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Literature summary for 3.4.17.B1 extracted from

  • Villa, A.; Zecca, L.; Fusi, P.; Colombo, S.; Tedeschi, G.; Tortora, P.
    Structural features responsible for kinetic thermal stability of a carboxypeptidase from the archaebacterium Sulfolobus solfataricus (1993), Biochem. J., 295, 827-831.
No PubMed abstract available
Search for more literature for 3.4.17.B1

Inhibitors

Inhibitors Comment Organism Structure
EDTA
-
 Saccharolobus solfataricus

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ metalloprotease, dependent on, reversible inactivation upon metal depletion Saccharolobus solfataricus
Zn2+ removal of Zn2+ by dialysis leads to reversible activity loss, which is promptly restored by addition of 0.08 mM ZnCl2 to the assay mixture Saccharolobus solfataricus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
peptide + H2O Saccharolobus solfataricus
-
 ?
-
 ?
peptide + H2O Saccharolobus solfataricus MT-4 / DSM 5833
-
 ?
-
 ?
protein + H2O Saccharolobus solfataricus
-
 peptides
-
 ?
protein + H2O Saccharolobus solfataricus MT-4 / DSM 5833
-
 peptides
-
 ?

Organism

Organism UniProt Comment Textmining
Saccharolobus solfataricus
-
-
-
Saccharolobus solfataricus P80092
-
-
Saccharolobus solfataricus MT-4 / DSM 5833
-
-
-
Saccharolobus solfataricus P2 P80092
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Saccharolobus solfataricus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
benzoyl-glycyl-arginine + H2O
-
 Saccharolobus solfataricus ?
-
 ?
benzoyl-glycyl-arginine + H2O
-
 Saccharolobus solfataricus MT-4 / DSM 5833 ?
-
 ?
peptide + H2O
-
 Saccharolobus solfataricus ?
-
 ?
peptide + H2O
-
 Saccharolobus solfataricus MT-4 / DSM 5833 ?
-
 ?
protein + H2O
-
 Saccharolobus solfataricus peptides
-
 ?
protein + H2O
-
 Saccharolobus solfataricus MT-4 / DSM 5833 peptides
-
 ?

Synonyms

Synonyms Comment Organism
M20.008 Merops-ID Saccharolobus solfataricus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
additional information
-
 calculation of activation energies, thermodynamics Saccharolobus solfataricus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
70
-
 inactivation rate constants of both holo- and apo-enzyme is determined at 70°C over a broad pH range. At pH values below 5.7, the metal-depleted enzyme is substantially more stable than the native form, a probable consequence of a reduction in electrostatic repulsion. In contrast, at any pH value above 5.7 loss of Zn2+ severely impairs enzyme stability. Below pH 5 the apoenzyme is also significantly destabilized Saccharolobus solfataricus
80
-
 holoenzyme is stable at 80°C, while the apoenzyme is rapidly inactivated Saccharolobus solfataricus
80
-
 first-order irreversible thermal inactivation of the metal-depleted enzyme shows an activation energy value of 205.6 kJ/mol, which is considerably lower than that of the holoenzyme (494.4 kJ/mol). The values of activation free energies, enthalpies and entropies also dropp with metal removal. Thermal inactivation of the apoenzyme is very quick at 80°C, whereas the holoenzyme is stable at the same temperature. The bivalent cation exhibits a major stabilizing role. Chaotropic salts strongly destabilize the holoenzyme, showing that hydrophobic interactions are involved in maintaining the native conformation of the enzyme. The inactivation rate is also increased by sodium sulfate, acetate and chloride, which are not chaotropes, indicating that one or more salt bridges concur in stabilizing the active enzyme Saccharolobus solfataricus

pH Stability

pH Stability pH Stability Maximum Comment Organism
additional information
-
 at the extremes of the pH-stability curve, NaCl does not affect the inactivation rate, confirming the stabilizing role of intramolecular ionic bonds, as a pH-dependent decrease in stability is likely to occur from breaking of salt bridges involved in maintaining the native conformation of the protein Saccharolobus solfataricus