3.4.17.B1: Sulfolobus solfataricus carboxypeptidase
This is an abbreviated version!
For detailed information about Sulfolobus solfataricus carboxypeptidase, go to the full flat file.
Word Map on EC 3.4.17.B1
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3.4.17.B1
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hyperthermophilic
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zinc-metalloenzyme
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n-blocked
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asparagine
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archaeon
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synthesis
- 3.4.17.B1
-
hyperthermophilic
-
zinc-metalloenzyme
-
n-blocked
- asparagine
- archaeon
- synthesis
Reaction
Release of basic, acidic and aromatic amino acids from the respective benzoylglycated and benzyloxycarbonylated amino acids. Slow hydrolysis of aliphatic amino acids. No activity with benzyloxycarbonyl-Pro and benzyloxycarbonyl-Trp =
Synonyms
carboxypeptidase, carboxypeptidase S1, CPS, cpsA, CPSso, M20.008, SSO1355, thermostable carboxypeptidase 1
ECTree
3.4.17.B1 Sulfolobus solfataricus carboxypeptidaseAdvanced search results
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results (Organic Solvent Stability
Organic Solvent Stability on EC 3.4.17.B1 - Sulfolobus solfataricus carboxypeptidase
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ORGANIC SOLVENT 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetonitril
dimethylformamide
Ethanol
Methanol
tetrahydrofuran
acetonitril
93% remaining activity in 50% acetonitril at 40°C after 101 min, inactivation at 70°C
acetonitril
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93% remaining activity in 50% acetonitril at 40°C after 101 min, inactivation at 70°C
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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
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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
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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
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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
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Ethanol
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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
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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
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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
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tetrahydrofuran
19% remaining activity in 50% tetrahydrofuran after 42 min at 40°C, nactivation at 70°C
tetrahydrofuran
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19% remaining activity in 50% tetrahydrofuran after 42 min at 40°C, nactivation at 70°C
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