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Information on EC 3.4.11.21 - aspartyl aminopeptidase and Organism(s) Mus musculus and UniProt Accession Q9Z2W0

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.11 Aminopeptidases
                3.4.11.21 aspartyl aminopeptidase
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This record set is specific for:
Mus musculus
UNIPROT: Q9Z2W0 not found.
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Word Map
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
release of an N-terminal aspartate or glutamate from a peptide, with a preference for aspartate
Synonyms
aspartyl aminopeptidase, dnpep, aspap, pfm18aap, peptidase e, acid peptidase, tgaap, m18aap, aspartyl-ap, alpha-aspartyl dipeptidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aspartyl aminopeptidase
-
alpha-aspartyl dipeptidase
-
-
-
-
aminopeptidase A
-
-
-
-
angiotensinase
-
-
-
-
Asp-AP
-
-
aspartate aminopeptidase
-
-
-
-
aspartic aminopeptidase
-
-
-
-
glutamyl aminopeptidase
-
-
-
-
L-aspartate aminopeptidase
-
-
-
-
additional information
-
the enzyme belongs to the peptidase family M18
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
release of an N-terminal aspartate or glutamate from a peptide, with a preference for aspartate
show the reaction diagram
the conserved residues His94, His170, and His440 are essential for activity
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
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
L-aspartyl-beta-naphthylamide + H2O
L-aspartic acid + beta-naphthylamine
show the reaction diagram
-
-
-
?
angiotensin + H2O
Asp + des-Asp-angiotensin
show the reaction diagram
-
metabolism of angiotensin I, angiotensin II, cholecystokinin-8 and neuropeptide, solube and membrane-bound AspAP play different functional roles in the brain
-
?
angiotensin II + H2O
Asp + angiotensin III
show the reaction diagram
-
i.e. Asp-Tyr-Arg-Val-Tyr-Ile-His-Pro-Phe
i.e. Tyr-Arg-Val-Tyr-Ile-His-Pro-Phe
-
?
Asp 2-naphthylamide + H2O
Asp + 2-naphthylamine
show the reaction diagram
-
higher affinity for Asp 2-naphthylamide than for Glu 2-naphthylamide
-
?
Asp-Ala-Pro-chromogen + H2O
Asp + Ala-Pro-chromogen
show the reaction diagram
-
-
-
-
?
Asp-Lys-Ala-Leu + H2O
Asp + Lys-Ala-Leu
show the reaction diagram
-
lower activity
-
-
?
Glu 2-naphthylamide + H2O
Glu + 2-naphthylamine
show the reaction diagram
-
-
-
?
N-(alpha-L-aspartyl)-4-nitroanilide + H2O
L-aspartic acid + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
N-(alpha-L-glutamyl)-2-naphthylamide + H2O
L-glutamic acid + 2-naphthylamine
show the reaction diagram
-
-
-
-
?
N-(alpha-L-glutamyl)-4-nitroanilide + H2O
L-glutamic acid + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
angiotensin + H2O
Asp + des-Asp-angiotensin
show the reaction diagram
-
metabolism of angiotensin I, angiotensin II, cholecystokinin-8 and neuropeptide, solube and membrane-bound AspAP play different functional roles in the brain
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
the enzyme is not affected by chloride ions
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
-
complete inhibition
DTT
-
high inhibition at 1 mM
EDTA
-
weak inhibition
additional information
-
no inhibition by Zn2+ in contrary to glutamyl aminopeptidase, EC 3.4.11.7, no inhibition by Glu-thiol, Asp-thiol, bestatin, amastatin, and puromycin
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
assay at
additional information
-
neutral pH-optimum
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
highest activity for membrane-bound Asp-AP
Manually annotated by BRENDA team
-
high levels for membrane-bound Asp-AP
Manually annotated by BRENDA team
-
highest activity for soluble Asp-AP
Manually annotated by BRENDA team
additional information
-
broad tissue distribution
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DNPEP_MOUSE
473
0
52207
Swiss-Prot
Mitochondrion (Reliability: 3)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ramirez-Exposito, M.J.; Martinez, J.M.; Prieto, I.; Alba, F.; Ramirez, M.
Comparative distribution of glutamyl and aspartyl aminopeptidase activities in mouse organs
Horm. Metab. Res.
32
161-163
2000
Mus musculus
Manually annotated by BRENDA team
Adang, M.J.
Aminopeptidase A
Handbook of Proteolytic Enzymes (2nd Edition)
1
299-303
2004
Mus musculus
-
Manually annotated by BRENDA team
Simmons, W.H.
Aspartyl aminopeptidase
Handbook of Proteolytic Enzymes (2nd Edition)
1
937-939
2004
Oryctolagus cuniculus, Homo sapiens, Mus musculus
-
Manually annotated by BRENDA team
Cai, W.W.; Wang, L.; Chen, Y.
Aspartyl aminopeptidase, encoded by an evolutionarily conserved syntenic gene, is colocalized with its cluster in secretory granules of pancreatic islet cells
Biosci. Biotechnol. Biochem.
74
2050-2055
2010
Mus musculus (Q9Z2W0)
Manually annotated by BRENDA team