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Information on EC 3.4.11.15 - aminopeptidase Y

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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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UNIPROT: O59485 not found.
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Word Map
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The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
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preferentially, release of N-terminal lysine
Synonyms
aminopeptidase y, lysine aminopeptidase, phtet3, yylape, aminopeptidase co, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aminopeptidase (cobalt-activated)
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-
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aminopeptidase Co
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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-
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-
CAS REGISTRY NUMBER
COMMENTARY hide
114796-97-3
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-alanyl-L-alanine 4-nitroanilide + H2O
L-alanine + L-alanine 4-nitroanilide
show the reaction diagram
L-alanine 4-nitroanilide accumulates very fast in the reaction mixture, and the L-alanine 4-nitroanilide/4-nitroaniline ratio diminishes from 123 at 5 min to 69 at 25 min, therefore indicating that the enzyme is mostly cleaving the substrate to L-alanine 4-nitroanilide, and then also this last product to give 4-nitroaniline
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-
?
L-alanyl-L-alanyl-L-alanine 4-nitroanilide + H2O
L-alanine + L-alanyl-L-alanine 4-nitroanilide
show the reaction diagram
L-alanyl-L-alanine 4-nitroanilide is produced, but also consumed by the enzyme while 4-nitroaniline is generated after a lag phase. At 26 min the ratios L-alanyl-L-alanine 4-nitroaniline/4-nitroaniline and L-alanyl 4-nitroanilide/4-nitroaniline are 8 and 33 respectively
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-
?
L-arginine 4-nitroanilide + H2O
L-arginine + 4-nitroaniline
show the reaction diagram
66.6% of the activity compared to L-lysine 4-nitroanilide
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-
?
L-glutamate 4-nitroanilide + H2O
L-glutamate + 4-nitroaniline
show the reaction diagram
20.1% of the activity compared to L-lysine 4-nitroanilide
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-
?
L-leucine 4-nitroanilide + H2O
L-leucine + 4-nitroaniline
show the reaction diagram
11.4% of the activity compared to L-lysine 4-nitroanilide
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-
?
L-lysine 4-nitroanilide + H2O
L-lysine + 4-nitroaniline
show the reaction diagram
Lys-4-nitroanilide + H2O
Lys + 4-nitroaniline
show the reaction diagram
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-
-
?
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
1 mM, 2.4fold activation
KCl
the enzyme is optimally active at salt concentration between 0.075 and 0.25 M KCl. More than 70% of the activity is maintained at 2 M KCl
Zinc
the purified enzyme contains two equivalent of zinc per monomer. When zinc is removed by EDTA treatment, the complex dissociates into dimeric species
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
amastatin
0.002 mM, 77% inhibition
bestatin
0.5 mM, 34% inhibition
Ca2+
1 mM,% inhibition
Cd2+
1 mM,% inhibition
chymostatin
1 mM, 22% inhibition
Cu2+
1 mM,% inhibition
EDTA
0.02 mM, 85% inhibition
Mg2+
1 mM,% inhibition
Mn2+
1 mM,% inhibition
pefabloc
5 mM, 20% inhibition
Zn2+
1 mM,% inhibition
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
the enzymatic activity is enhanced by pressure up to 180 MPa. The enzyme is active under hydrostatic pressure of up to 350 MPa
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
L-lysine 4-nitroanilide
KM-value as a function of pressure
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8.5
pH 6: about 50% of maximal activity, pH 8.0: about 90% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
O59485_PYRHO
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
354
0
39008
TrEMBL
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40000
12 * 40000, SDS-PAGE, the active sites of the PhTET complexes are located inside the particles, in the catalytic chambers that are enclosed by the tetrahedron apices. The walls of these chambers are positively charged, and each one contains three active sites arranged in a circular way. Adjacent to the active sites, the specificity pockets appear as small cavities. The geometry of these pockets is different in each PhTET complex, as well as their location in the particles relative to the active sites. In PhTET3, the specificity pocket is formed by the side-chains of D262, T240, T295 and T297, which leads to a negative charge
500000
dodecameric complex, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dodecamer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the 12-subunit PhTET3 complex is crystallized and its 3D structure is solved at a resolution of 1.9 A by molecular replacement
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100
half-life: 27 min
80
half-life: 17.83 min
90
half-life: 3.44 min
95
half-life: 55.1 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
high robustness of the oligomeric enzyme under high pressure of up to 300 MPa at 25°C as well as at 90°C
the enzyme is stable and functional under hypersaline conditions
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Rosenbaum, E.; Gabel, F.; Dura, M.A.; Finet, S.; Clery-Barraud, C.; Masson, P.; Franzetti, B.
Effects of hydrostatic pressure on the quaternary structure and enzymatic activity of a large peptidase complex from Pyrococcus horikoshii
Arch. Biochem. Biophys.
517
104-110
2012
Pyrococcus horikoshii (O59485), Pyrococcus horikoshii OT-3 (O59485)
Manually annotated by BRENDA team
Rosenbaum, E.; Ferruit, M.; Dura, M.A.; Franzetti, B.
Studies on the parameters controlling the stability of the TET peptidase superstructure from Pyrococcus horikoshii revealed a crucial role of pH and catalytic metals in the oligomerization process
Biochim. Biophys. Acta
1814
1289-1294
2011
Pyrococcus horikoshii (O59485), Pyrococcus horikoshii
Manually annotated by BRENDA team
Dura, M.A.; Rosenbaum, E.; Larabi, A.; Gabel, F.; Vellieux, F.M.; Franzetti, B.
The structural and biochemical characterizations of a novel TET peptidase complex from Pyrococcus horikoshii reveal an integrated peptide degradation system in hyperthermophilic Archaea
Mol. Microbiol.
72
26-40
2009
Pyrococcus horikoshii (O59485), Pyrococcus horikoshii
Manually annotated by BRENDA team