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
3.4.17.B1 Sulfolobus solfataricus carboxypeptidaseAdvanced search results
results (
results (Substrates Products
Substrates Products 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.
top
SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
benzoyl-glycyl-L-lysine + H2O
benzoyl-glycine + L-lysine
-
-
-
?
benzyloxycarbonyl-Ala + H2O
L-alanine + benzyloxycarbonate
-
-
-
?
benzyloxycarbonyl-Ala-Ser-methyl ester + H2O
?
-
-
?
benzyloxycarbonyl-Ala-Val-methyl ester + H2O
?
-
-
?
benzyloxycarbonyl-Asp + H2O
L-aspartate + benzyloxycarbonate
-
-
-
?
benzyloxycarbonyl-L-Arg + H2O
benzyloxycarbonate + L-Arg
-
-
-
?
benzyloxycarbonyl-Leu-Ala-methyl ester + H2O
?
-
-
?
benzyloxycarbonyl-Leu-Gly-methyl ester + H2O
?
-
-
?
benzyloxycarbonyl-Phe + H2O
L-phenylalanine + benzyloxycarbonate
-
-
-
?
benzoyl-L-arginine + H2O
benzoic acid + L-arginine
-
-
-
?
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
?
broad substrate specificity, overview
-
?
peptide + H2O
?
broad substrate specificity, overview
-
?
protein + H2O
peptides
broad substrate specificity, overview
-
?
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
-
?
