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Information on EC 3.4.11.1 - leucyl aminopeptidase and Organism(s) Pyrococcus horikoshii and UniProt Accession O59196

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.11 Aminopeptidases
                3.4.11.1 leucyl aminopeptidase
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This record set is specific for:
Pyrococcus horikoshii
UNIPROT: O59196 not found.
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Word Map
The taxonomic range for the selected organisms is: Pyrococcus horikoshii
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
release of an N-terminal amino acid, Xaa-/-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolysed, but rates on arylamides are exceedingly low
release of an N-terminal amino acid, Xaa-/-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid mides and methyl esters are also readily hydrolysed, but rates on arylamides are exceedingly low
Synonyms
leucine aminopeptidase, erap2, leucyl aminopeptidase, leucine amino peptidase, l-leucine aminopeptidase, leucinaminopeptidase, pilsap, leucine aminopeptidase 3, leucylaminopeptidase, adipocyte-derived leucine aminopeptidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Aminopeptidase A/I
-
-
-
-
cathepsin III
-
-
-
-
cytosol aminopeptidase
-
-
-
-
DR57
-
-
-
-
FTBL proteins
-
-
-
-
L-leucine aminopeptidase
-
-
-
-
LAP
-
-
-
-
leucinamide aminopeptidase
-
-
-
-
leucinaminopeptidase
-
-
-
-
leucine aminopeptidase
-
-
-
-
Leucyl aminopeptidase
-
-
-
-
leucyl peptidase
-
-
-
-
peptidase S
-
-
-
-
proline aminopeptidase
-
-
-
-
Prolyl aminopeptidase
-
-
-
-
proteins, specific or class, FTBL
-
-
-
-
PATHWAY SOURCE
PATHWAYS
CAS REGISTRY NUMBER
COMMENTARY hide
9001-61-0
-
90119-07-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-alanine 4-nitroanilide + H2O
L-alanine + 4-nitroaniline
show the reaction diagram
L-glutamate 4-nitroanilide + H2O
L-glutamate + 4-nitroaniline
show the reaction diagram
about 20% of the activity compared to Leu-4-nitroanilide
-
-
?
L-isoleucine 4-nitroanilide + H2O
L-isoleucine + 4-nitroaniline
show the reaction diagram
14.3% of the activity compared to Leu-4-nitroanilide
-
-
?
L-leucine 4-nitroanilide + H2O
L-leucine + 4-nitroaniline
show the reaction diagram
-
-
-
?
L-leucine 4-nitroanilide + H2O
leucine + 4-nitroaniline
show the reaction diagram
-
-
-
?
L-methionine 4-nitroanilide + H2O
L-methionine + 4-nitroaniline
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
optimally stimulates at 0.5-10 mM
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
bestatin
0.05 mM 35.6% inhibition
EDTA
2 mM, 80% inhibition
Mn2+
0.5 mM, around 50% inhibition
phosphoramidon
1 mM, 25% inhibition
Zn2+
0.5 mM, around 50% inhibition
additional information
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
pH 7.0: about 60% of maximal activity, pH 9.0: about 65% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
475000
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dodecamer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method. The quaternary structure is built by dimers with a length of 100 A that form the edges of the tetrahedron. All 12 active sites are located on the inside of the tetrahedron. Substrate access is granted by pores with a maximal diameter of 10 A, allowing only small peptides and unfolded proteins access to the active site
the crystal structure of of the enzyme is determined at 1.6 A resolution in native form and in complex with the inhibitor amastatin, hanging drop, vapour-diffusion method
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100
half-life: 24.8 min
80
half-life: 10.03 h
90
half-life: 3.0 h
95
half-life: 59.4 min
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Russo, S.; Baumann, U.
Crystal structure of a dodecameric tetrahedral-shaped aminopeptidase
J. Biol. Chem.
279
51275-51281
2004
Pyrococcus horikoshii (O59196), Pyrococcus horikoshii OT-3 (O59196)
Manually annotated by BRENDA team
Dura, M.A.; Receveur-Brechot, V.; Andrieu, J.P.; Ebel, C.; Schoehn, G.; Roussel, A.; Franzetti, B.
Characterization of a TET-like aminopeptidase complex from the hyperthermophilic archaeon Pyrococcus horikoshii
Biochemistry
44
3477-3486
2005
Pyrococcus horikoshii (O59196), Pyrococcus horikoshii, Pyrococcus horikoshii OT-3 (O59196)
Manually annotated by BRENDA team
Borissenko, L.; Groll, M.
Crystal structure of TET protease reveals complementary protein degradation pathways in prokaryotes
J. Mol. Biol.
346
1207-1219
2005
Pyrococcus horikoshii (O59196), Pyrococcus horikoshii OT-3 (O59196)
Manually annotated by BRENDA team