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Enzyme Nomenclature
Information on EC 3.4.11.7 - glutamyl aminopeptidase
for references in articles please use BRENDA:EC3.4.11.7
Word Map on EC 3.4.11.7
- 3.4.11.7
- apa
-
aminopeptidases
-
renin-angiotensin
- hypertension
-
dipeptidyl
- renin
- amastatin
- border
-
brush
- bestatin
-
angiotensin-converting
-
antihypertensive
- vasopressin
-
alanyl
- losartan
-
pressor
- metallopeptidase
-
angii
- angiotensinogen
-
dipeptidylpeptidase
-
exopeptidase
- medicine
- beta-naphthylamide
-
arylamide
-
ectoenzyme
-
3.2.1.20
- lactase
- microvillar
-
kininase
-
intracerebroventricularly
- sucrase-isomaltase
- oxytocinase
-
ras-regulating
- drug development
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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EC NUMBER 
COMMENTARY 
3.4.11.7
-
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RECOMMENDED NAME
GeneOntology No.
glutamyl aminopeptidase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
release of N-terminal glutamate (and to a lesser extent aspartate) from a peptide
-
-
-
-
release of N-terminal glutamate (and to a lesser extent aspartate) from a peptide
active site structure and organization
-
release of N-terminal glutamate (and to a lesser extent aspartate) from a peptide
active site structure and organization, modeling, residues Glu352, Glu386, Tyr471, and Glu408 are important in catalysis
-
release of N-terminal glutamate (and to a lesser extent aspartate) from a peptide
active site structure and organization
-
release of N-terminal glutamate (and to a lesser extent aspartate) from a peptide
active site structure and organization
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis
hydrolysis of peptide bond
hydrolysis of peptide bond
-
-
hydrolysis of peptide bond
-
-
exopeptidase, N-terminus, amino acid
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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CAS REGISTRY NUMBER
COMMENTARY
9074-83-3
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
35868, 36013, 36017, 36018, 36019, 36027, 36032, 36036, 663609, 665010, 665723, 666460, 680004, 683508, 683663, 698166, 699650, 731548, 732286
-
-
and strains DBPZ1010, DBPZ1017, DBPZ1018, DBPZ1020, DBPZ1024
-
-
and strains DBPZ0988, DBPZ0989, DBPZ0990, DBPZ0991, DBPZ0992, DBPZ0993, DBPZ0998, DBPZ0999, DBPZ1002, DBPZ1003, DBPZ1008, DBPZ1011, DBPZ1012, DBPZ1014, DBPZ1015, DBPZ1019, DBPZ1021, DBPZ1023, DBPZ1025
-
-
and strains DBPZ0988, DBPZ0989, DBPZ0990, DBPZ0991, DBPZ0992, DBPZ0993, DBPZ0998, DBPZ0999, DBPZ1002, DBPZ1003, DBPZ1008, DBPZ1011, DBPZ1012, DBPZ1014, DBPZ1015, DBPZ1019, DBPZ1021, DBPZ1023, DBPZ1025
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-
and strains DBPZ0986, DBPZ0995, DBPZ1005, DBPZ1016, DBPZ1026, DBPZ102
-
-
and strains DBPZ0986, DBPZ0995, DBPZ1005, DBPZ1016, DBPZ1026, DBPZ102
-
-
-
-
-
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SwissProt
-
-
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hypertensive DOCA-salt rat, for the on vitro activity assay recombinant mouse APA is used
-
-
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
enzyme acts as a multifunctional adhesin, binding to both heparin and plasminogen. It binds plasminogen and facilitates its activation by tissue plasminogen activator. Plasmin cleaves host extracellular matrix proteins and activates matrix metalloproteases, generating peptide substrates for the enzyme and a source of amino acids for growth of Mycoplasma hyopneumoniae
physiological function
-
enzyme acts as a multifunctional adhesin, binding to both heparin and plasminogen. It binds plasminogen and facilitates its activation by tissue plasminogen activator. Plasmin cleaves host extracellular matrix proteins and activates matrix metalloproteases, generating peptide substrates for the enzyme and a source of amino acids for growth of Mycoplasma hyopneumoniae
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
angiotensin I + H2O
Asp + Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu
-
-
-
-
?
angiotensin III + H2O
? + angiotensin IV
-
i.e. Tyr-Arg-Val-Tyr-Ile-His-Pro-Phe, low activity in absence of Ca2+
-
-
?
Asp-4-methylcoumaryl-7-amide + H2O
Asp + 7-amino-4-methylcoumarin
-
low activity in absence and presence of Ca2+
-
-
?
Asp-7-amido-4-methylcoumarin + H2O
Asp + 7-amino-4-methylcoumarin
Q8I2J3;
assay for measuring aspartyl aminopeptidase activity
-
-
?
chromogranin A + H2O
Glu + EEEEMAVVPQGLFRG-NH2
-
i.e. EEEEEMAVVPQGLFRG-NH2
-
-
?
Gln-4-methylcoumaryl-7-amide + H2O
Gln + 7-amino-4-methylcoumarin
-
low activity in absence and presence of Ca2+
-
-
?
Glu-7-amido-4-methylcoumarin + H2O
Glu + 7-amino-4-methylcoumarin
Q8I2J3;
assay for measuring aspartyl aminopeptidase activity
-
-
?
kallidin + H2O
Lys + bradykinin
-
i.e. Lys-bradykinin or KRPPGFSPFR, the reaction is performed only in absence of Ca2+
i.e. RPPGFSPFR
-
?
Leu-7-amido-4-methylcoumarin + H2O
Leu + 7-amino-4-methylcoumarin
Q8I2J3;
assay for measuring aspartyl aminopeptidase activity
-
-
?
N-Glu-L-Phe-4-nitroanilide + H2O
L-Glu + L-Phe-4-nitroanilide
-
-
-
-
?
angiotensin II + H2O
angiotensin III + Arg
-
i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe
i.e. Arg-Val-Tyr-Ile-His-Pro-Phe
-
ir
angiotensin II + H2O
angiotensin III + Arg
-
i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe
i.e. Arg-Val-Tyr-Ile-His-Pro-Phe
-
ir
angiotensin II + H2O
angiotensin III + Arg
-
i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe
i.e. Arg-Val-Tyr-Ile-His-Pro-Phe
-
ir
angiotensin II + H2O
angiotensin III + Arg
-
i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe
i.e. Arg-Val-Tyr-Ile-His-Pro-Phe
-
ir
angiotensin II + H2O
Asp + angiotensin III
-
angiotensin is the most active compound of the renin-angiotensin-system, RAS, involved in regulation of blood pressure in the brain
-
-
?
angiotensin II + H2O
Asp + angiotensin III
-
i.e. Asp-Tyr-Arg-Val-Tyr-Ile-His-Pro-Phe
i.e. Tyr-Arg-Val-Tyr-Ile-His-Pro-Phe
-
?
angiotensin II + H2O
Asp + angiotensin III
-
angiotensin is the most active compound of the renin-angiotensin-system, RAS, involved in renal development
-
-
?
