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Literature summary for 3.4.21.B54 extracted from

  • Dib, R.; Chobert, J.M.; Dalgalarrondo, M.; Barbier, G.; Haertle, T.
    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.
    View publication on PubMed

General Stability

General Stability Organism
the enzyme is inactivated instantly in the presence of SDS Pyrococcus abyssi

Inhibitors

Inhibitors Comment Organism Structure
4-(2-aminoethyl)-benzenesulfonyl fluoride 90% inhibition Pyrococcus abyssi
Ca2+ 0.01-0.1 M: 50-60% decrease in activity Pyrococcus abyssi
KCl 0.2-0.45 M: no effect. 0.1 M: 30-40% decrease in activity Pyrococcus abyssi
Mg2+ 0.01-0.1 M: 50-60% decrease in activity Pyrococcus abyssi
NaCl 0.2-0.45 M: no effect. 0.1 M: 30-40% decrease in activity Pyrococcus abyssi
phenylmethylsulfonyl fluoride 80% ihibition Pyrococcus abyssi
Soybean trypsin inhibitor 100% inhibition Pyrococcus abyssi
Urea
-
Pyrococcus abyssi

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
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

Organism UniProt Comment Textmining
Pyrococcus abyssi
-
-
-
Pyrococcus abyssi st 549
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Pyrococcus abyssi

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
-
?
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
-
?
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
-
?
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
-
?
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
-
?
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

Subunits Comment Organism
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]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
95
-
-
Pyrococcus abyssi

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
60 95 60°C: about 40% of maximal activity, 95°C: maximal activity Pyrococcus abyssi

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
100
-
t1/2: 165 min Pyrococcus abyssi
105
-
t1/2: 29 min Pyrococcus abyssi
110
-
t1/2: 7.3 min Pyrococcus abyssi
115
-
t1/2: 2.2 min Pyrococcus abyssi

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9
-
-
Pyrococcus abyssi

pH Range

pH Minimum pH Maximum Comment Organism
7 11 pH 7.0: about 40% of maximal activity, pH 11.0: about 40% of maximal activity Pyrococcus abyssi