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Literature summary extracted from

  • Cannio, R.; Catara, G.; Fiume, I.; Balestrieri, M.; Rossi, M.; Palmieri, G.
    Identification of a cell-bound extracellular protease overproduced by Sulfolobus solfataricus in peptide-rich media (2010), Protein Pept. Lett., 17, 78-85.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.23.42 Diazoacetyl-DL-norleucine methyl ester
-
Saccharolobus solfataricus
3.4.23.42 EDTA
-
Saccharolobus solfataricus
3.4.23.42 pepstatin
-
Saccharolobus solfataricus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.23.42 membrane associated with outer membrane Saccharolobus solfataricus 16020
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.23.42 120000
-
SDS-PAGE Saccharolobus solfataricus

Organism

EC Number Organism UniProt Comment Textmining
3.4.23.42 Saccharolobus solfataricus Q97WS1
-
-
3.4.23.42 Saccharolobus solfataricus P2 Q97WS1
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.23.42
-
Saccharolobus solfataricus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.23.42 Bovine insulin B-chain + H2O the preferential peptide bonds hydrolyzed are: Phe-Phe, Tyr-Leu, Phe-Tyr, Leu-Val and Tyr-Thr Saccharolobus solfataricus ?
-
?
3.4.23.42 Bovine insulin B-chain + H2O the preferential peptide bonds hydrolyzed are: Phe-Phe, Tyr-Leu, Phe-Tyr, Leu-Val and Tyr-Thr Saccharolobus solfataricus P2 ?
-
?
3.4.23.42 Hemoglobin + H2O the preferential peptide bonds hydrolyzed are: Phe-Phe, Tyr-Leu, Phe-Tyr, Leu-Val and Tyr-Thr Saccharolobus solfataricus ?
-
?
3.4.23.42 Hemoglobin + H2O the preferential peptide bonds hydrolyzed are: Phe-Phe, Tyr-Leu, Phe-Tyr, Leu-Val and Tyr-Thr Saccharolobus solfataricus P2 ?
-
?
3.4.23.42 additional information the enzyme shows no sequence similarity to aspartic proteases of the pepsin family or to pepstatin-insensitive acid protease. The characteristic active site amino acid sequence for aspartic proteases, Asp-Thr-Gly, which is present in all aspartic proteases even with only distant evolutionary relatedness, is absent in SsMTP from Sulfolobus solfataricus as in Sulfolobus acidocaldarius thermopsin, suggesting that different catalytic mechanisms are employed by these proteases Saccharolobus solfataricus ?
-
?
3.4.23.42 additional information the enzyme shows no sequence similarity to aspartic proteases of the pepsin family or to pepstatin-insensitive acid protease. The characteristic active site amino acid sequence for aspartic proteases, Asp-Thr-Gly, which is present in all aspartic proteases even with only distant evolutionary relatedness, is absent in SsMTP from Sulfolobus solfataricus as in Sulfolobus acidocaldarius thermopsin, suggesting that different catalytic mechanisms are employed by these proteases Saccharolobus solfataricus P2 ?
-
?

Subunits

EC Number Subunits Comment Organism
3.4.23.42 monomer 1 * 120000, SDS-PAGE Saccharolobus solfataricus

Synonyms

EC Number Synonyms Comment Organism
3.4.23.42 SsMTP a multi-domain thermopsin-like protease containing the catalytic domain followed by two distinct domains, PKD and Y_Y_Y, which are usually involved in a range of protein-protein interactions among the extracellular proteins. The characteristic active site amino acid sequence for aspartic proteases, Asp Thr Gly, which is present in all aspartic proteases even with only distant evolutionary relatedness, is absent in SsMTP as in Sulfolobus acidocaldarius thermopsin, suggesting that different catalytic mechanisms are employed by these proteases Saccharolobus solfataricus
3.4.23.42 SSO2045 locus name Saccharolobus solfataricus
3.4.23.42 Sulfolobus solfataricus multidomain thermopsin-like protease
-
Saccharolobus solfataricus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.23.42 70
-
-
Saccharolobus solfataricus

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.4.23.42 70 90 70°C: optimum, 90°C: 80% of maximal activity Saccharolobus solfataricus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.4.23.42 80
-
half-life: 20 d Saccharolobus solfataricus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.23.42 2
-
at 70°C Saccharolobus solfataricus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.4.23.42 2 4 pH 2.0: optimum, pH 4.0: about 50% of maximal activity, no activity detectable at pH 6.0 Saccharolobus solfataricus

Expression

EC Number Organism Comment Expression
3.4.23.42 Saccharolobus solfataricus overproduced in response to the peptide-enriched media up