3.4.11.15: aminopeptidase Y
This is an abbreviated version!
For detailed information about aminopeptidase Y, go to the full flat file.
Word Map on EC 3.4.11.15
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3.4.11.15
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carboxypeptidase
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pyrococcus
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aminopeptidases
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horikoshii
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bestatin
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p-nitroanilide
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griseus
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lys-pna
- 3.4.11.15
- carboxypeptidase
-
pyrococcus
- aminopeptidases
- horikoshii
- bestatin
- p-nitroanilide
- griseus
-
lys-pna
Reaction
preferentially, release of N-terminal lysine =
Synonyms
AAP, aminopeptidase (cobalt-activated), aminopeptidase Co, APE3, LapB, lysine aminopeptidase, PF1861, PH1821, PhTET3, TET3, yylAPE
ECTree
3.4.11.15 aminopeptidase YAdvanced search results
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results (Substrates Products
Substrates Products on EC 3.4.11.15 - aminopeptidase Y
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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
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-
?
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
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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
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-
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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
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-
?
additional information
?
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-
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
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-
?
additional information
?
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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
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-
?
additional information
?
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-
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
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-
?
additional information
?
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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
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-
?
additional information
?
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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
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-
?
additional information
?
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generally higher activities with dipeptide-4-methylcoumaryl-7-amides than with amino-acid-4-methylcoumaryl-7-amides
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?
additional information
?
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only those p-nitroanilide derivatives containing basic amino acids are cleaved
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?
additional information
?
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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
?
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regulation on translational and posttranslational level, according to medium conditions: more active enzyme produced under C- or N-starving conditions
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?