angiotensin II + H2O
Asp + angiotensin III
-
i.e. Asp-Tyr-Arg-Val-Tyr-Ile-His-Pro-Phe
i.e. Tyr-Arg-Val-Tyr-Ile-His-Pro-Phe
-
?
angiotensin II + H2O
Asp + angiotensin III
-
the enzyme is responsible for the convertion of angiotensin II into angiotensin III in the brain
-
-
?
angiotensin II + H2O
Asp + angiotensin III
-
angiotensin is the most active compound of the renin-angiotensin-system, RAS, involved in renal development
-
-
?
angiotensin II + H2O
Asp + angiotensin III
-
i.e. Asp-Tyr-Arg-Val-Tyr-Ile-His-Pro-Phe
i.e. Tyr-Arg-Val-Tyr-Ile-His-Pro-Phe
-
?
angiotensin II + H2O
Asp + angiotensin III
-
angiotensin II is the principal effector of the renin-angiotensin-system, RAS, which induces vasoconstriction and increases sodium and water retention thereby leading to increased blood pressure
-
-
?
angiotensin II + H2O
Asp + angiotensin III
-
aspartyl aminopeptidase and several other aminopeptidases, i.e. angiotensinases, are involved in angiotensin II and cholecystokinin, CCK, metabolism, angiotensin II is the principal effector of the renin-angiotensin-system, RAS, which induces vasoconstriction and increases sodium and water retention thereby leading to increased blood pressure
-
-
?
angiotensin II + H2O
Asp + angiotensin III
-
i.e. Asp-Tyr-Arg-Val-Tyr-Ile-His-Pro-Phe
i.e. Tyr-Arg-Val-Tyr-Ile-His-Pro-Phe
-
?
angiotensin II + H2O
aspartic acid + angiotensin III
-
angiotensin II: Asp-Arg-Val-Tyr-Ile-His-Pro-Phe
angiotensin III: Arg-Val-Tyr-Ile-His-Pro-Phe
-
?
angiotensin II + H2O
aspartic acid + angiotensin III
-
angiotensin II: Asp-Arg-Val-Tyr-Ile-His-Pro-Phe
angiotensin III: Arg-Val-Tyr-Ile-His-Pro-Phe
-
?
angiotensin II + H2O
aspartic acid + angiotensin III
-
angiotensin II: Asp-Arg-Val-Tyr-Ile-His-Pro-Phe
angiotensin III: Arg-Val-Tyr-Ile-His-Pro-Phe
-
?
angiotensin II + H2O
aspartic acid + angiotensin III
-
angiotensin II: Asp-Arg-Val-Tyr-Ile-His-Pro-Phe
angiotensin III: Arg-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe
-
?
angiotensin III + H2O
angiotensin IV + Arg
-
the enzyme is involved in regulation of blood pressure in the renin-angiotensin system in the brain causing hypertension
-
-
ir
angiotensin III + H2O
angiotensin IV + Arg
-
the enzyme is involved in regulation of blood pressure in the renin-angiotensin system in the brain causing hypertension
-
-
ir
angiotensin III + H2O
angiotensin IV + Arg
-
the enzyme is involved in regulation of blood pressure in the renin-angiotensin system in the brain causing hypertension
-
-
ir
angiotensin III + H2O
angiotensin IV + Arg
-
the enzyme is involved in regulation of blood pressure in the renin-angiotensin system in the brain causing hypertension
-
-
ir
Asp-beta-naphthylamide + H2O
Asp + naphthylamine
-
dog kidney enzyme 3 times more active compared to Glu-beta-naphthylamide
-
-
?
Glu-2-naphthylamide + H2O
Glu + 2-naphthylamine
-
synthetic substrate used in the activity assay
-
-
?
Glu-2-naphthylamide + H2O
Glu + 2-naphthylamine
-
synthetic substrate used in the activity assay
-
-
?
Glu-4-methylcoumaryl-7-amide + H2O
Glu + 7-amino-4-methylcoumarin
-
low activity in absence of Ca2+
-
-
?
Glu-7-amido-4-methylcoumarin + H2O
Gln + 7-amino-4-methylcoumarin
-
-
-
-
?
Glu-7-amido-4-methylcoumarin + H2O
Gln + 7-amino-4-methylcoumarin
-
activity assay
-
-
?
Glu-7-amido-4-methylcoumarin + H2O
Gln + 7-amino-4-methylcoumarin
-
-
-
-
?
Glu-beta-naphthylamide + H2O
Glu + naphthylamine
-
aminopeptidase A six times more active compared to Asp-beta-naphthylamide
-
-
?
Glu-p-nitroanilide + H2O
Glu + 4-nitroaniline
-
peptidase activity assay
-
-
?
Glu-p-nitroanilide + H2O
Glu + 4-nitroaniline
-
peptidase activity assay
-
-
?
Glu-p-nitroanilide + H2O
Glu + p-nitroaniline
-
activity assay, cleaved p-nitroanilide is measured
-
-
?
Glu-p-nitroanilide + H2O
glutamic acid + p-nitroaniline
-
peptidase activity assay
-
-
?
Glu-p-nitroanilide + H2O
glutamic acid + p-nitroaniline
-
peptidase activity assay
-
-
?
Glu-p-nitroanilide + H2O
glutamic acid + p-nitroaniline
-
peptidase activity assay
-
-
?
Glu-p-nitroanilide + H2O
glutamic acid + p-nitroaniline
-
peptidase activity assay
-
-
?
Glu-p-nitroanilide + H2O
glutamic acid + p-nitroaniline
-
peptidase activity assay
-
-
?
Glu-p-nitroanilide + H2O
glutamic acid + p-nitroaniline
-
peptidase activity assay
-
-
?
Glu-p-nitroanilide + H2O
glutamic acid + p-nitroaniline
-
peptidase activity assay
-
-
?
Glu-p-nitroanilide + H2O
glutamic acid + p-nitroaniline
-
peptidase activity assay
-
-
?
Glu-p-nitroanilide + H2O
glutamic acid + p-nitroaniline
-
peptidase activity assay
-
-
?
L-Ala-4-methylcoumaryl-7-amide + H2O
L-Ala + 7-amino-4-methylcoumarin
about 50% of the activity with L-Glu-4-methylcoumaryl-7-amide
-
-
?
L-Ala-4-methylcoumaryl-7-amide + H2O
L-Ala + 7-amino-4-methylcoumarin
about 50% of the activity with L-Glu-4-methylcoumaryl-7-amide
-
-
?
L-Asp-peptide + H2O
L-Asp + peptide
-
free gamma-carboxyl group of N-terminal amino acid essential
-
-
?
L-Asp-peptide + H2O
L-Asp + peptide
-
specificity for di- and tri-peptides with Asp or Glu at N-terminal end
-
-
?
L-Glu-4-methylcoumaryl-7-amide + H2O
L-Glu + 7-amino-4-methylcoumarin
-
-
-
?
L-Glu-4-methylcoumaryl-7-amide + H2O
L-Glu + 7-amino-4-methylcoumarin
-
-
-
?
