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Literature summary for 3.4.23.42 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
Search for more literature for 3.4.23.42

Inhibitors

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

Localization

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Saccharolobus solfataricus Q97WS1
-
-
Saccharolobus solfataricus P2 Q97WS1
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Saccharolobus solfataricus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Bovine insulin B-chain + H2O the preferential peptide bonds hydrolyzed are: Phe-Phe, Tyr-Leu, Phe-Tyr, Leu-Val and Tyr-Thr Saccharolobus solfataricus ?
-
 ?
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 ?
-
 ?
Hemoglobin + H2O the preferential peptide bonds hydrolyzed are: Phe-Phe, Tyr-Leu, Phe-Tyr, Leu-Val and Tyr-Thr Saccharolobus solfataricus ?
-
 ?
Hemoglobin + H2O the preferential peptide bonds hydrolyzed are: Phe-Phe, Tyr-Leu, Phe-Tyr, Leu-Val and Tyr-Thr Saccharolobus solfataricus P2 ?
-
 ?
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 ?
-
 ?
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

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

Synonyms

Synonyms Comment Organism
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
SSO2045 locus name Saccharolobus solfataricus
Sulfolobus solfataricus multidomain thermopsin-like protease
-
 Saccharolobus solfataricus

Temperature Optimum [°C]

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

Temperature Range [°C]

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

Temperature Stability [°C]

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

pH Optimum

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

pH Range

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

Expression

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