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(Arg)3 + H2O
Arg + Arg-Arg
-
-
-
ir
(Leu)3 + H2O
Leu + Leu-Leu
-
-
-
ir
(Lys)3 + H2O
Lys + Lys-Lys
-
-
-
ir
Ala-7-amido-4-methylcoumarin + H2O
Ala + 7-amino-4-methylcoumarin
Arg-2-naphthylamide + H2O
Arg + 2-naphthylamine
-
-
-
-
?
Arg-4-nitroanilide + H2O
Arg + 4-nitroaniline
-
-
-
ir
Arg-7-amido-4-methylcoumarin + H2O
Arg + 7-amino-4-methylcoumarin
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 + H2O
Arg + Val
-
-
-
ir
Arg-Val-OMe + H2O
Arg + Val-OMe
-
-
-
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-arginine 4-nitroanilide + H2O
L-arginine + 4-nitroaniline
L-glutamate 4-nitroanilide + H2O
L-glutamate + 4-nitroaniline
20.1% of the activity compared to L-lysine 4-nitroanilide
-
-
?
L-leucine 4-nitroanilide + H2O
L-leucine + 4-nitroaniline
L-leucine p-nitroanilide + H2O
L-leucine + p-nitroaniline
-
-
-
-
?
L-lysine 4-nitroanilide + H2O
L-lysine + 4-nitroaniline
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-4-nitroanilide + H2O
Leu + 4-nitroaniline
-
-
-
ir
Leu-7-amido-4-methylcoumarin + H2O
Leu + 7-amino-4-methylcoumarin
Leu-Arg-Arg-Ala-Ser-Leu-Gly + H2O
Leu + Arg-Arg-Ala-Ser-Leu-Gly
-
-
-
ir
Leu-Leu + H2O
Leu + Leu
-
-
-
ir
Leu-Leu-OMe + H2O
Leu + Leu-OMe
-
-
-
ir
Lys-4-nitroanilide + H2O
Lys + 4-nitroaniline
Lys-7-amido-4-methylcoumarin + H2O
Lys + 7-amino-4-methylcoumarin
Lys-Ala + H2O
Lys + Ala
-
-
-
?
Lys-Ala-4-methylcoumaryl-7-amide + H2O
Lys + Ala-4-methylcoumaryl-7-amide
-
-
-
ir
Lys-Gly-Gly + H2O
Lys + Gly-Gly
-
-
-
?
Lys-Gly-Gly-Lys + H2O
Lys + Gly-Gly-Lys
-
-
-
?
Lys-Leu + H2O
Lys + Leu
-
-
-
?
Lys-Lys-Lys + H2O
Lys + Lys-Lys
-
-
-
?
Lys-Lys-Lys-Lys + H2O
Lys + Lys-Lys-Lys
-
-
-
?
Lys-Phe + H2O
Lys + Phe
-
-
-
?
Met-7-amido-4-methylcoumarin + H2O
Met + 7-amino-4-methylcoumarin
Met-Ala-Ser + H2O
Met + Ala-Ser
-
-
-
ir
Met-Arg-Phe + H2O
Met + Arg-Phe
-
-
-
ir
Met-Gly-Gly + H2O
Met + Gly-Gly
-
-
-
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
Tyr-Gly-Gly-Phe-Leu + H2O
Tyr + Gly-Gly-Phe-Leu
-
-
-
ir
additional information
?
-
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
-
-
-
?
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-4-nitroanilide + H2O
Lys + 4-nitroaniline
-
-
-
-
?
Lys-4-nitroanilide + H2O
Lys + 4-nitroaniline
-
-
-
?
Lys-4-nitroanilide + H2O
Lys + 4-nitroaniline
-
-
-
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
?
-
-
-
-
-
?
additional information
?
-
-
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
-
-
?
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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Achstetter, T.; Ehmann, C.; Wolf, D.H.
Aminopeptidase Co, a new yeast peptidase
Biochem. Biophys. Res. Commun.
109
341-347
1982
Saccharomyces cerevisiae
brenda
Herrerra-Camacho, I.; Suarez-Rendueles, P.
Regulation of the yeast vacuolar aminopeptidase Y gene (APY1) expression
FEMS Microbiol. Lett.
139
127-132
1996
Saccharomyces cerevisiae
brenda
Yasuhara, T.; Nakai, T.; Ohashi, A.
Aminopeptidase Y, a new aminopeptidase from Saccharomyces cerevisiae. Purification, properties, localization, and processing by protease B
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269
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Saccharomyces cerevisiae
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Molecular cloning of the aminopeptidase Y gene of Saccharomyces cerevisiae. Sequence analysis and gene disruption of a new aminopeptidase
J. Biol. Chem.
269
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Saccharomyces cerevisiae
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Ultracytochemical localization of the vacuolar marker enzymes alkaline phosphatase, adenosine triphosphatase, carboxypeptidase Y and aminopeptidase reveal new concept of vacuole biogenesis in Saccharomyces cerevisiae
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92
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1989
Saccharomyces cerevisiae
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Jorgensen, M.U.; Emr, S.D.; Winther, J.R.
Ligand recognition and domain structure of Vps10p, a vacuolar protein sorting receptor in Saccharomyces cerevisiae
Eur. J. Biochem.
260
461-469
1999
Saccharomyces cerevisiae
brenda
Pan, D.; Tanokura, M.
Purification and characterization of an aminopeptidase from Lactobacillus helveticus JCM 1004
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88
511-516
2004
Lactobacillus helveticus, Lactobacillus helveticus JCM 1004
brenda
Nakai, T.; Yasuhara, T.
Aminopeptidase Y
Handbook of proteolytic enzymes (Barrett, A. J. , Rawlings, N. D. , Woessner, J. F. , eds. ) Academic Press
1
956-957
2004
Saccharomyces cerevisiae
-
brenda
Rossier, O.; Dao, J.; Cianciotto, N.P.
The type II secretion system of Legionella pneumophila elaborates two aminopeptidases, as well as a metalloprotease that contributes to differential infection among protozoan hosts
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74
753-761
2008
Legionella pneumophila
brenda
Hernandez-Montanez, Z.; Araujo-Osorio, J.; Noriega-Reyes, Y.; Chavez-Camarillo, G.; Villa-Tanaca, L.
The intracellular proteolytic system of Yarrowia lipolytica and characterization of an aminopeptidase
FEMS Microbiol. Lett.
268
178-186
2007
Yarrowia lipolytica
brenda
Munih, P.; Moulin, A.; Stamper, C.C.; Bennett, B.; Ringe, D.; Petsko, G.A.; Holz, R.C.
X-ray crystallographic characterization of the Co(II)-substituted Tris-bound form of the aminopeptidase from Aeromonas proteolytica
J. Inorg. Biochem.
101
1099-1107
2007
Vibrio proteolyticus
brenda
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
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517
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2012
Pyrococcus horikoshii (O59485), Pyrococcus horikoshii OT-3 (O59485)
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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
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1814
1289-1294
2011
Pyrococcus horikoshii (O59485), Pyrococcus horikoshii
brenda
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
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187
2077-2083
2005
Pyrococcus furiosus (Q8TZW4), Pyrococcus furiosus
brenda
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
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72
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Pyrococcus horikoshii (O59485), Pyrococcus horikoshii
brenda
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Enhanced lysosomal activity by overexpressed aminopeptidase Y in Saccharomyces cerevisiae
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417
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2016
Saccharomyces cerevisiae
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