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benzoyl-glycyl-arginine + H2O
?
benzoyl-glycyl-L-lysine + H2O
benzoyl-glycine + L-lysine
-
-
-
?
benzoyl-glycyl-lysine + H2O
?
-
-
?
benzoyl-L-arginine + H2O
benzoic acid + L-arginine
benzyloxycarbonyl-Ala + H2O
L-alanine + benzyloxycarbonate
-
-
-
?
benzyloxycarbonyl-Ala-Ser-methyl ester + H2O
?
-
-
?
benzyloxycarbonyl-Ala-Val-methyl ester + H2O
?
-
-
?
benzyloxycarbonyl-Arg + H2O
?
-
-
?
benzyloxycarbonyl-Asp + H2O
?
benzyloxycarbonyl-Asp + H2O
L-aspartate + benzyloxycarbonate
-
-
-
?
benzyloxycarbonyl-Glu-methyl ester + H2O
?
-
-
?
benzyloxycarbonyl-Gly-Gly-Phe + H2O
?
benzyloxycarbonyl-L-Arg + H2O
benzyloxycarbonate + L-Arg
-
-
-
?
benzyloxycarbonyl-Leu-Ala-methyl ester + H2O
?
-
-
?
benzyloxycarbonyl-Leu-Gly-methyl ester + H2O
?
-
-
?
benzyloxycarbonyl-Phe + H2O
?
-
-
?
benzyloxycarbonyl-Phe + H2O
L-phenylalanine + benzyloxycarbonate
-
-
-
?
benzyloxycarbonyl-Phe-Leu + H2O
benzyloxycarbonyl-Phe + Leu
benzyloxycarbonyl-Tyr-ethyl ester + H2O
?
-
-
?
Bz-Gly + H2O
benzoic acid + glycine
-
-
-
-
?
Fur-Gly + H2O
furoic acid + glycine
-
-
-
-
?
furylacryloyl-L-phenylalanine + H2O
furylacrylic acid + L-phenylalanine
L-Bz-Ala + H2O
benzoic acid + L-alanine
-
-
-
-
?
L-Bz-Arg + H2O
benzoic acid + L-arginine
-
-
-
-
?
L-Bz-Glu + H2O
benzoic acid + L-glutamate
-
-
-
-
?
L-Bz-His + H2O
benzoic acid + L-histidine
-
-
-
-
?
L-Bz-Leu + H2O
benzoic acid + L-leucine
-
-
-
-
?
L-Bz-Met + H2O
benzoic acid + L-methionine
-
-
-
-
?
L-Bz-Phe + H2O
benzoic acid + L-phenylalanine
-
-
-
-
?
L-Fur-Leu + H2O
furoic acid + L-leucine
-
-
-
-
?
L-Fur-Phe + H2O
furoic acid + L-phenylalanine
-
-
-
-
?
N-[3-(2-Furylacryloyl)]-L-Ala-L-Lys + H2O
N-[3-(2-Furylacryloyl)]-L-Ala + L-Lys
additional information
?
-
benzoyl-glycyl-arginine + H2O
?
-
-
?
benzoyl-glycyl-arginine + H2O
?
-
-
?
benzoyl-glycyl-arginine + H2O
?
-
-
-
?
benzoyl-L-arginine + H2O
benzoic acid + L-arginine
-
-
-
-
?
benzoyl-L-arginine + H2O
benzoic acid + L-arginine
-
-
-
?
benzoyl-L-arginine + H2O
benzoic acid + L-arginine
-
-
-
?
benzyloxycarbonyl-Asp + H2O
?
-
-
-
?
benzyloxycarbonyl-Asp + H2O
?
-
-
?
benzyloxycarbonyl-Asp + H2O
?
-
-
-
?
benzyloxycarbonyl-Gly-Gly-Phe + H2O
?
-
-
-
?
benzyloxycarbonyl-Gly-Gly-Phe + H2O
?
best substrate
-
?
benzyloxycarbonyl-Gly-Gly-Phe + H2O
?
best substrate
-
?
benzyloxycarbonyl-Phe-Leu + H2O
benzyloxycarbonyl-Phe + Leu
-
-
-
?
benzyloxycarbonyl-Phe-Leu + H2O
benzyloxycarbonyl-Phe + Leu
-
-
-
?
furylacryloyl-L-phenylalanine + H2O
furylacrylic acid + L-phenylalanine
-
-
-
?
furylacryloyl-L-phenylalanine + H2O
furylacrylic acid + L-phenylalanine
-
-
-
?
N-[3-(2-Furylacryloyl)]-L-Ala-L-Lys + H2O
N-[3-(2-Furylacryloyl)]-L-Ala + L-Lys
-
-
-
?
