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Information on EC 3.4.11.B4 - Pyrococcus horikoshii deblocking aminopeptidase

for references in articles please use BRENDA:EC3.4.11.B4
preliminary BRENDA-supplied EC number
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UNIPROT: O59485
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Word Map
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
deblocking aminopeptidase
-
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 activity (turnover number) with N-acetyl-Ala-Ala is 11500fold lower compared to the activity with Ala-Ala
-
-
?
Ala-Ala-Ala + H2O
Ala-Ala + L-alanine
show the reaction diagram
the activity (turnover number) with N-acetyl-Ala-Ala-Ala is 1700fold lower compared to the activity with Ala-Ala-Ala
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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 70% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80 - 110
80°C: about 50% of maximal activity, 110°C: about 70% 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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
O59485_PYRHO
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
354
0
39008
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
330000
gel filtration
41000
8 * 41000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
octamer
8 * 41000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop method, crystallized in the native and selenomethionine-substituted state, resolution of 3 A
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
98
2 h, over 70% of the activity remains
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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