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Information on EC 3.4.11.7 - glutamyl aminopeptidase and Organism(s) Plasmodium falciparum and UniProt Accession Q8I2J3

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.11 Aminopeptidases
                3.4.11.7 glutamyl aminopeptidase
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This record set is specific for:
Plasmodium falciparum
UNIPROT: Q8I2J3 not found.
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Word Map
The taxonomic range for the selected organisms is: Plasmodium falciparum
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
release of N-terminal glutamate (and to a lesser extent aspartate) from a peptide
Synonyms
aminopeptidase a, angiotensinase, lap-a, gluap, glutamyl aminopeptidase, angiotensinase a, aspartyl-aminopeptidase, aminopeptidase-a, glutamyl-aminopeptidase, aspartate aminopeptidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aspartyl aminopeptidase
-
M18 aspartyl aminopeptidase
-
aminopeptidase A
-
-
-
-
aminopeptidase, aspartate
-
-
-
-
angiotensinase A
-
-
-
-
APA
-
-
-
-
aspartate aminopeptidase
-
-
-
-
BP-1/6C3 antigen
-
-
-
-
Ca2+-activated glutamate aminopeptidase
-
-
-
-
Differentiation antigen gp160
-
-
-
-
EAP
-
-
-
-
glutamyl aminopeptidase
-
-
-
-
glutamyl peptidase
-
-
-
-
L-alpha-aspartyl(L-alpha-glutamyl)-peptide hydrolase
-
-
-
-
L-aspartate aminopeptidase
-
-
-
-
membrane aminopeptidase II
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -
CAS REGISTRY NUMBER
COMMENTARY hide
9074-83-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Asp-7-amido-4-methylcoumarin + H2O
Asp + 7-amino-4-methylcoumarin
show the reaction diagram
assay for measuring aspartyl aminopeptidase activity
-
-
?
Glu-7-amido-4-methylcoumarin + H2O
Glu + 7-amino-4-methylcoumarin
show the reaction diagram
assay for measuring aspartyl aminopeptidase activity
-
-
?
Leu-7-amido-4-methylcoumarin + H2O
Leu + 7-amino-4-methylcoumarin
show the reaction diagram
assay for measuring aspartyl aminopeptidase activity
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(1-aminopropane-1,3-diyl)bis(phosphonic acid)
-
(3R)-3-amino-3-phosphonopropanoic acid
-
3-amino-3-[hydroxy(phenyl)phosphoryl]propanoic acid
-
3-[(1-amino-2-carboxyethyl)(hydroxy)phosphoryl]-2-methylpropanoic acid
-
3-[[amino(carboxy)methyl](hydroxy)phosphoryl]-2-methylpropanoic acid
-
5-amino-5-phosphonopentanoic acid
-
amino(phosphono)acetic acid
-
amino[hydroxy(methyl)phosphoryl]acetic acid
-
EDTA
activity is reduced to 14% after incubating with 10 mM EDTA
o-phenanthroline
activity is reduced to 8.3% after incubating with 20 mM o-phenanthroline
Zn2+
Zn2+ abolishes enzyme activity at a concentration of 1 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.3273 - 0.3848
Asp-7-amido-4-methylcoumarin
0.1351 - 0.1363
Glu-7-amido-4-methylcoumarin
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.05 - 0.354
Asp-7-amido-4-methylcoumarin
0.011 - 0.33
Glu-7-amido-4-methylcoumarin
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0044
(1-aminopropane-1,3-diyl)bis(phosphonic acid)
-
0.00034
(3R)-3-amino-3-phosphonopropanoic acid
-
2
3-amino-3-[hydroxy(phenyl)phosphoryl]propanoic acid
-
0.0427
3-[(1-amino-2-carboxyethyl)(hydroxy)phosphoryl]-2-methylpropanoic acid
-
0.1831
3-[[amino(carboxy)methyl](hydroxy)phosphoryl]-2-methylpropanoic acid
-
0.105
5-amino-5-phosphonopentanoic acid
-
0.0271
amino(phosphono)acetic acid
-
0.395
amino[hydroxy(methyl)phosphoryl]acetic acid
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
607
Glu-7-amido-4-methylcoumarin
662.5
Asp-7-amido-4-methylcoumarin
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
activity assay
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
activity assay
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
560000
octamer, determined by gel filtration HPLC on a Superdex-200 column
65000
determined by reducing SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by affinity chromatography on a Ni-NTA column
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
using codons for optimized gene expression in the yeast Pichia pastoris, for protein expression Sf9 insect cells are infected with PfM18AAP recombinant Baculovirus, furthermore pGEM, pHGFPB and pHcmycB are used
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
enzyme is a promising target for new anti-malarial drug development
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Teuscher, F.; Lowther, J.; Skinner-Adams, T.S.; Spielmann, T.; Dixon, M.W.; Stack, C.M.; Donnelly, S.; Mucha, A.; Kafarski, P.; Vassiliou, S.; Gardiner, D.L.; Dalton, J.P.; Trenholme, K.R.
The M18 aspartyl aminopeptidase of the human malaria parasite Plasmodium falciparum
J. Biol. Chem.
282
30817-30826
2007
Plasmodium falciparum (Q8I2J3), Plasmodium falciparum
Manually annotated by BRENDA team