N-[3-(2-Furylacryloyl)]-L-Ala-L-Lys + H2O
N-[3-(2-Furylacryloyl)]-L-Ala + L-Lys
-
-
-
?
peptide + H2O
?
-
-
?
peptide + H2O
?
broad substrate specificity, overview
-
?
peptide + H2O
?
broad substrate specificity, overview
-
?
protein + H2O
peptides
-
-
?
protein + H2O
peptides
-
-
-
?
protein + H2O
peptides
-
-
?
protein + H2O
peptides
broad substrate specificity, overview
-
?
protein + H2O
peptides
-
-
-
?
protein + H2O
peptides
-
-
-
?
additional information
?
-
enzyme also shows esterase activity, no activity with 4-nitroanilide substrates
-
?
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
-
-
?
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
-
-
?
additional information
?
-
enzyme also shows esterase activity, no activity with 4-nitroanilide substrates
-
?
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0.022
-
crude cell extract, cells grown on glucose, exponential phase
0.029
-
crude cell extract, cells grown on glucose, stationary phase
0.079
-
crude cell extract, cells grown on yeast extract, stationary phase
0.095
-
crude cell extract, cells grown on yeast extract, exponential phase
16.3
purified enzyme, substrate benzyloxycarbonyl-Arg
21.9
purified enzyme, substrate benzoyl-glycyl-arginine
27.2
purified enzyme, substrate benzoyl-glycyl-lysine
38.7
purified enzyme, substrate benzyloxycarbonyl-Gly-Gly-Phe
4.1
purified enzyme, substrate benzyloxycarbonyl-Phe
8.6
purified enzyme, substrate benzyloxycarbonyl-Asp
additional information
substrate specificity, esterase activity
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0 - 25
instable at, glycerol stabilizes
20
stable for several days at room temperature in buffer containing 10 mM imidazole-HCl, 10 mM potassium acetate and 23 mM Tris-HCl, pH 7.2, in the presence of 2 mM 2-mercaptoethanol and 50% (v/v) glycerol
25
the enzyme gradually loses its activity resulting in a complete inactivation after 96 h. The nanobioconjugate of the enzyme immobilized on silica-coated magnetic nanoparticles leads to a substantial increase in stability, up to 85% of initial activity being retained after 96 h
40
in the presence of ethanol at 40°C and various concentrations the inactivation profiles shows that the enzyme has a residual activity of 50% after 6 h, which decreases to 20% after 24 h incubation. The nanobioconjugate of the enzyme immobilized on silica-coated magnetic nanoparticles reveales a significantly improved stability in ethanol at the different tested concentrations compared with free enzyme, up to 80-90% of residual activity after 6 h, and 70% after 24 h incubation in 80% ethanol being retained
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
95
17% remaining activity
50
in the absence of glycerol and 2-mercaptoethanol, at 50°C, the enzyme undergoes a slow thermal inactivation upon dilution in an aqueous buffer at pH 6.5. This loss of activity can be inhibited when the enzyme is maintained at high pressure. At higher temperatures, higher pressures (up to 400 MPa) are required to maintain the enzyme in its active state
50
after 1 h of incubation at 50°C and 1 MPa in the absence of substrate, the activity is decreased by 30%. This effect is abolished when the enzyme is incubated at 200 MPa. Activity loss at atmospheric pressure is about 7% in 10 min, the activity can be stabilized completely at 300 MPa
80
holoenzyme is stable at 80°C, while the apoenzyme is rapidly inactivated
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
90
85% remaining activity
90
-
stable at, 15 min, pH 7.0
90
enzyme looses activity at the rate of 25% in 10 min, a pressure raise of 400 MPa results in a 4fold decrease of the inactivation rate
additional information
hydrophobic interactions between Leu7 and Leu376 increase protein thermostability
additional information
-
hydrophobic interactions between Leu7 and Leu376 increase protein thermostability
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acetonitril
93% remaining activity in 50% acetonitril at 40°C after 101 min, inactivation at 70°C
acetonitril
-
93% remaining activity in 50% acetonitril at 40°C after 101 min, inactivation at 70°C
-
dimethylformamide
the enzyme gradually loses its activity by increasing the dimethylformamide in the solvent mixture, while the nanobioconiugate retains 80% of residual activity even in the presence of 80% dimethylformamide
dimethylformamide
-
