3.4.11.B4: Pyrococcus horikoshii deblocking aminopeptidase
This is an abbreviated version!
For detailed information about Pyrococcus horikoshii deblocking aminopeptidase, go to the full flat file.
Word Map on EC 3.4.11.B4
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3.4.11.B4
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hyperthermophilic
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archaeon
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furiosus
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thermococcus
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cobalt
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leu-pna
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tetrahedral
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aminopeptidases
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onnurineus
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exoprotease
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dodecameric
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oligomer
- 3.4.11.B4
-
hyperthermophilic
- archaeon
- furiosus
-
thermococcus
- cobalt
-
leu-pna
-
tetrahedral
- aminopeptidases
- onnurineus
-
exoprotease
-
dodecameric
- oligomer
Reaction
The enzyme exhibits aminopeptidase activity and with lower efficiency deblocking activity (i.e. hydrolysis of acetylated amino acids from the N-terminus of peptides). The turnover number with Ac-Ala-Ala-Ala is 260-540fold lower compared to the activity with Ala-Ala-Ala. The turnover number with Ac-Ala-Ala is 350fold lower compared to the activity with Ala-Ala. Low hydrolytic activity for peptide substrates longer than 10 residues. The enzyme is activated by Co2+ or Zn2+. Contains 1.32 mol of Ca2+ per mol of monomer. =
Synonyms
DAP1, DAP2, DAP3, DAPPh, DAPPh2, DAPPh3, deblocking aminopeptidase, PH0519, PH1527, PH1821
ECTree
3.4.11.B4 Pyrococcus horikoshii deblocking aminopeptidaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.4.11.B4 - Pyrococcus horikoshii deblocking aminopeptidase
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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
N-acetyl-L-Ala-Ala + H2O
N-acetyl-L-alanine + L-alanine
the turnover number with N-acetyl-Ala-Ala is 350fold lower compared to the activity with Ala-Ala
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-
?
N-acetyl-L-alanyl 4-nitroanilide + H2O
N-acetyl-L-alanine + 4-nitroaniline
-
-
-
?
N-acetyl-L-leucyl 4-nitroanilide + H2O
N-acetyl-L-leucine + 4-nitroaniline
-
-
-
?
Ala-Ala + H2O
L-alanine + L-alanine
the activity (turnover number) with N-acetyl-Ala-Ala is 11500fold lower compared to the activity with Ala-Ala
-
-
?
Ala-Ala + H2O
L-alanine + L-alanine
the turnover number with N-acetyl-Ala-Ala is 350fold lower compared to the activity with Ala-Ala
-
-
?
Ala-Ala-Ala + H2O
Ala-Ala + L-alanine
the activity (turnover number) with N-acetyl-Ala-Ala-Ala is 1700fold lower compared to the activity with Ala-Ala-Ala
-
-
?
Ala-Ala-Ala + H2O
Ala-Ala + L-alanine
the activity (turnover number) with N-acetyl-Ala-Ala-Ala is 260fold lower compared to the activity with Ala-Ala-Ala
-
-
?
Ala-Ala-Ala + H2O
Ala-Ala + L-alanine
the turnover number with N-acetyl-Ala-Ala-Ala is 540fold lower compared to the activity with Ala-Ala-Ala
-
-
?
N-acetyl-Ala-Ala-Ala + H2O
Ala-Ala + N-acetyl-L-alanine
the activity (turnover number) with N-acetyl-Ala-Ala-Ala is 260fold lower compared to the activity with Ala-Ala-Ala
-
-
?
N-acetyl-Ala-Ala-Ala + H2O
Ala-Ala + N-acetyl-L-alanine
the turnover number with N-acetyl-Ala-Ala-Ala is 540fold lower compared to the activity with Ala-Ala-Ala
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-
?
additional information
?
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low hydrolytic activity for peptide substrates longer than 10 residues. The enzyme exhibits aminopeptidase and with lower efficiency deblocking activity (hydrolysis of acetylated amino acids from the N-terminus of peptides). No activity with Ala-Pro-Ala, D-Ala-Ala and D-Ala-D-Ala-D-Ala
-
-
?
additional information
?
-
low hydrolytic activity for peptide substrates longer than 10 residues. The enzyme exhibits aminopeptidase and with lower efficiency deblocking activity (hydrolysis of acetylated amino acids from the N-terminus of peptides). No activity with Ala-Pro-Ala, D-Ala-Ala and D-Ala-D-Ala-D-Ala
-
-
?
additional information
?
-
low hydrolytic activity for peptide substrates longer than 10 residues. The enzyme exhibits aminopeptidase and with lower efficiency deblocking activity (hydrolysis of N-acetylated amino acids from the N-terminus of peptides). No activity with Ala-Pro-Ala, D-Ala-Ala and D-Ala-D-Ala-D-Ala
-
-
?
additional information
?
-
low hydrolytic activity for peptide substrates longer than 10 residues. The enzyme exhibits aminopeptidase and with lower efficiency deblocking activity (hydrolysis of N-acetylated amino acids from the N-terminus of peptides). No activity with Ala-Pro-Ala, D-Ala-Ala and D-Ala-D-Ala-D-Ala
-
-
?
