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
-
3.4.17.B1
-
hyperthermophilic
-
zinc-metalloenzyme
-
n-blocked
-
asparagine
-
archaeon
-
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
Advanced search results
pH Stability
pH Stability on EC 3.4.17.B1 - Sulfolobus solfataricus carboxypeptidase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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
649646
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
649646