L-Glu-7-amido-4-methylcoumarin + H2O
L-Glu + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Glu-peptide + H2O
L-Glu + peptide
-
specificity for di-and tripeptides with Asp or Glu at N-terminal end
-
-
?
L-Leu-4-methylcoumaryl-7-amide + H2O
L-Leu + 7-amino-4-methylcoumarin
-
about 20% of the activity with L-Glu-4-methylcoumaryl-7-amide
-
?
L-Leu-4-methylcoumaryl-7-amide + H2O
L-Leu + 7-amino-4-methylcoumarin
-
about 20% of the activity with L-Glu-4-methylcoumaryl-7-amide
-
?
N-(alpha-L-aspartyl)-2-naphthylamide + H2O
L-aspartic acid + 2-naphthylamine
-
-
-
-
?
N-(alpha-L-aspartyl)-2-naphthylamide + H2O
L-aspartic acid + 2-naphthylamine
-
-
-
-
?
N-(alpha-L-aspartylyl)-2-naphthylamide + H2O
L-aspartic acid + 2-naphthylamine
-
-
-
-
?
N-(alpha-L-aspartylyl)-2-naphthylamide + H2O
L-aspartic acid + 2-naphthylamine
-
-
-
-
?
N-(alpha-L-aspartylyl)-2-naphthylamide + H2O
L-aspartic acid + 2-naphthylamine
-
-
-
-
?
N-(alpha-L-aspartylyl)-2-naphthylamide + H2O
L-aspartic acid + 2-naphthylamine
-
-
-
-
?
N-(alpha-L-glutamyl)-2-naphthylamide + H2O
L-glutamic acid + 2-naphthylamine
-
-
-
-
?
N-(alpha-L-glutamyl)-2-naphthylamide + H2O
L-glutamic acid + 2-naphthylamine
-
-
-
-
?
N-(alpha-L-glutamyl)-2-naphthylamide + H2O
L-glutamic acid + 2-naphthylamine
-
-
-
-
?
N-(alpha-L-glutamyl)-2-naphthylamide + H2O
L-glutamic acid + 2-naphthylamine
-
-
-
-
?
N-(alpha-L-glutamyl)-4-nitroanilide + H2O
L-glutamic acid + 4-nitroaniline
-
-
-
-
?
N-(alpha-L-glutamyl)-4-nitroanilide + H2O
L-glutamic acid + 4-nitroaniline
-
-
-
-
?
N-(alpha-L-glutamyl)-4-nitroanilide + H2O
L-glutamic acid + 4-nitroaniline
-
-
-
-
?
N-(alpha-L-glutamyl)-beta-naphthylamide + H2O
L-glutamic acid + beta-naphthylamine
-
-
-
-
?
N-(alpha-L-glutamyl)-beta-naphthylamide + H2O
L-glutamic acid + beta-naphthylamine
-
-
-
-
?
N-(alpha-L-glutamyl)-beta-naphthylamide + H2O
L-glutamic acid + beta-naphthylamine
-
-
-
-
?
additional information
?
-
-
the enzyme catalyzes the hydrolysis of N-(alpha-L-glutamyl)- moieties more efficiently than the hydrolysis of alpha-L-aspartyl derivatives
-
-
-
additional information
?
-
-
slow hydrolysis of Ala-beta-naphthylamide, Arg-beta-naphthylamide
-
-
-
additional information
?
-
-
the enzyme catalyses the hydrolysis of N-terminal glutamic or aspartic acid residues from regulatory peptides, the enzyme is involved in metabolism of angiotensin II and angiotensin III in the brain, overview
-
-
-
additional information
?
-
-
substrate specificity in presence or absence of Ca2+
-
-
-
additional information
?
-
-
substrate specificity, overview, the enzyme catalyses the hydrolysis of N-terminal glutamic or aspartic acid residues from regulatory peptides
-
-
-
additional information
?
-
-
potential biological functions, overview
-
-
-
additional information
?
-
-
the enzyme removes N-terminal Glu, Asp, and to a lesser extent also Ser residues from peptide substrates, no activity with Glu-substrate with a blocked N-terminus
-
-
-
additional information
?
-
-
potential biological functions, overview
-
-
-
additional information
?
-
-
the enzyme removes N-terminal Glu, Asp, and to a lesser extent also Ser residues from peptide substrates
-
-
-
additional information
?
-
-
association between elevated BP-1 expression and cell growth. The enzyme is not involved in immune system development
-
-
-
additional information
?
-
-
the S1' subsite is hydrophobic whereas the S2' subsite recognizes preferentially negatively charged residues derived from aspartic acid
-
-
-
additional information
?
-
-
The C-terminal domain of aminopeptidase A is an intramolecular chaperone required for the correct folding, cell surface expression, and activity of the enzyme
-
-
-
additional information
?
-
-
the enzyme catalyses the hydrolysis of N-terminal glutamic or aspartic acid residues from regulatory peptides, the enzyme is involved in metabolism of angiotensin II and angiotensin III in the brain, overview
-
-
-
additional information
?
-
-
the enzyme is involved in angiotensin metabolism
-
-
-
additional information
?
-
-
the enzyme is involved in conversion of angiotensin II to angiotensin III and thus in controlling of vasopressin release and blood pressure, overview
-
-
-
additional information
?
-
-
substrate specificity, overview, the enzyme catalyses the hydrolysis of N-terminal glutamic or aspartic acid residues from regulatory peptides
-
-
-
additional information
?
-
-
the enzyme catalyzes the hydrolysis of N-(alpha-L-glutamyl)- moieties more efficiently than the hydrolysis of alpha-L-aspartyl derivatives
-
-
-
additional information
?
-
-
administration of purified enzyme into hypertensive rats leads to a decrease in blood pressure, while enzyme inhibition increases blood pressure
-
-
-
additional information
?
-
-
the enzyme catalyses the hydrolysis of N-terminal glutamic or aspartic acid residues from regulatory peptides, the enzyme is involved in metabolism of angiotensin II and angiotensin III in the brain, overview
-
-
-
additional information
?
-
-
the enzyme is involved in conversion of angiotensin II to angiotensin III and thus in controlling of vasopressin release and blood pressure, overview
-
-
-
additional information
?
-
-
substrate specificity, overview, the enzyme catalyses the hydrolysis of N-terminal glutamic or aspartic acid residues from regulatory peptides
-
-
-
additional information
?
-
-
the enzyme catalyzes the hydrolysis of N-(alpha-L-glutamyl)- moieties more efficiently than the hydrolysis of alpha-L-aspartyl derivatives
-
-
-
additional information
?
-
-
potential biological functions, overview
-
-
-
additional information
?
-
-
the enzyme removes N-terminal Glu, Asp, and to a lesser extent also Ser residues from peptide substrates
-
-
-
additional information
?
-
-
potential biological functions, overview
-
-
-
additional information
?
-
-
the enzyme removes N-terminal Glu, Asp, and to a lesser extent also Ser residues from peptide substrates
-
-
-
additional information
?
-
-
potential biological functions, overview
-
-
-
additional information
?
-
-
the enzyme removes N-terminal Glu, Asp, and to a lesser extent also Ser residues from peptide substrates
-
-
-
additional information
?
