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Information on EC 3.4.11.15 - aminopeptidase Y and Organism(s) Pyrococcus furiosus and UniProt Accession Q8TZW4

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.11 Aminopeptidases
                3.4.11.15 aminopeptidase Y
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This record set is specific for:
Pyrococcus furiosus
UNIPROT: Q8TZW4 not found.
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Word Map
The taxonomic range for the selected organisms is: Pyrococcus furiosus
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
preferentially, release of N-terminal lysine
Synonyms
aminopeptidase y, lysine aminopeptidase, phtet3, yylape, aminopeptidase co, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
lysine aminopeptidase
-
aminopeptidase (cobalt-activated)
-
-
-
-
aminopeptidase Co
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
114796-97-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-arginine 4-nitroanilide + H2O
L-arginine + 4-nitroaniline
show the reaction diagram
47% of the activity compared to Lys-4-nitroanilide, recombinant enzyme
-
-
?
L-leucine 4-nitroanilide + H2O
L-leucine + 4-nitroaniline
show the reaction diagram
7% of the activity compared to Lys-4-nitroanilide, recombinant enzyme
-
-
?
L-lysine 4-nitroanilide + H2O
L-lysine + 4-nitroaniline
show the reaction diagram
-
-
-
?
L-proline 4-nitroanilide + H2O
L-proline + 4-nitroaniline
show the reaction diagram
6% of the activity compared to Lys-4-nitroanilide, recombinant enzyme
-
-
?
Lys-Ala + H2O
Lys + Ala
show the reaction diagram
-
-
-
?
Lys-Gly-Gly + H2O
Lys + Gly-Gly
show the reaction diagram
-
-
-
?
Lys-Gly-Gly-Lys + H2O
Lys + Gly-Gly-Lys
show the reaction diagram
-
-
-
?
Lys-Leu + H2O
Lys + Leu
show the reaction diagram
-
-
-
?
Lys-Lys-Lys + H2O
Lys + Lys-Lys
show the reaction diagram
-
-
-
?
Lys-Lys-Lys-Lys + H2O
Lys + Lys-Lys-Lys
show the reaction diagram
-
-
-
?
Lys-Phe + H2O
Lys + Phe
show the reaction diagram
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
0.2 mM, 4fold stimulation. When the sample is preincubated with 0.2 mM Co2+ ions and subjected to gel filtration, only 10% of the activity remains, while addition of Co2+ (0.2 mM) to the reaction mixture completely restores enzyme activity. Co2+ions could not be replaced with other divalent (Ca2+, Cd2+, Cu2+, Fe2+, Mg2+, Mn2+, Ni2+, or Zn2+) or monovalent cations (Na+or K+) when used at concentrations of up to 0.2 mM
Zinc
the enzyme contains 2.0 zinc atoms per subunit
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.4
L-arginine 4-nitroanilide
pH 8.0, 100°C, recombinant enzyme
4 - 4.6
L-lysine 4-nitroanilide
1.8 - 2.7
Lys-Gly-Gly
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
769
L-arginine 4-nitroanilide
pH 8.0, 100°C, recombinant enzyme
1260 - 1840
L-lysine 4-nitroanilide
305 - 1460
Lys-Gly-Gly
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
550
L-arginine 4-nitroanilide
pH 8.0, 100°C, recombinant enzyme
274 - 460
L-lysine 4-nitroanilide
169 - 540
Lys-Gly-Gly
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1900
pH 8.0, 100°C, 0.2 mM Co2+, purified enzyme from Pyrococcus furiosus
220
pH 8.0, 100°C, 0.2 mM Co2+, purified enzyme from Pyrococcus furiosus
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
enzyme from Pyrococcus furiosus and recombinant enzyme
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100
activity of enzyme from Pyrococcus furiosus and recombinant enzyme increase from 40°C to 100°C
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60 - 100
at 60°C the recombinant enzyme shows about 35% of the activity at 100°C. At 60°C the enzyme from Pyrococcus furiosus shows about 60% of the activity at 100°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
160000
gel filtration
38214
4 * 38214, calculated from sequence
40000
4 * 40000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100
6 h, enzyme from Pyrococcus furiosus loses 50% of its activity, recombinant enzyme loses 50% of its activity within 10 min, presence of 0.2 mM CoCl2 increases half-life of the recombinant enzyme to 6 h
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native and recombinant enzyme
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
the recombinant protein containing a polyhistidine tag at the N terminus is produced in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Story, S.V.; Shah, C.; Jenney, F.E. Jr.; Adams, M.W.
Characterization of a novel zinc-containing, lysine-specific aminopeptidase from the hyperthermophilic archaeon Pyrococcus furiosus
J. Bacteriol.
187
2077-2083
2005
Pyrococcus furiosus (Q8TZW4), Pyrococcus furiosus
Manually annotated by BRENDA team