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Information on EC 3.4.11.15 - aminopeptidase Y
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EC Tree
3.4.11.15 aminopeptidase YSpecify your search results
Word Map
- 3.4.11.15
- carboxypeptidase
-
pyrococcus
- aminopeptidases
- horikoshii
- bestatin
- p-nitroanilide
- griseus
-
lys-pna
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
aminopeptidase y, lysine aminopeptidase, phtet3, yylape, aminopeptidase co, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aminopeptidase (cobalt-activated)
-
-
-
-
aminopeptidase Co
-
-
-
-
PhTET3
TET3
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
preferentially, release of N-terminal lysine
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
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CAS REGISTRY NUMBER
COMMENTARY
114796-97-3
-
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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
Arg-Arg-4-methylcoumaryl-7-amide + H2O
Arg + Arg-4-methylcoumaryl-7-amide
-
-
-
ir
Arg-Arg-Lys-Ala-Leu-Ser-Pro + H2O
Arg + Arg-Lys-Ala-Leu-Ser-Pro
-
-
-
ir
Arg-Gly-Tyr-Ser-Leu-Gly + H2O
Arg + Gly-Tyr-Ser-Leu-Gly
-
-
-
ir
Arg-Val-Tyr-Ile-His-Pro-Phe + H2O
Arg + Val-Tyr-Ile-His-Pro-Phe
-
-
-
ir
L-alanyl-L-alanine 4-nitroanilide + H2O
L-alanine + L-alanine 4-nitroanilide
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
-
-
?
L-alanyl-L-alanyl-L-alanine 4-nitroanilide + H2O
L-alanine + L-alanyl-L-alanine 4-nitroanilide
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
-
-
?
L-glutamate 4-nitroanilide + H2O
L-glutamate + 4-nitroaniline
20.1% of the activity compared to L-lysine 4-nitroanilide
-
-
?
L-lysyl-4-nitroanilide + H2O
L-lysine + 4-nitroaniline
-
maximal hydrolysis rates are obtained when lysine is in the N-position (Lys-pNA)
-
-
?
L-proline 4-nitroanilide + H2O
L-proline + 4-nitroaniline
6% of the activity compared to Lys-4-nitroanilide, recombinant enzyme
-
-
?
Leu-Arg-Arg-Ala-Ser-Leu-Gly + H2O
Leu + Arg-Arg-Ala-Ser-Leu-Gly
-
-
-
ir
Lys-Ala-4-methylcoumaryl-7-amide + H2O
Lys + Ala-4-methylcoumaryl-7-amide
-
-
-
ir
Pro-Phe-Arg-4-methylcoumaryl-7-amide + H2O
Pro + Phe-Arg-4-methylcoumaryl-7-amide
-
-
-
ir
Ser-7-amido-4-methylcoumarin + H2O
Ser + 7-amino-4-methylcoumarin
-
-
-
ir
Ala-7-amido-4-methylcoumarin + H2O
Ala + 7-amino-4-methylcoumarin
-
-
-
-
?
Ala-7-amido-4-methylcoumarin + H2O
Ala + 7-amino-4-methylcoumarin
-
-
-
ir
Arg-7-amido-4-methylcoumarin + H2O
Arg + 7-amino-4-methylcoumarin
-
-
-
ir
Arg-7-amido-4-methylcoumarin + H2O
Arg + 7-amino-4-methylcoumarin
-
Arg-7-amido-4-methylcoumarin and Lys-7-amido-4-methylcoumarin are the most sensitive substrates. Leu-7-amido-4-methylcoumarin, Met-7-amido-4-methylcoumarin and Ala-7-amido-4-methylcoumarin are next in susceptibility to hydrolysis, followed by Ser-7-amido-4-methylcoumarin, Phe-7-amido-4-methylcoumarin, Tyr-7-amido-4-methylcoumarin and Pro-7-amido-4-methylcoumarin
-
-
?
L-arginine 4-nitroanilide + H2O
L-arginine + 4-nitroaniline
47% of the activity compared to Lys-4-nitroanilide, recombinant enzyme
-
-
?