-
-
potential biological functions, overview
-
-
-
additional information
?
-
-
the enzyme removes N-terminal Glu, Asp, and to a lesser extent also Ser residues from peptide substrates
-
-
-
additional information
?
-
-
potential biological functions, overview
-
-
-
additional information
?
-
-
the enzyme removes N-terminal Glu, Asp, and to a lesser extent also Ser residues from peptide substrates
-
-
-
additional information
?
-
-
the enzyme catalyses the hydrolysis of N-terminal glutamic or aspartic acid residues from regulatory peptides, the enzyme is involved in metabolism of angiotensin II and angiotensin III in the brain, overview
-
-
-
additional information
?
-
-
substrate specificity, overview, the enzyme catalyses the hydrolysis of N-terminal glutamic or aspartic acid residues from regulatory peptides
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
angiotensin II + H2O
Asp + angiotensin III
-
angiotensin is the most active compound of the renin-angiotensin-system, RAS, involved in regulation of blood pressure in the brain
-
-
?
angiotensin II + H2O
Asp + angiotensin III
-
angiotensin is the most active compound of the renin-angiotensin-system, RAS, involved in renal development
-
-
?
angiotensin II + H2O
Asp + angiotensin III
-
the enzyme is responsible for the convertion of angiotensin II into angiotensin III in the brain
-
-
?
angiotensin II + H2O
Asp + angiotensin III
-
angiotensin is the most active compound of the renin-angiotensin-system, RAS, involved in renal development
-
-
?
angiotensin II + H2O
Asp + angiotensin III
-
angiotensin II is the principal effector of the renin-angiotensin-system, RAS, which induces vasoconstriction and increases sodium and water retention thereby leading to increased blood pressure
-
-
?
angiotensin II + H2O
Asp + angiotensin III
-
aspartyl aminopeptidase and several other aminopeptidases, i.e. angiotensinases, are involved in angiotensin II and cholecystokinin, CCK, metabolism, angiotensin II is the principal effector of the renin-angiotensin-system, RAS, which induces vasoconstriction and increases sodium and water retention thereby leading to increased blood pressure
-
-
?
angiotensin II + H2O
aspartic acid + angiotensin III
-
angiotensin II: Asp-Arg-Val-Tyr-Ile-His-Pro-Phe
angiotensin III: Arg-Val-Tyr-Ile-His-Pro-Phe
-
?
angiotensin II + H2O
aspartic acid + angiotensin III
-
angiotensin II: Asp-Arg-Val-Tyr-Ile-His-Pro-Phe
angiotensin III: Arg-Val-Tyr-Ile-His-Pro-Phe
-
?
angiotensin II + H2O
aspartic acid + angiotensin III
-
angiotensin II: Asp-Arg-Val-Tyr-Ile-His-Pro-Phe
angiotensin III: Arg-Val-Tyr-Ile-His-Pro-Phe
-
?
angiotensin III + H2O
angiotensin IV + Arg
-
the enzyme is involved in regulation of blood pressure in the renin-angiotensin system in the brain causing hypertension
-
-
ir
angiotensin III + H2O
angiotensin IV + Arg
-
the enzyme is involved in regulation of blood pressure in the renin-angiotensin system in the brain causing hypertension
-
-
ir
angiotensin III + H2O
angiotensin IV + Arg
-
the enzyme is involved in regulation of blood pressure in the renin-angiotensin system in the brain causing hypertension
-
-
ir
angiotensin III + H2O
angiotensin IV + Arg
-
the enzyme is involved in regulation of blood pressure in the renin-angiotensin system in the brain causing hypertension
-
-
ir
additional information
?
-
-
the enzyme catalyses the hydrolysis of N-terminal glutamic or aspartic acid residues from regulatory peptides, the enzyme is involved in metabolism of angiotensin II and angiotensin III in the brain, overview
-
-
-
additional information
?
-
-
potential biological functions, overview
-
-
-
additional information
?
-
-
potential biological functions, overview
-
-
-
additional information
?
-
-
association between elevated BP-1 expression and cell growth. The enzyme is not involved in immune system development
-
-
-
additional information
?
-
-
The C-terminal domain of aminopeptidase A is an intramolecular chaperone required for the correct folding, cell surface expression, and activity of the enzyme
-
-
-
additional information
?
-
-
the enzyme catalyses the hydrolysis of N-terminal glutamic or aspartic acid residues from regulatory peptides, the enzyme is involved in metabolism of angiotensin II and angiotensin III in the brain, overview
-
-
-
additional information
?
-
-
the enzyme is involved in angiotensin metabolism
-
-
-
additional information
?
-
-
the enzyme is involved in conversion of angiotensin II to angiotensin III and thus in controlling of vasopressin release and blood pressure, overview
-
-
-
additional information
?
-
-
administration of purified enzyme into hypertensive rats leads to a decrease in blood pressure, while enzyme inhibition increases blood pressure
-
-
-
additional information
?
-
-
the enzyme catalyses the hydrolysis of N-terminal glutamic or aspartic acid residues from regulatory peptides, the enzyme is involved in metabolism of angiotensin II and angiotensin III in the brain, overview
-
-
-
additional information
?
-
-
the enzyme is involved in conversion of angiotensin II to angiotensin III and thus in controlling of vasopressin release and blood pressure, overview
-
-
-
additional information
?
-
-
potential biological functions, overview
-
-
-
additional information
?
-
-
potential biological functions, overview
-
-
-
additional information
?
-
-
potential biological functions, overview
-
-
-
additional information
?
-
-
potential biological functions, overview
-
-
-
additional information
?
-
-
potential biological functions, overview
-
-
-
additional information
?
