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Information on EC 3.4.17.B5 - Pyrococcus furiosus carboxypeptidase and Organism(s) Pyrococcus furiosus and UniProt Accession Q8U3L0

for references in articles please use BRENDA:EC3.4.17.B5
preliminary BRENDA-supplied EC number
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This record set is specific for:
Pyrococcus furiosus
UNIPROT: Q8U3L0
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The taxonomic range for the selected organisms is: Pyrococcus furiosus
The expected taxonomic range for this enzyme is: Pyrococcus furiosus
Reaction Schemes
broad specificity for neutral, aromatic, polar, and basic C-terminal residues. No activity with N-carboxybenzoyl-Ala-Pro, N-carboxybenzoyl-Ala-Asp, N-carboxybenzoyl-Ala-Gly, N-carboxybenzoyl-Ala-Glu.
Synonyms
pfucp, pyrococcus furiosus carboxypeptidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Ac-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe + H2O
Ac-Asp-Arg-Val-Tyr-Ile-His-Pro + L-phenylalanine
show the reaction diagram
-
-
-
?
Ac-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His + H2O
Ac-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe + L-histidine
show the reaction diagram
-
-
-
?
Ac-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu + H2O
Ac-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His + L-leucine
show the reaction diagram
-
-
-
?
Ac-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Leu + H2O
Ac-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu + L-leucine
show the reaction diagram
-
-
-
?
Ac-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Leu-Val + H2O
Ac-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Leu + L-valine
show the reaction diagram
-
-
-
?
Ac-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Leu-Val-Tyr + H2O
Ac-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Leu-Val + L-tyrosine
show the reaction diagram
-
-
-
?
Ac-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Leu-Val-Tyr-Ser + H2O
Ac-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Leu-Val-Tyr + L-serine
show the reaction diagram
stepwise hydrolysis of up to seven residues from the C-terminus
-
-
?
N-carboxybenzoyl-Ala-Ala + H2O
N-carboxybenzoyl-Ala + L-alanine
show the reaction diagram
-
-
-
?
N-carboxybenzoyl-Ala-Arg + H2O
N-carboxybenzoyl-Ala + L-arginine
show the reaction diagram
-
-
-
?
N-carboxybenzoyl-Ala-Ile + H2O
N-carboxybenzoyl-Ala + L-isoleucine
show the reaction diagram
-
-
-
?
N-carboxybenzoyl-Ala-Leu + H2O
N-carboxybenzoyl-Ala + L-leucine
show the reaction diagram
-
-
-
?
N-carboxybenzoyl-Ala-Lys + H2O
N-carboxybenzoyl-Ala + L-lysine
show the reaction diagram
-
-
-
?
N-carboxybenzoyl-Ala-Met + H2O
N-carboxybenzoyl-Ala + L-methionine
show the reaction diagram
-
-
-
?
N-carboxybenzoyl-Ala-Phe + H2O
N-carboxybenzoyl-Ala + L-phenylalanine
show the reaction diagram
-
-
-
?
N-carboxybenzoyl-Ala-Trp + H2O
N-carboxybenzoyl-Ala + L-tryptophan
show the reaction diagram
-
-
-
?
N-carboxybenzoyl-Ala-Tyr + H2O
N-carboxybenzoyl-Ala + L-tyrosine
show the reaction diagram
-
-
-
?
N-carboxybenzoyl-Ala-Val + H2O
N-carboxybenzoyl-Ala + L-valine
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
purified in its inactive state by the addition of EDTA and dithiothreitol to purification buffers, and the activity is restored by the addition of Co2+. No activation by Zn2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
DTT
2 mM, complete inhibition
EDTA
1 mM, complete inhibition. Inhibition is fully reversible upon 50fold dilution and re-activation by Co2+
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.9
N-carboxybenzoyl-Ala-Arg
80°C, pH 6.5, 0.4 mM CoCl2
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
600
N-carboxybenzoyl-Ala-Arg
80°C, pH 6.5, 0.4 mM CoCl2
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
667
N-carboxybenzoyl-Ala-Arg
80°C, pH 6.5, 0.4 mM CoCl2
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1391
substrate: N-carboxybenzoyl-Ala-Arg, 80°C, pH 6.5, 0.4 mM CoCl2
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.3 - 7.3
pH 5.3: about 50% of maximal activity, pH 7.3: about 50% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
128000
gel filtration
58000
2 * 58000, SDS-PAGE
59000
2 * 59000, matrix-assisted laser desorption ionization time-of flight mass spectrometry
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
the overall structure of the holoenzyme is extremely thermostable. The activities of both the apo and holo enzyme exhibit a similar second-order decay over time, with 50% activity remaining after 40 min at 80°C
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified in its inactive state by the addition of EDTA and dithiothreitol to purification buffers, and the activity is restored by the addition of Co2+
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cheng, T.C.; Ramakrishnan, V.; Chan, S.I.
Purification and characterization of a cobalt-activated carboxypeptidase from the hyperthermophilic archaeon Pyrococcus furiosus
Protein Sci.
8
2474-2486
1999
Pyrococcus furiosus (Q8U3L0), Pyrococcus furiosus
Manually annotated by BRENDA team