L-arginine 4-nitroanilide + H2O
L-arginine + 4-nitroaniline
66.6% of the activity compared to L-lysine 4-nitroanilide
-
-
?
L-leucine 4-nitroanilide + H2O
L-leucine + 4-nitroaniline
7% of the activity compared to Lys-4-nitroanilide, recombinant enzyme
-
-
?
L-leucine 4-nitroanilide + H2O
L-leucine + 4-nitroaniline
11.4% of the activity compared to L-lysine 4-nitroanilide
-
-
?
L-lysine 4-nitroanilide + H2O
L-lysine + 4-nitroaniline
-
-
-
?
L-lysine 4-nitroanilide + H2O
L-lysine + 4-nitroaniline
-
-
-
?
Leu-7-amido-4-methylcoumarin + H2O
Leu + 7-amino-4-methylcoumarin
-
-
-
-
?
Leu-7-amido-4-methylcoumarin + H2O
Leu + 7-amino-4-methylcoumarin
-
-
-
ir
Lys-7-amido-4-methylcoumarin + H2O
Lys + 7-amino-4-methylcoumarin
-
-
-
-
?
Lys-7-amido-4-methylcoumarin + H2O
Lys + 7-amino-4-methylcoumarin
-
-
-
ir
Met-7-amido-4-methylcoumarin + H2O
Met + 7-amino-4-methylcoumarin
-
-
-
-
?
Met-7-amido-4-methylcoumarin + H2O
Met + 7-amino-4-methylcoumarin
-
-
-
ir
additional information
?
-
-
the enzyme shows high activity towards 4-nitroanilide derivatives of amino acids (Leu, Ala, and Phe) or diaminocarboxylic acids (Lys and Arg) at the N-termini but not 4-nitroanilide derivatives or peptides with proline at their N-termini or C-termini, such as Pro-4-nitroanilide, Gly-Pro-4-nitroanilide, Pro-Leu and Ala-Pro
-
-
?
additional information
?
-
-
the enzyme shows high activity towards 4-nitroanilide derivatives of amino acids (Leu, Ala, and Phe) or diaminocarboxylic acids (Lys and Arg) at the N-termini but not 4-nitroanilide derivatives or peptides with proline at their N-termini or C-termini, such as Pro-4-nitroanilide, Gly-Pro-4-nitroanilide, Pro-Leu and Ala-Pro
-
-
?
additional information
?
-
no activity (or less than 5% compared to L-lysine 4-nitroanilide): L-alanine 4-nitroanilide, L-glycine 4-nitroanilide, L-histidine 4-nitroanilide, L-phenylalanine 4-nitroanilide, phenylacetyl 4-nitroanilide
-
-
?
additional information
?
-
-
no activity (or less than 5% compared to L-lysine 4-nitroanilide): L-alanine 4-nitroanilide, L-glycine 4-nitroanilide, L-histidine 4-nitroanilide, L-phenylalanine 4-nitroanilide, phenylacetyl 4-nitroanilide
-
-
?
additional information
?
-
poor activity is detected against L-ornithinyl- and L-glutaminyl-7-amido-4-methylcoumarin, and L-aspartyl-, L-methionyl- and L-alanyl 4-nitroanilide, while the enzyme shows very poor or no activity against the other aminoacyl-4-nitroanilides or aminoacyl-7-amido-4-methylcoumarines assayed. No activity can be measured against any of the N-terminal blocked derivatives
-
-
?
additional information
?
-
-
poor activity is detected against L-ornithinyl- and L-glutaminyl-7-amido-4-methylcoumarin, and L-aspartyl-, L-methionyl- and L-alanyl 4-nitroanilide, while the enzyme shows very poor or no activity against the other aminoacyl-4-nitroanilides or aminoacyl-7-amido-4-methylcoumarines assayed. No activity can be measured against any of the N-terminal blocked derivatives
-
-
?
additional information
?
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-
generally higher activities with dipeptide-4-methylcoumaryl-7-amides than with amino-acid-4-methylcoumaryl-7-amides
-
-
?
additional information
?