-
-
the enzyme catalyses the hydrolysis of N-terminal glutamic or aspartic acid residues from regulatory peptides, the enzyme is involved in metabolism of angiotensin II and angiotensin III in the brain, overview
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ba2+
Ca2+
Co2+
Mn2+
Sr2+
Zinc
-
zinc-dependent metalloprotease, activity requires the HEXXH zinc-binding motif
Zn2+
additional information
Ca2+
-
activates activity with some substrates, decreases activity with other substrates, required for activity with Asp-/Glu-substrates, regulatory function and influence on substrate specificity
Ca2+
-
7.3fold increase of ratio of turnover number to Km-value for the wild-type enzyme. Activity of mutant enzyme H450F is not measurable in absence of Ca2+. His450 together with Ca2+ may contribute to substrate specificity
Ca2+
-
each APA monomer contains one Ca2+ atom, Ca2+ (from 0 to 4 mM) increases the activity of the wild type enzyme
Ca2+
-
the presence of 4 mM Ca2+ enhances the enzymatic activity of wild type enzyme by a factor of 8
Zn2+
-
zinc-metallopeptidase, inhibits the activity with Glu- and Gln-substrates
Zn2+
-
zinc-metallopeptidase, the enzyme contains the zinc-binding motif HEXXH residues 385-389 with catalytically important Glu386
Zn2+
-
zinc-metallopeptidase, the enzyme contains the zinc-binding motif HEXXH
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3-amino-4-thio-butyl sulfonic acid
-
EC33, specific and selective APA inhibitor
3-[(1-amino-2-carboxyethyl)(hydroxy)phosphoryl]-2-methylpropanoic acid
Q8I2J3;
-
3-[[amino(carboxy)methyl](hydroxy)phosphoryl]-2-methylpropanoic acid
Q8I2J3;
-
angiotensin II
-
competitive against Glu-4-methylcoumaryl-7-amide, IC50 is 0.065 mM in presence of Ca2+
cholecystokinin-8
-
competitive against Glu-4-methylcoumaryl-7-amide, IC50 is 0.024 mM in presence of Ca2+
chromogranin A
-
competitive against Glu-4-methylcoumaryl-7-amide, IC50 is 0.049 mM in presence of Ca2+
-
neurokinin B
-
competitive against Glu-4-methylcoumaryl-7-amide,IC50 is 0.060 mM in presence of Ca2+
[Ag2(E-6-(hydroxyimino)ethyl-1,3,7-trimethyl-pteridine-2,4(1H,3H)-dione)2(CF3SO3)2(EtOH)]n x nEtOH
-
compound shows cytotoxicity against both U373-MG abd NB-69 cell lines. NB-69 cells need higher concentrations of silver complexes than U373-MG cells to obtain a 50% growth inhibition. All compounds tested show apoptotic effects, with U373-MG cells being more susceptible. The silver complexes tested also show a dose-dependent inhibitory effect on aminopeptidase A activity in NB-69 and U373-MG cells, although U373-MG cells are more sensitive
-
[Ag2(E-6-(hydroxyimino)ethyl-1,3,7-trimethyl-pteridine-2,4(1H,3H)-dione)2(ClO4)2]n
-
compound shows cytotoxicity against both U373-MG abd NB-69 cell lines. NB-69 cells need higher concentrations of silver complexes than U373-MG cells to obtain a 50% growth inhibition. All compounds tested show apoptotic effects, with U373-MG cells being more susceptible. The silver complexes tested also show a dose-dependent inhibitory effect on aminopeptidase A activity in NB-69 and U373-MG cells, although U373-MG cells are more sensitive
-
[Ag2(E-6-(hydroxyimino)ethyl-1,3,7-trimethyl-pteridine-2,4(1H,3H)-dione)2(NO3)2]n
-
compound shows cytotoxicity against both U373-MG abd NB-69 cell lines. NB-69 cells need higher concentrations of silver complexes than U373-MG cells to obtain a 50% growth inhibition. All compounds tested show apoptotic effects, with U373-MG cells being more susceptible. The silver complexes tested also show a dose-dependent inhibitory effect on aminopeptidase A activity in NB-69 and U373-MG cells, although U373-MG cells are more sensitive
-
[[(2R,3R)-3-amino-2-sulfhydryl-5-sulfonate]pentanoyl]-Tyr-homosulfoalanine-OH
-
-
[[(2S,3R)-3-amino-2-sulfhydryl-5-sulfonate]pentanoyl]-Tyr-homosulfoalanine-OH
-
-
additional information
-
inhibitory effects of peptide hormones on enzyme activity in presence or absence of Ca2+, overview, no or poor inhibition by 4-(amidinophenyl)-methanesulfonyl fluoride, pepstatin, and bestatin
-
(S)-3-amino-4-mercapto-butylsulfonic acid
-
specific and selective aminopeptidase A inhibitor
(S)-3-amino-4-mercapto-butylsulfonic acid
-
specific and selective APA inhibitor
(S)-3-amino-4-mercaptobutyl sulfonic acid
-
EC33, specific and selective APA inhibitor
(S)-3-amino-4-mercaptobutyl sulfonic acid
-
EC33, specific and selective APA inhibitor
4,4'-dithio[bis(3)-aminobutylsulfonic acid]
-
RB150, a prodrug of EC33
amastatin
-
inhibits the enzyme and blocks the metabolism of brain angiotensin II and III
amastatin
-
inhibits the enzyme and blocks the metabolism of brain angiotensin II and III
amastatin
-
inhibits the enzyme and blocks the metabolism of brain angiotensin II and III
amastatin
-
an APA inhibitor, enzyme inhibition leads to increased blood pressure
amastatin
-
inhibits the enzyme and blocks the metabolism of brain angiotensin II and III
angiotensin IV
-
competitive feedback inhibition, negative regulatory function in absence or presence of Ca2+; IC50 is 0.010 mM
bestatin
-
inhibits the enzyme and blocks the metabolism of brain angiotensin II and III
bestatin
-
inhibits the enzyme and blocks the metabolism of brain angiotensin II and III
bestatin
-
inhibits the enzyme and blocks the metabolism of brain angiotensin II and III
bestatin
-
