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Literature summary for 3.4.17.B1 extracted from

  • Sommaruga, S.; De Palma, A.; Mauri, P.L.; Trisciani, M.; Basilico, F.; Martelli, P.L.; Casadio, R.; Tortora, P.; Occhipinti, E.
    A combined approach of mass spectrometry, molecular modeling, and site-directed mutagenesis highlights key structural features responsible for the thermostability of Sulfolobus solfataricus carboxypeptidase (2008), Proteins, 71, 1843-1852.
    View publication on PubMed
Search for more literature for 3.4.17.B1

Cloned(Commentary)

Cloned (Comment) Organism
expression of His6-tagged wild-type and mutant CPSso in Escherichia coli strain BL21(DE3) Saccharolobus solfataricus

Protein Variants

Protein Variants Comment Organism
A380S site-directed mutagenesis, the mutation does not affect enzyme activity Saccharolobus solfataricus
L376D site-directed mutagenesis, the mutant displays higher values of thermodynamic activation parameters with respect to those of wild type and shows a dramatic drop in thermostability Saccharolobus solfataricus
L376N site-directed mutagenesis, the mutant displays lower values of thermodynamic activation parameters with respect to those of wild type and shows a dramatic drop in thermostability Saccharolobus solfataricus
L7D site-directed mutagenesis, the mutant displays higher values of thermodynamic activation parameters with respect to those of wild type and shows a dramatic drop in thermostability Saccharolobus solfataricus
L7N site-directed mutagenesis, the mutant displays lower values of thermodynamic activation parameters with respect to those of wild type and shows a dramatic drop in thermostability Saccharolobus solfataricus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetics and thermodynamics, recombinant His-tagged CPSso, overview Saccharolobus solfataricus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Saccharolobus solfataricus CPSso, unlike most known carboxypeptidases, removes any amino acid from the C-terminus of short peptides, with the sole exception of proline, and also hydrolyzes N-blocked amino acids, thus acting as an aminoacylase, overview ?
-
 ?

Organism

Organism UniProt Comment Textmining
Saccharolobus solfataricus P80092 gene cpsA1
-

Purification (Commentary)

Purification (Comment) Organism
recombinant HIs6-tagged wild-type and mutant CPSso from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Saccharolobus solfataricus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information CPSso, unlike most known carboxypeptidases, removes any amino acid from the C-terminus of short peptides, with the sole exception of proline, and also hydrolyzes N-blocked amino acids, thus acting as an aminoacylase, overview Saccharolobus solfataricus ?
-
 ?

Subunits

Subunits Comment Organism
More disulfide bridge formed by Cys286 and Cys293 and protease-resistant N- and C-terminal stretches, 3D-structure model, mass spectrometry, overview Saccharolobus solfataricus

Synonyms

Synonyms Comment Organism
carboxypeptidase
-
 Saccharolobus solfataricus
CPSso
-
 Saccharolobus solfataricus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
22
-
 CPSso is maximally active at room temperature Saccharolobus solfataricus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
 hydrophobic interactions between Leu7 and Leu376 increase protein thermostability Saccharolobus solfataricus
90
-
 about, stable up to Saccharolobus solfataricus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
 assay at Saccharolobus solfataricus