-
-
only those p-nitroanilide derivatives containing basic amino acids are cleaved
-
-
?
additional information
?
-
-
Vps10p is important for the vacuolar sorting of high levels of APY and APY interacts with domain 2 of Vps10p
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-
?
additional information
?
-
-
regulation on translational and posttranslational level, according to medium conditions: more active enzyme produced under C- or N-starving conditions
-
-
?
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NATURAL SUBSTRATE
NATURAL 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
additional information
?
-
-
Vps10p is important for the vacuolar sorting of high levels of APY and APY interacts with domain 2 of Vps10p
-
-
?
additional information
?
-
-
regulation on translational and posttranslational level, according to medium conditions: more active enzyme produced under C- or N-starving conditions
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
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
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
Co2+
-
25fold enhancement of hydrolysis of Arg-7-amido-4-methylcoumarin and Lys-7-amido-4-methylcoumarin. Hydrolysis of substrates longer than tripeptide or dipeptide-7-amido-4-methylcoumarin is inhibited
Co2+
-
for spectroscopic studies the enzyme containing magnetically and spectroscopically silent Zn(II) ion is substituted with Co(II)
Zinc
the purified enzyme contains two equivalent of zinc per monomer. When zinc is removed by EDTA treatment, the complex dissociates into dimeric species
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Co2+
-
25fold enhancement of hydrolysis of Arg-7-amido-4-methylcoumarin and Lys-7-amido-4-methylcoumarin. Hydrolysis of substrates longer than tripeptide or dipeptide-7-amido-4-methylcoumarin is inhibited, IC50: 0.1 mM
additional information
the enzyme is insensitive to the papain and trypsin inhibitor antipain, to the cysteine proteases inhibitor E-64, to the serine and cysteine proteases inhibitor leupeptin, to the aspartate proteases inhibitor pepstatin, and to the metalloendopeptidases inhibitor phosphoramidon. Puromycin, an inhibitor of some exopeptidases, has practically no effect on the activity of PhTET3
-
additional information
-
the enzyme is insensitive to the papain and trypsin inhibitor antipain, to the cysteine proteases inhibitor E-64, to the serine and cysteine proteases inhibitor leupeptin, to the aspartate proteases inhibitor pepstatin, and to the metalloendopeptidases inhibitor phosphoramidon. Puromycin, an inhibitor of some exopeptidases, has practically no effect on the activity of PhTET3
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
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
-
additional information
-
activation of 75000 Da-proform to 70000 Da active form by protease B
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Leiomyoma
Activities of proteinases and of a proteinase B inhibitor in tumors of the human uterus.
Neoplasms
Activities of proteinases and of a proteinase B inhibitor in tumors of the human uterus.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
L-lysine 4-nitroanilide
KM-value as a function of pressure
4.6
L-lysine 4-nitroanilide
pH 8.0, 100°C, enzyme from Pyrococcus furiosus
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1260
L-lysine 4-nitroanilide
pH 8.0, 100°C, enzyme from Pyrococcus furiosus
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
274
L-lysine 4-nitroanilide
pH 8.0, 100°C, enzyme from Pyrococcus furiosus
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.1
Co2+
Saccharomyces cerevisiae
-
25fold enhancement of hydrolysis of Arg-7-amido-4-methylcoumarin and Lys-7-amido-4-methylcoumarin. Hydrolysis of substrates longer than tripeptide or dipeptide-7-amido-4-methylcoumarin is inhibited, IC50: 0.1 mM
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
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
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8.5
pH 6: about 50% of maximal activity, pH 8.0: about 90% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100
activity of enzyme from Pyrococcus furiosus and recombinant enzyme increase from 40°C to 100°C
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
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
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
within microglobules in juvenile vacuoles, concept of vavuole biogenesis based on enzyme allocation
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
lysosomes isolated from APE3 overexpressing cells exhibit better antimicrobial effects than normal cells, and anticancerous effects of lysosomes isolated from the overexpressing Saccharomyces cerevisiae increase on cancer cells such as HeLa, HaCaT, and melanoma cells by in vitro assay