inhibits the enzyme and blocks the metabolism of brain angiotensin II and III
Ca2+
-
inhibits activity with Gln-substrate, regulatory function and influence on substrate specificity
Ca2+
-
Ca2+ up- or down-regulates the enzyme activity depending on the substrate tested
Ca2+
-
Ca2+ up- or down-regulates the enzyme activity depending on the substrate tested
Ca2+
-
Ca2+ up- or down-regulates the enzyme activity depending on the substrate tested
EDTA
Q8I2J3;
activity is reduced to 14% after incubating with 10 mM EDTA
glutamate phosphonate
-
0.001 mM, activity of wild-type enzyme is completely abolished
o-phenanthroline
Q8I2J3;
activity is reduced to 8.3% after incubating with 20 mM o-phenanthroline
RB150
-
selective and specific prodrug of the enzyme inhibitor EC33, inhibits the enzyme given i.v. to rats
RB150
-
selective and specific prodrug of the enzyme inhibitor EC33, inhibits the enzyme given i.v. to rats
RB150
-
selective and specific prodrug of the enzyme inhibitor EC33, inhibits the enzyme given i.v. to mice
RB150
-
selective and specific prodrug of the enzyme inhibitor EC33, inhibits the enzyme given i.v. to rats
Zn2+
-
zinc-metallopeptidase, inhibits the activity with Glu- and Gln-substrates
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ca2+
-
Ca2+ up- or down-regulates the enzyme activity depending on the substrate tested
Ca2+
-
Ca2+ up- or down-regulates the enzyme activity depending on the substrate tested
Ca2+
-
Ca2+ up- or down-regulates the enzyme activity depending on the substrate tested
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kinetics and substrate specificity in presence or absence of Ca2+
-
2.272
alpha-L-Asp-2-naphthylamide
-
pH 7.4, 37°C, mutant enzyme wild-type enzyme N353Q
2.307
alpha-L-Asp-2-naphthylamide
-
pH 7.4, 37°C, mutant enzyme wild-type enzyme N353A
1.943
alpha-L-Glu-2-naphthylamide
-
pH 7.4, 37°C, mutant enzyme wild-type enzyme N353A
2.687
alpha-L-Glu-2-naphthylamide
-
pH 7.4, 37°C, mutant enzyme wild-type enzyme N353Q
0.171
alpha-L-Glu-beta-naphthylamide
-
pH 7.4, 37°C, wild-type enzyme, in presence of 4 mM Ca2+
0.432
alpha-L-Glu-beta-naphthylamide
-
pH 7.4, 37°C, wild-type enzyme, in presence of 0.025 mM Ca2+
0.697
alpha-L-Glu-beta-naphthylamide
-
pH 7.4, 37°C, wild-type enzyme, without Ca2+
4.383
alpha-L-Glu-beta-naphthylamide
-
pH 7.4, 37°C, mutant enzyme H450F enzyme, in presence of 4 mM Ca2+
5.94
alpha-L-Glu-beta-naphthylamide
-
pH 7.4, 37°C, mutant enzyme H450F, in presence of 0.025 mM Ca2+
1.4
Asp-4-methylcoumaryl-7-amide
-
recombinant enzyme, pH 7.5, 37°C, in presence of 1 mM Ca2+
2.3
Asp-4-methylcoumaryl-7-amide
-
recombinant enzyme, pH 7.5, 37°C, in absence of Ca2+
0.3273
Asp-7-amido-4-methylcoumarin
Q8I2J3;
in the presence of 1 mM cobalt
0.6
Gln-4-methylcoumaryl-7-amide
-
recombinant enzyme, pH 7.5, 37°C, in absence of Ca2+
7.1
Gln-4-methylcoumaryl-7-amide
-
recombinant enzyme, pH 7.5, 37°C, in presence of 1 mM Ca2+
0.4
Glu-4-methylcoumaryl-7-amide
-
recombinant enzyme, pH 7.5, 37°C, in presence of 1 mM Ca2+
1.2
Glu-4-methylcoumaryl-7-amide
-
recombinant enzyme, pH 7.5, 37°C, in absence of Ca2+
0.1363
Glu-7-amido-4-methylcoumarin
Q8I2J3;
in the presence of 1 mM cobalt
1.65
Glu-7-amido-4-methylcoumarin
-
mutant D221N, in the presence of 1.0 mM CaCl2
1.95
Glu-7-amido-4-methylcoumarin
-
mutant D221Q, in the presence of 1.0 mM CaCl2
2.87
Glu-7-amido-4-methylcoumarin
-
mutant D221E, in the presence of 1.0 mM CaCl2
4.31
Glu-7-amido-4-methylcoumarin
-
mutant D221A, in the presence of 1.0 mM CaCl2
0.091 - 1.2
Glu-beta-naphthylamide
-
value depending on source of enzyme and presence of divalent cations
0.091 - 1.2
Glu-beta-naphthylamide
-
value depending on source of enzyme and presence of divalent cations
0.159
L-Glu-2-naphthylamide
-
recombinant mutant enzyme T348S, in 50 mM Tris-HCl buffer, pH 7.4, in the presence of 4 mM Ca2+
0.198
L-Glu-2-naphthylamide
-
recombinant wild type enzyme, in 50 mM Tris-HCl buffer, pH 7.4, in the presence of 4 mM Ca2+
0.258
L-Glu-2-naphthylamide
-
recombinant mutant enzyme T348D, in 50 mM Tris-HCl buffer, pH 7.4, in the presence of 4 mM Ca2+
0.282
L-Glu-2-naphthylamide
-
recombinant mutant enzyme T348Y, in 50 mM Tris-HCl buffer, pH 7.4, in the presence of 4 mM Ca2+
1.136
L-Glu-2-naphthylamide
-
recombinant mutant enzyme T348D, in 50 mM Tris-HCl buffer, pH 7.4, in the absence of Ca2+
1.481
L-Glu-2-naphthylamide
-
recombinant wild type enzyme, in 50 mM Tris-HCl buffer, pH 7.4, in the absence of Ca2+
1.919
L-Glu-2-naphthylamide
-
recombinant mutant enzyme T348Y, in 50 mM Tris-HCl buffer, pH 7.4, in the absence of Ca2+
2.034
L-Glu-2-naphthylamide
-
recombinant mutant enzyme T348S, in 50 mM Tris-HCl buffer, pH 7.4, in the absence of Ca2+
0.152
L-Glu-p-nitroanilide
-
wild type enzyme, in absence of Ca2+, in 50 mM Tris/HCl buffer (pH 7.4), at 37°C
1.475
L-Glu-p-nitroanilide
-
wild type enzyme, in absence of Ca2+, in 50 mM Tris/HCl buffer (pH 7.4), at 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
14
alpha-L-Asp-2-naphthylamide
-
pH 7.4, 37°C, mutant enzyme wild-type enzyme N353A
25
alpha-L-Asp-2-naphthylamide
-
pH 7.4, 37°C, mutant enzyme wild-type enzyme N353Q
184
alpha-L-Glu-2-naphthylamide
-
pH 7.4, 37°C, mutant enzyme wild-type enzyme N353Q
227
alpha-L-Glu-2-naphthylamide
-
pH 7.4, 37°C, mutant enzyme wild-type enzyme N353A
1.8
