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Information on EC 3.4.11.B4 - Pyrococcus horikoshii deblocking aminopeptidase and Organism(s) Pyrococcus horikoshii and UniProt Accession O59196

for references in articles please use BRENDA:EC3.4.11.B4
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Pyrococcus horikoshii
UNIPROT: O59196
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The taxonomic range for the selected organisms is: Pyrococcus horikoshii
The expected taxonomic range for this enzyme is: Pyrococcus horikoshii
Reaction Schemes
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
deblocking aminopeptidase, more
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Ala-Ala + H2O
L-alanine + L-alanine
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
the turnover number with N-acetyl-Ala-Ala-Ala is 540fold lower compared to the activity with Ala-Ala-Ala
-
-
?
N-acetyl-L-Ala-Ala + H2O
N-acetyl-L-alanine + L-alanine
show the reaction diagram
the turnover number with N-acetyl-Ala-Ala is 350fold lower compared to the activity with Ala-Ala
-
-
?
Ala-Ala + H2O
L-alanine + L-alanine
show the reaction diagram
Ala-Ala-Ala + H2O
Ala-Ala + L-alanine
show the reaction diagram
Ala-Ala-Ala-Ala + H2O
Ala-Ala-Ala + L-alanine
show the reaction diagram
-
-
-
?
Ala-Ala-Ala-Ala-Ala + H2O
Ala-Ala-Ala-Ala + L-alanine
show the reaction diagram
-
-
-
?
N-acetyl-Ala-Ala-Ala + H2O
Ala-Ala + N-acetyl-L-alanine
show the reaction diagram
the activity (turnover number) with N-acetyl-Ala-Ala-Ala is 260fold lower compared to the activity with Ala-Ala-Ala
-
-
?
N-acetyl-L-alanyl 4-nitroanilide + H2O
N-acetyl-L-alanine + 4-nitroaniline
show the reaction diagram
-
-
-
?
N-acetyl-L-leucyl 4-nitroanilide + H2O
N-acetyl-L-leucine + 4-nitroaniline
show the reaction diagram
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
39.9
Ala-Ala
pH 7.5, 85°C
3.4 - 18.2
Ala-Ala-Ala
13.2
Ala-Ala-Ala-Ala
pH 7.5, 85°C
10.8
Ala-Ala-Ala-Ala-Ala
pH 7.5, 85°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.18
Ala-Ala
pH 7.5, 85°C
0.091 - 9.01
Ala-Ala-Ala
0.022
N-acetyl-L-alanyl 4-nitroanilide
pH 7.5, 85°C
0.116
N-acetyl-L-leucyl 4-nitroanilide
pH 7.5, 85°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.3 - 8.5
pH 6.3: about 20% of maximal activity, pH 8.5: about 55% of maximal activity
6.3 - 8.5
pH 6.3: about 20% of maximal activity, pH 8.5: about 70% of maximal activity
7 - 8.3
pH 6.5: about 20% of maximal activity, pH 7.0: about 90% of maximal activity, pH 8.3: about 50% of maximal activity
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
85 - 110
85°C: about 40% of maximal activity, 110°C: about 90% of maximal activity
80 - 110
80°C: about 50% of maximal activity, 110°C: about 70% of maximal activity
85 - 98
85°C: about 35% of maximal activity, 98°C: about 85% of maximal activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
Pyrococcus horikoshii has three similar aminopeptidases with deblocking activity. These enzymes appear to play important roles in hydrolyzing small peptides in Pyrococcus horikoshii cells
physiological function
Pyrococcus horikoshii has three similar aminopeptidases with deblocking activity. These enzymes appear to play important roles in hydrolyzing small peptides in Pyrococcus horikoshii cells
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
330000
gel filtration
42000
8 * 42000, SDS-PAGE
330000
gel filtration
36900
41000
8 * 41000, SDS-PAGE
440000
gel filtration, HPLC
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
octamer
8 * 42000, SDS-PAGE
?
x * 36900, wild-type enzyme, mutant enzymes D173N, E205Q and E206Q, SDS-PAGE
octamer
8 * 41000, SDS-PAGE
oligomer
x * 36900, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop method, crystallized in the native and selenomethionine-substituted state, resolution of 3 A
sitting drop method, crystallized in the native and selenomethionine-substituted state, resolution of 3 A
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D173N
Km-value for Ala-Ala-Ala is not significantly different from the KM-value for the wild-type enzyme, kcat is significantly reduced
E205Q
Km-value for Ala-Ala-Ala is not significantly different from the KM-value for the wild-type enzyme, kcat is significantly reduced
E206Q
Km-value for Ala-Ala-Ala is not significantly different from the KM-value for the wild-type enzyme, kcat is significantly reduced
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
98
2 h, over 70% of the activbity remains
90
2 h, about 20% loss of activity
95
about 15% loss of activity after 1 h, about 70% loss of activity after 2 h
98
2 h, over 70% of the activity remains
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
overexpressed in Escherichia coli
expression in Escherichia coli
overexpressed in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Porciero, S.; Receveur-Brchot, V.; Mori, K.; Franzetti, B.; Roussel, A.
Expression, purification, crystallization and preliminary crystallographic analysis of a deblocking aminopeptidase from Pyrococcus horikoshii
Acta Crystallogr. Sect. F
61
239-242
2005
Pyrococcus horikoshii (O58255), Pyrococcus horikoshii (O59196), Pyrococcus horikoshii (O59485), Pyrococcus horikoshii
Manually annotated by BRENDA team
Onoe, S.; Ando, S.; Ataka, M.; Ishikawa, K.
Active site of deblocking aminopeptidase from Pyrococcus horikoshii
Biochem. Biophys. Res. Commun.
290
994-997
2002
Pyrococcus horikoshii (O58255), Pyrococcus horikoshii
Manually annotated by BRENDA team
Mori, K.; Ishikawa, K.
New deblocking aminopeptidases from Pyrococcus horikoshii
Biosci. Biotechnol. Biochem.
69
1854-1860
2005
Pyrococcus horikoshii (O59196), Pyrococcus horikoshii (O59485)
Manually annotated by BRENDA team
Ando, S.; Ishikawa, K.; Ishida, H.; Kawarabayasi, Y.; Kikuchi, H.; Kosugi, Y.
Thermostable aminopeptidase from Pyrococcus horikoshii
FEBS Lett.
447
25-28
1999
Pyrococcus horikoshii (O58255), Pyrococcus horikoshii
Manually annotated by BRENDA team