stability | Organism |
|---|---|---|
| 3.4.21.B54 | the enzyme is inactivated instantly in the presence of SDS | Pyrococcus abyssi |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.21.B54 | 4-(2-aminoethyl)-benzenesulfonyl fluoride | 90% inhibition | Pyrococcus abyssi |  |
| 3.4.21.B54 | Ca2+ | 0.01-0.1 M: 50-60% decrease in activity | Pyrococcus abyssi | |
| 3.4.21.B54 | KCl | 0.2-0.45 M: no effect. 0.1 M: 30-40% decrease in activity | Pyrococcus abyssi | |
| 3.4.21.B54 | Mg2+ | 0.01-0.1 M: 50-60% decrease in activity | Pyrococcus abyssi | |
| 3.4.21.B54 | NaCl | 0.2-0.45 M: no effect. 0.1 M: 30-40% decrease in activity | Pyrococcus abyssi | |
| 3.4.21.B54 | phenylmethylsulfonyl fluoride | 80% ihibition | Pyrococcus abyssi | |
| 3.4.21.B54 | Soybean trypsin inhibitor | 100% inhibition | Pyrococcus abyssi | |
| 3.4.21.B54 | Urea | - |
Pyrococcus abyssi | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 3.4.21.B54 | 18800 | - |
x * 18800, PfPI protease has a monomeric form of 18800 Da oligomerising into a form of 200000 Da. The monomer and dimer are proteolyticaly inactive, SDS-PAGE | Pyrococcus abyssi |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.21.B54 | Pyrococcus abyssi | - |
- |
- |
| 3.4.21.B54 | Pyrococcus abyssi st 549 | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.4.21.B54 | - |
Pyrococcus abyssi |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.21.B54 | oxidized insulin B-chain + H2O | high affinity for aromatic (Phe and Tyr) and hydrophobic amino acids (mainly Leu) in P1 position, specificity for aromatic moieties in P1' position | Pyrococcus abyssi | oxidized insulin B-chain peptide fragments | - |
? | |
| 3.4.21.B54 | oxidized insulin B-chain + H2O | high affinity for aromatic (Phe and Tyr) and hydrophobic amino acids (mainly Leu) in P1 position, specificity for aromatic moieties in P1' position | Pyrococcus abyssi st 549 | oxidized insulin B-chain peptide fragments | - |
? | |
| 3.4.21.B54 | succinyl-Ala-Ala-Pro-Leu-4-nitroanilide + H2O | protease specificity in the P1 position is tested on a wide range of peptidyl-4-nitroanilide substrates. Only the succinyl-Ala-Ala-Pro-Leu-p-nitroanilide and the succinyl-Ala-Ala-Pro-Phe-p-nitroanilide are hydrolyzed | Pyrococcus abyssi | succinyl-Ala-Ala-Pro-Leu + 4-nitroaniline | - |
? | |
| 3.4.21.B54 | succinyl-Ala-Ala-Pro-Leu-4-nitroanilide + H2O | protease specificity in the P1 position is tested on a wide range of peptidyl-4-nitroanilide substrates. Only the succinyl-Ala-Ala-Pro-Leu-p-nitroanilide and the succinyl-Ala-Ala-Pro-Phe-p-nitroanilide are hydrolyzed | Pyrococcus abyssi st 549 | succinyl-Ala-Ala-Pro-Leu + 4-nitroaniline | - |
? | |
| 3.4.21.B54 | succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O | protease specificity in the P1 position is tested on a wide range of peptidyl-4-nitroanilide substrates. Only the succinyl-Ala-Ala-Pro-Leu-p-nitroanilide and the succinyl-Ala-Ala-Pro-Phe-p-nitroanilide are hydrolyzed | Pyrococcus abyssi | succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline | - |
? | |
| 3.4.21.B54 | succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O | protease specificity in the P1 position is tested on a wide range of peptidyl-4-nitroanilide substrates. Only the succinyl-Ala-Ala-Pro-Leu-p-nitroanilide and the succinyl-Ala-Ala-Pro-Phe-p-nitroanilide are hydrolyzed | Pyrococcus abyssi st 549 | succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.4.21.B54 | oligomer | x * 18800, PfPI protease has a monomeric form of 18800 Da oligomerising into a form of 200000 Da. The monomer and dimer are proteolyticaly inactive, SDS-PAGE | Pyrococcus abyssi |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.4.21.B54 | 95 | - |
- |
Pyrococcus abyssi |
Temperature Range [°C]
| EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.4.21.B54 | 60 | 95 | 60°C: about 40% of maximal activity, 95°C: maximal activity | Pyrococcus abyssi |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.4.21.B54 | 100 | - |
t1/2: 165 min | Pyrococcus abyssi |
| 3.4.21.B54 | 105 | - |
t1/2: 29 min | Pyrococcus abyssi |
| 3.4.21.B54 | 110 | - |
t1/2: 7.3 min | Pyrococcus abyssi |
| 3.4.21.B54 | 115 | - |
t1/2: 2.2 min | Pyrococcus abyssi |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.4.21.B54 | 9 | - |
- |
Pyrococcus abyssi |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.4.21.B54 | 7 | 11 | pH 7.0: about 40% of maximal activity, pH 11.0: about 40% of maximal activity | Pyrococcus abyssi |
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