alpha-L-Glu-beta-naphthylamide
-
pH 7.4, 37°C, mutant enzyme H450F, in presence of 0.025 mM Ca2+
7.5
alpha-L-Glu-beta-naphthylamide
-
pH 7.4, 37°C, mutant enzyme H450F enzyme, in presence of 4 mM Ca2+
93
alpha-L-Glu-beta-naphthylamide
-
pH 7.4, 37°C, wild-type enzyme, without Ca2+
149
alpha-L-Glu-beta-naphthylamide
-
pH 7.4, 37°C, wild-type enzyme, in presence of 0.025 mM Ca2+
166
alpha-L-Glu-beta-naphthylamide
-
pH 7.4, 37°C, wild-type enzyme, in presence of 4 mM Ca2+
2.8
Asp-4-methylcoumaryl-7-amide
-
recombinant enzyme, pH 7.5, 37°C, in absence of Ca2+
12.2
Asp-4-methylcoumaryl-7-amide
-
recombinant enzyme, pH 7.5, 37°C, in presence of 1 mM Ca2+
0.354
Asp-7-amido-4-methylcoumarin
Q8I2J3;
in the presence of 1 mM cobalt
0.031 - 0.51
cholecystokinin-8
-
mutant D221N, in the absence of CaCl2; wild-type, in the presence of 1.0 mM CaCl2
9.5
Gln-4-methylcoumaryl-7-amide
-
recombinant enzyme, pH 7.5, 37°C, in absence of Ca2+
14.1
Gln-4-methylcoumaryl-7-amide
-
recombinant enzyme, pH 7.5, 37°C, in presence of 1 mM Ca2+
13.3
Glu-4-methylcoumaryl-7-amide
-
recombinant enzyme, pH 7.5, 37°C, in absence of Ca2+
33.3
Glu-4-methylcoumaryl-7-amide
-
recombinant enzyme, pH 7.5, 37°C, in presence of 1 mM Ca2+
0.33
Glu-7-amido-4-methylcoumarin
Q8I2J3;
in the presence of 1 mM cobalt
0.58
Glu-7-amido-4-methylcoumarin
-
mutant D221A, in the presence of 1.0 mM CaCl2
1.23
Glu-7-amido-4-methylcoumarin
-
mutant D221E, in the presence of 1.0 mM CaCl2
2.78
Glu-7-amido-4-methylcoumarin
-
mutant D221Q, in the presence of 1.0 mM CaCl2
3.68
Glu-7-amido-4-methylcoumarin
-
mutant D221N, in the presence of 1.0 mM CaCl2
2 - 8
L-Glu-2-naphthylamide
-
recombinant mutant enzyme T348Y, in 50 mM Tris-HCl buffer, pH 7.4, in the absence of Ca2+
40
L-Glu-2-naphthylamide
-
recombinant mutant enzyme T348D, in 50 mM Tris-HCl buffer, pH 7.4, in the presence of 4 mM Ca2+
92
L-Glu-2-naphthylamide
-
recombinant mutant enzyme T348D, in 50 mM Tris-HCl buffer, pH 7.4, in the absence of Ca2+
167
L-Glu-2-naphthylamide
-
recombinant mutant enzyme T348Y, in 50 mM Tris-HCl buffer, pH 7.4, in the presence of 4 mM Ca2+
256
L-Glu-2-naphthylamide
-
recombinant wild type enzyme, in 50 mM Tris-HCl buffer, pH 7.4, in the presence of 4 mM Ca2+
292
L-Glu-2-naphthylamide
-
recombinant wild type enzyme, in 50 mM Tris-HCl buffer, pH 7.4, in the absence of Ca2+
575
L-Glu-2-naphthylamide
-
recombinant mutant enzyme T348S, in 50 mM Tris-HCl buffer, pH 7.4, in the presence of 4 mM Ca2+
640
L-Glu-2-naphthylamide
-
recombinant mutant enzyme T348S, in 50 mM Tris-HCl buffer, pH 7.4, in the absence of Ca2+
295
L-Glu-p-nitroanilide
-
wild type enzyme, in absence of Ca2+, in 50 mM Tris/HCl buffer (pH 7.4), at 37°C
720
L-Glu-p-nitroanilide
-
wild type enzyme, in absence of Ca2+, in 50 mM Tris/HCl buffer (pH 7.4), at 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0427
3-[(1-amino-2-carboxyethyl)(hydroxy)phosphoryl]-2-methylpropanoic acid
Q8I2J3;
-
0.1831
3-[[amino(carboxy)methyl](hydroxy)phosphoryl]-2-methylpropanoic acid
Q8I2J3;
-
0.00007
N-(2-aminoethyl)-4-methyl-5-sulfanyl-pentanamide
-
wild type enzyme, in 50 mM Tris/HCl buffer (pH 7.4), 4 mM Ca2+, at 37°C
0.000292
[[(2R,3R)-3-amino-2-sulfhydryl-5-sulfonate]pentanoyl]-D-Ile-Asp-OH
-
pH 7.3, 37°C
0.0000833
[[(2R,3R)-3-amino-2-sulfhydryl-5-sulfonate]pentanoyl]-Ile-3-sulfoalanine-OH
-
pH 7.3, 37°C
0.000283
[[(2R,3R)-3-amino-2-sulfhydryl-5-sulfonate]pentanoyl]-Ile-D-Asp-OH
-
pH 7.3, 37°C
0.0042
[[(2R,3R)-3-amino-2-sulfhydryl-5-sulfonate]pentanoyl]-Ile-NH2
-
pH 7.3, 37°C
0.0012
[[(2R,3R)-3-amino-2-sulfhydryl-5-sulfonate]pentanoyl]-Ile-OH
-
pH 7.3, 37°C
0.000027
[[(2R,3R)-3-amino-2-sulfhydryl-5-sulfonate]pentanoyl]-Tyr-Asp-OH
-
pH 7.3, 37°C
0.0000733
[[(2R,3R)-3-amino-2-sulfhydryl-5-sulfonate]pentanoyl]-Tyr-homosulfoalanine-OH
-
pH 7.3, 37°C
0.000267
[[(2R,3R)-3-amino-5-carboxylate-2-sulfhydryl]pentanoyl]-Ile-Asp-OH
-
pH 7.3, 37°C
0.00091
[[(2R,3R)-3-amino-5-phosphonate-2-sulfhydryl]pentanoyl]-Ile-Asp-OH
-
pH 7.3, 37°C
0.00005
[[(2R,3S)-3-amino-2-sulfhydryl-5-sulfonate]pentanoyl]-Ile-Asp-OH
-
pH 7.3, 37°C
0.000016
[[(2R,3S)-3-amino-5-carboxylate-2-sulfhydryl]pentanoyl]-Ile-Asp-OH
-
pH 7.3, 37°C
0.000051
[[(2RS,3RS)-3-amino2-sulfhydryl-5-sulfamoyl]pentane]-Ile-Asp-OH
-
pH 7.3, 37°C
0.00008
[[(2RS,3RS)-3-amino2-sulfhydryl-5-sulfamoyl]pentanoyl]-Ile-Asp-OH
-
pH 7.3, 37°C
0.00015
[[(2RS,3RS)-3-amino2-sulfhydryl-5-sulfamoyl]pentanoyl]-Tyr-Asp-OH
-
pH 7.3, 37°C
0.0000147
[[(2S,3R)-3-amino-2-sulfhydryl-5-sulfonate]pentanoyl]-D-Ile-Asp-OH
-
pH 7.3, 37°C
0.0000036
[[(2S,3R)-3-amino-2-sulfhydryl-5-sulfonate]pentanoyl]-Ile-3-sulfoalanine-OH
-
pH 7.3, 37°C
0.00000536
[[(2S,3R)-3-amino-2-sulfhydryl-5-sulfonate]pentanoyl]-Ile-D-Asp-OH
-
pH 7.3, 37°C
0.000145
[[(2S,3R)-3-amino-2-sulfhydryl-5-sulfonate]pentanoyl]-Ile-NH2
-
pH 7.3, 37°C
0.00004
[[(2S,3R)-3-amino-2-sulfhydryl-5-sulfonate]pentanoyl]-Ile-OH
-
pH 7.3, 37°C
0.0000043
[[(2S,3R)-3-amino-2-sulfhydryl-5-sulfonate]pentanoyl]-Tyr-Asp-OH
-
pH 7.3, 37°C
0.0000093
[[(2S,3R)-3-amino-2-sulfhydryl-5-sulfonate]pentanoyl]-Tyr-homosulfoalanine-OH
-
pH 7.3, 37°C
0.00000356
[[(2S,3R)-3-amino-5-carboxylate-2-sulfhydryl]pentanoyl]-Ile-Asp-OH
-
pH 7.3, 37°C
0.000012
[[(2S,3R)-3-amino-5-phosphonate-2-sulfhydryl]pentanoyl]-Ile-Asp-OH
-
pH 7.3, 37°C
0.00002
[[(2S,3S)-3-amino-2-sulfhydryl-5-sulfonate]pentanoyl]-Ile-Asp-OH
