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Literature summary for 3.4.21.B55 extracted from

  • Voorhorst, W.G.; Eggen, R.I.; Geerling, A.C.; Platteeuw, C.; Siezen, R.J.; Vos, W.M.
    Isolation and characterization of the hyperthermostable serine protease, pyrolysin, and its gene from the hyperthermophilic archaeon Pyrococcus furiosus (1996), J. Biol. Chem., 271, 20426-20431.
    View publication on PubMed
Search for more literature for 3.4.21.B55

Cloned(Commentary)

Cloned (Comment) Organism
-
 Pyrococcus furiosus

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
 Pyrococcus furiosus 16020
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
 two proteolytically active fractions designated as high and low molecular weight pyrolysin Pyrococcus furiosus
150000
-
 x * 150000, SDS-PAGE, after acid denaturation, high molecular weight pyrolysin Pyrococcus furiosus
155000
-
 x * 155000, calculated from sequence of pyrolysin precursor, high molecular weight pyrolysin Pyrococcus furiosus

Organism

Organism UniProt Comment Textmining
Pyrococcus furiosus P72186
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Pyrococcus furiosus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
beta-casein + H2O
-
 Pyrococcus furiosus ?
-
 ?
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
-
 ?
kappa-casein + H2O
-
 Pyrococcus furiosus ?
-
 ?
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
-
 ?
additional information no activity with Ala-Ala-Phe-4-nitroanilide or pyroglutamyl-Pro-Val-4-nitroanilide Pyrococcus furiosus ?
-
 ?
RPKHPIKHQGLPQEVLNENLLRF + H2O i.e. alphaS1-casein-(1–23) 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 1–16 and 10–23 and the appearance of new cleavage products. Pyrolysin is an endopeptidase with two preferential cleavage sites in alphaS1-casein, at bonds 9–10 and 16–17 Pyrococcus furiosus RPKHPIKHQ + GLPQEVL + NENLLRF
-
 ?
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
-
 ?
succinyl-Ala-Ala-Pro-Lys-4-nitroanilide + H2O
-
 Pyrococcus furiosus succinyl-Ala-Ala-Pro-Lys + 4-nitroaniline
-
 ?
succinyl-Ala-Ala-Pro-Met-4-nitroanilide + H2O 13% of the activity compared to succinyl-Ala-Ala-Pro-Lys-4-nitroanilide Pyrococcus furiosus succinyl-Ala-Ala-Pro-Met + 4-nitroaniline
-
 ?
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O 14% of the activity compared to succinyl-Ala-Ala-Pro-Lys-4-nitroanilide Pyrococcus furiosus succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
 ?
succinyl-Glu-Ala-Pro-Phe-4-nitroanilide + H2O 7% of the activity compared to succinyl-Ala-Ala-Pro-Lys-4-nitroanilide Pyrococcus furiosus succinyl-Glu-Ala-Pro-Phe + 4-nitroaniline
-
 ?
succinyl-Lys-Ala-Pro-Phe-4-nitroanilide + H2O 65% of the activity compared to succinyl-Ala-Ala-Pro-Lys-4-nitroanilide Pyrococcus furiosus succinyl-Lys-Ala-Pro-Phe + 4-nitroaniline
-
 ?

Subunits

Subunits Comment Organism
? x * 150000, SDS-PAGE, after acid denaturation, high molecular weight pyrolysin Pyrococcus furiosus
? x * 155000, calculated from sequence of pyrolysin precursor, high molecular weight pyrolysin Pyrococcus furiosus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
95
-
 assay at Pyrococcus furiosus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Pyrococcus furiosus