the enzyme gradually loses its activity by increasing the dimethylformamide in the solvent mixture, while the nanobioconiugate retains 80% of residual activity even in the presence of 80% dimethylformamide
-
Ethanol
90% remaining activity in pure ethanol at 40°C after 98 min, inactivation over this time period at 70°C, 2% remaining activity in 50% ethanol at 70°C
Ethanol
nanobioconjugate of the enzyme immobilized on silica-coated magnetic nanoparticles exhibits enhanced stability in aqueous media at room temperature as well as in different organic solvents. The improved stability in ethanol paves the way to possible applications of immobilized enzyme, in particular as a biocatalyst for the synthesis of N-blocked amino acids
Ethanol
-
nanobioconjugate of the enzyme immobilized on silica-coated magnetic nanoparticles exhibits enhanced stability in aqueous media at room temperature as well as in different organic solvents. The improved stability in ethanol paves the way to possible applications of immobilized enzyme, in particular as a biocatalyst for the synthesis of N-blocked amino acids
-
Ethanol
-
90% remaining activity in pure ethanol at 40°C after 98 min, inactivation over this time period at 70°C, 2% remaining activity in 50% ethanol at 70°C
-
Methanol
56% remaining activity in pure methanol at 40°C after 98 min, inactivation over this time period at 70°C, 11% remaining activity in 50% methanol at 70°C
Methanol
-
56% remaining activity in pure methanol at 40°C after 98 min, inactivation over this time period at 70°C, 11% remaining activity in 50% methanol at 70°C
-
tetrahydrofuran
19% remaining activity in 50% tetrahydrofuran after 42 min at 40°C, nactivation at 70°C
tetrahydrofuran
-
19% remaining activity in 50% tetrahydrofuran after 42 min at 40°C, nactivation at 70°C
-
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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
Biochem. J.
295
827-831
1993
Saccharolobus solfataricus, Saccharolobus solfataricus (P80092), Saccharolobus solfataricus MT-4 / DSM 5833, Saccharolobus solfataricus P2 (P80092)
-
brenda
Colombo, S.; D'Auria, S.; Fusi, P.; Zecca, L.; Raia, C.A.; Tortora, P.
Purification and characterization of a thermostable carboxypeptidase from the extreme thermophilic archaebacterium Sulfolobus solfataricus
Eur. J. Biochem.
206
349-357
1992
Saccharolobus solfataricus (P80092), Saccharolobus solfataricus P2 (P80092)
brenda
Fusi, P.; Villa, M.; Burlini, N.; Tortora, P.; Guerritore, A.
Intracellular proteases from the extremely thermophilic archaebacterium Sulfolobus solfataricus
Experientia
47
1057-1060
1991
Saccharolobus solfataricus, Saccharolobus solfataricus MT-4 / DSM 5833
-
brenda
Occhipinti, E.; Bec, N.; Gambirasio, B.; Baietta, G.; Martelli, P.L.; Casadio, R.; Balny, C.; Lange, R.; Tortora, P.
Pressure and temperature as tools for investigating the role of individual non-covalent interactions in enzymatic reactions Sulfolobus solfataricus carboxypeptidase as a model enzyme
Biochim. Biophys. Acta
1764
563-572
2006
Saccharolobus solfataricus
brenda
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
Proteins
71
1843-1852
2008
Saccharolobus solfataricus (P80092), Saccharolobus solfataricus
brenda
Colombo, S.; Toietta, G.; Zecca, L.; Vanoni, M.; Tortora, P.
Molecular cloning, nucleotide sequence, and expression of a carboxypeptidase-encoding gene from the archaebacterium Sulfolobus solfataricus
J. Bacteriol.
177
:5561-5566
1995
Saccharolobus solfataricus (P80092)
brenda
Bec, N.; Villa, A.; Tortora, P.; Mozhaev, V.V.; Balny, C.; Lange, R.
Enhanced stability of carboxypeptidase from Sulfolobus solfataricus at high pressure
Biotechnol. Lett.
18
483-488
1996
Saccharolobus solfataricus (P80092), Saccharolobus solfataricus P2 (P80092)
-
brenda
Occhipinti, E.; Martelli, P.L.; Spinozzi, F.; Corsi, F.; Formantici, C.; Molteni, L.; Amenitsch, H.; Mariani, P.; Tortora, P.; Casadio, R.
3D structure of Sulfolobus solfataricus carboxypeptidase developed by molecular modeling is confirmed by site-directed mutagenesis and small angle X-ray scattering
Biophys. J.
85
1165-1175
2003
Saccharolobus solfataricus
brenda
Sommaruga, S.; Galbiati, E.; Penaranda-Avila, J.; Brambilla, C.; Tortora, P.; Colombo, M.; Prosperi, D.
Immobilization of carboxypeptidase from Sulfolobus solfataricus on magnetic nanoparticles improves enzyme stability and functionality in organic media
BMC Biotechnol.
14
82
2014
Saccharolobus solfataricus (P80092), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (P80092)
brenda