-
pH 7.3, 37°C
0.000013
[[(2S,3S)-3-amino-5-carboxylate-2-sulfhydryl]pentanoyl]-Ile-Asp-OH
-
pH 7.3, 37°C
additional information
additional information
-
inhibition constant of 3-amino-4-thio-butyl sulfonic acid for aminopeptidase A: 0.29 microM/L
-
0.00061
glutamate phosphonic acid
-
pH 7.4, 37°C, wild-type enzyme, 0.025 mM Ca2+
0.00084
glutamate phosphonic acid
-
pH 7.4, 37°C, mutant enzyme H450F, 4 mM Ca2+
0.056
glutamate phosphonic acid
-
pH 7.4, 37°C, mutant enzyme H450F, 0.025 mM Ca2+
0.00038
glutamate thiol
-
mutant enzyme T348S, in 50 mM Tris-HCl buffer, pH 7.4, in the presence of 4 mM Ca2+
0.00085
glutamate thiol
-
mutant enzyme T348Y, in 50 mM Tris-HCl buffer, pH 7.4, in the presence of 4 mM Ca2+
0.00103
glutamate thiol
-
mutant enzyme T348D, in 50 mM Tris-HCl buffer, pH 7.4, in the presence of 4 mM Ca2+
0.0011
glutamate thiol
-
wild type enzyme, in 50 mM Tris-HCl buffer, pH 7.4, in the absence of Ca2+
0.00194
glutamate thiol
-
mutant enzyme T348S, in 50 mM Tris-HCl buffer, pH 7.4, in the absence of Ca2+
0.00197
glutamate thiol
-
mutant enzyme T348D, in 50 mM Tris-HCl buffer, pH 7.4, in the absence of Ca2+
0.002
glutamate thiol
-
wild type enzyme, in 50 mM Tris-HCl buffer, pH 7.4, in the presence of 4 mM Ca2+
0.00206
glutamate thiol
-
mutant enzyme T348Y, in 50 mM Tris-HCl buffer, pH 7.4, in the absence of Ca2+
0.0001
lysine thiol
-
mutant enzyme T348S, in 50 mM Tris-HCl buffer, pH 7.4, in the absence of Ca2+
0.00022
lysine thiol
-
wild type enzyme, in 50 mM Tris-HCl buffer, pH 7.4, in the absence of Ca2+
0.00026
lysine thiol
-
mutant enzyme T348Y, in 50 mM Tris-HCl buffer, pH 7.4, in the absence of Ca2+
0.0009
lysine thiol
-
mutant enzyme T348D, in 50 mM Tris-HCl buffer, pH 7.4, in the absence of Ca2+
0.00275
lysine thiol
-
mutant enzyme T348S, in 50 mM Tris-HCl buffer, pH 7.4, in the presence of 4 mM Ca2+
0.00298
lysine thiol
-
wild type enzyme, in 50 mM Tris-HCl buffer, pH 7.4, in the presence of 4 mM Ca2+
0.0036
lysine thiol
-
mutant enzyme T348Y, in 50 mM Tris-HCl buffer, pH 7.4, in the presence of 4 mM Ca2+
0.00394
lysine thiol
-
mutant enzyme T348D, in 50 mM Tris-HCl buffer, pH 7.4, in the presence of 4 mM Ca2+
0.00019
methionine thiol
-
mutant enzyme T348S, in 50 mM Tris-HCl buffer, pH 7.4, in the absence of Ca2+
0.00026
methionine thiol
-
mutant enzyme T348D, in 50 mM Tris-HCl buffer, pH 7.4, in the absence of Ca2+
0.00029
methionine thiol
-
mutant enzyme T348Y, in 50 mM Tris-HCl buffer, pH 7.4, in the absence of Ca2+
0.00058
methionine thiol
-
wild type enzyme, in 50 mM Tris-HCl buffer, pH 7.4, in the absence of Ca2+
0.00307
methionine thiol
-
mutant enzyme T348Y, in 50 mM Tris-HCl buffer, pH 7.4, in the presence of 4 mM Ca2+
0.00403
methionine thiol
-
mutant enzyme T348S, in 50 mM Tris-HCl buffer, pH 7.4, in the presence of 4 mM Ca2+
0.00667
methionine thiol
-
mutant enzyme T348D, in 50 mM Tris-HCl buffer, pH 7.4, in the presence of 4 mM Ca2+
0.0084
methionine thiol
-
wild type enzyme, in 50 mM Tris-HCl buffer, pH 7.4, in the presence of 4 mM Ca2+
0.000053
[[(2R,3R)-3-amino-2-sulfhydryl-5-sulfonate]pentanoyl]-Ile-Asp-OH
-
pH 7.3, 37°C
0.00047
[[(2R,3R)-3-amino-2-sulfhydryl-5-sulfonate]pentanoyl]-Ile-Asp-OH
-
pH 7.3, 37°C
0.0000032
[[(2S,3R)-3-amino-2-sulfhydryl-5-sulfonate]pentanoyl]-Ile-Asp-OH
-
pH 7.3, 37°C
0.000015
[[(2S,3R)-3-amino-2-sulfhydryl-5-sulfonate]pentanoyl]-Ile-Asp-OH
-
pH 7.3, 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.065
angiotensin II
Homo sapiens;
-
competitive against Glu-4-methylcoumaryl-7-amide, IC50 is 0.065 mM in presence of Ca2+
0.024
cholecystokinin-8
Homo sapiens;
-
competitive against Glu-4-methylcoumaryl-7-amide, IC50 is 0.024 mM in presence of Ca2+
0.049
chromogranin A
Homo sapiens;
-
competitive against Glu-4-methylcoumaryl-7-amide, IC50 is 0.049 mM in presence of Ca2+
-
0.06
neurokinin B
Homo sapiens;
-
competitive against Glu-4-methylcoumaryl-7-amide,IC50 is 0.060 mM in presence of Ca2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.000004
-
soluble glutamyl aminopeptidase activity in the atrium of euthyroid adult male rats; soluble glutamyl aminopeptidase activity in the atrium of hyperthyroid adult male rats; soluble glutamyl aminopeptidase activity in the atrium of hypothyroid adult male rats
0.0000071
0.000014
0.000045
-
membrane-bound glutamyl aminopeptidase activity in the atrium of hypothyroid adult male rats
0.00005
-
membrane-bound glutamyl aminopeptidase activity in the atrium of euthyroid adult male rats
0.000065
-
membrane-bound glutamyl aminopeptidase activity in the atrium of hyperthyroid adult male rats
0.06
-
aminopeptidase A activity, cortex, aminopeptidase A-deficient mice; aminopeptidase A activity, striatum, aminopeptidase A-deficient mice
0.09
-
aminopeptidase A activity, tegmentum/colliculi, aminopeptidase A-deficient mice
7
-
aminopeptidase A activity depending on alcohol, lung, wild-type mice, with access to a 10% ethanol solution
11
-
aminopeptidase A activity depending on alcohol, lung, wild-type mice, without access to a 10% ethanol solution
21
-
aminopeptidase A activity depending on alcohol, kidney, wild-type mice, without access to a 10% ethanol solution
26
-
aminopeptidase A activity depending on alcohol, kidney, wild-type mice, with access to a 10% ethanol solution
additional information
additional information