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alpha-L-Asp-2-naphthylamide + H2O
L-Asp + 2-naphthylamine
-
-
-
?
alpha-L-Asp-Val-angiotensin II + H2O
Asp + Val-angiotensin II
-
-
-
-
?
alpha-L-aspartate-beta-naphthylamide + H2O
L-aspartate + beta-naphthylamine
high activity
-
-
?
alpha-L-Glu-2-naphthylamide + H2O
alpha-L-Glu + 2-naphthylamine
-
-
-
?
alpha-L-Glu-beta-naphthylamide + H2O
L-Glu + 2-naphthylamine
alpha-L-glutamyl-beta-naphthylamide + H2O
L-glutamine + beta-naphthylamine
best substrate
-
-
?
angiotensin I + H2O
Asp + Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu
-
-
-
-
?
angiotensin II
Asp + Arg-Val-Tyr-Ile-His-Pro-Phe
angiotensin II + H2O
angiotensin III + L-Asp
angiotensin II + H2O
Asp + angiotensin III
angiotensin II + H2O
aspartic acid + angiotensin III
angiotensin II + H2O
L-Asp + angiotensin III
-
-
-
-
?
angiotensin II + H2O
L-aspartic acid + angiotensin III
angiotensin III + H2O
? + angiotensin IV
-
i.e. Tyr-Arg-Val-Tyr-Ile-His-Pro-Phe, low activity in absence of Ca2+
-
-
?
angiotensin III + H2O
angiotensin IV + Arg
Asp-4-methylcoumaryl-7-amide + H2O
Asp + 7-amino-4-methylcoumarin
-
low activity in absence and presence of Ca2+
-
-
?
Asp-4-nitroanilide + H2O
Asp + 4-nitroaniline
-
-
-
-
?
Asp-7-amido-4-methylcoumarin + H2O
Asp + 7-amino-4-methylcoumarin
assay for measuring aspartyl aminopeptidase activity
-
-
?
Asp-beta-naphthylamide + H2O
Asp + naphthylamine
Asp-Phe-NH2 + H2O
Asp + Phe + NH3
-
-
-
-
?
aspartame + H2O
L-Asp + L-Phe methyl ester
-
-
-
-
?
cholecystokinin-8 + H2O
?
cholecystokinin-8 + H2O
Asp + YMGWMDF-NH2
-
i.e. CCK8 or DYMGWMDF-NH2
-
-
?
cholecystokinin-8 + H2O
L-Asp + YMGWMDF-NH2
-
-
-
-
?
chromogranin A + H2O
?
-
-
-
-
?
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-2-naphthylamide + H2O
Glu + 2-naphthylamine
Glu-4-methylcoumaryl-7-amide + H2O
Glu + 7-amino-4-methylcoumarin
Glu-4-nitroanilide + H2O
Glu + 4-nitroaniline
Glu-7-amido-4-methylcoumarin + H2O
Glu + 7-amino-4-methylcoumarin
Glu-beta-naphthylamide + H2O
Glu + naphthylamine
Glu-Glu + H2O
2 Glu
-
many Glu-Xxx and Asp-Xxx dipeptides are substrates
-
-
?
Glu-p-nitroanilide + H2O
Glu + 4-nitroaniline
Glu-p-nitroanilide + H2O
Glu + p-nitroaniline
Glu-p-nitroanilide + H2O
glutamic acid + p-nitroaniline
Gly-7-amido-4-methylcoumarin + H2O
Gly + 7-amino-4-methylcoumarin
-
-
-
?
kallidin + H2O
?
-
-
-
-
?
kallidin + H2O
Lys + bradykinin
-
i.e. Lys-bradykinin or KRPPGFSPFR, the reaction is performed only in absence of Ca2+
i.e. RPPGFSPFR
-
?
L-Ala-4-methylcoumaryl-7-amide + H2O
L-Ala + 7-amino-4-methylcoumarin
L-Ala-7-amido-4-methylcoumarin + H2O
L-Ala + 7-amino-4-methylcoumarin
-
-
-
?
L-alanine-beta-naphthylamide + H2O
L-alanine + beta-naphthylamine
low activity
-
-
?
L-Arg-2-naphthylamide + H2O
L-Arg + 2-naphthylamine
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
L-Asp-4-nitroanilide + H2O
L-Asp + 4-nitroaniline
L-Asp-peptide + H2O
L-Asp + peptide
L-aspartate-beta-naphthylamide + H2O
L-aspartate + beta-naphthylamine
-
-
-
?
L-Glu-2-naphthylamide + H2O
L-Glu + 2-naphthylamine
L-Glu-4-methylcoumaryl-7-amide + H2O
L-Glu + 7-amino-4-methylcoumarin
L-Glu-4-nitroanilide + H2O
L-Glu + 4-nitroaniline
L-Glu-7-amido-4-methylcoumarin + H2O
L-Glu + 7-amino-4-methylcoumarin
L-Glu-beta-naphthylamide + H2O
L-Glu + beta-naphthylamine
-
-
-
?
L-Glu-p-nitroanilide + H2O
L-Glu + p-nitroaniline
-
-
-
?
L-Glu-peptide + H2O
L-Glu + peptide
L-glutamic acid gamma-2-naphthylamide + H2O
L-glutamate + 2-naphthylamide
L-glutamyl beta-naphthylamide + H2O
L-Glu + beta-naphthylamine
L-glutamyl-beta-naphthylamide + H2O
L-glutamine + beta-naphthylamine
-
-
-
?
L-Leu-4-methylcoumaryl-7-amide + H2O
L-Leu + 7-amino-4-methylcoumarin
L-Leu-7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
-
-
-
?
L-lysine-beta-naphthylamide + H2O
L-lysine + beta-naphthylamine
low activity
-
-
?
L-Phe-7-amido-4-methylcoumarin + H2O
L-Phe + 7-amino-4-methylcoumarin
-
-
-
?
L-Pro-7-amido-4-methylcoumarin + H2O
L-Pro + 7-amino-4-methylcoumarin
-
-
-
?
L-Tyr-7-amido-4-methylcoumarin + H2O
L-Tyr + 7-amino-4-methylcoumarin
-
-
-
?
L-Val-7-amido-4-methylcoumarin + H2O
L-Val + 7-amino-4-methylcoumarin
-
-
-
?
Leu-7-amido-4-methylcoumarin + H2O
Leu + 7-amino-4-methylcoumarin
assay for measuring aspartyl aminopeptidase activity
-
-
?
milk proteins + H2O
?
-
-
-
-
?
N-(alpha-L-Ala-L-Leu-L-Lys-Arg)-2-naphthylamide + H2O
?
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-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)-beta-naphthylamide + H2O
L-glutamic acid + beta-naphthylamine
N-Glu-L-Phe-4-nitroanilide + H2O
L-Glu + L-Phe-4-nitroanilide
-
-
-
-
?
neurokinin B + H2O
?
-
-
-
-
?
neurokinin B + H2O
Asp + MHDFFVGLM-NH2
-
i.e. DMHDFFVGLM-NH2
-
-
?
additional information
?
-
alpha-L-Glu-beta-naphthylamide + H2O
L-Glu + 2-naphthylamine
-
-
-
?
alpha-L-Glu-beta-naphthylamide + H2O
L-Glu + 2-naphthylamine
-
-
-
-
?
alpha-L-Glu-beta-naphthylamide + H2O
L-Glu + 2-naphthylamine
-
-
-
?
angiotensin I + H2O
?
-
cleavage only in vitro
-
-
?
angiotensin I + H2O
?
-
cleavage only in vitro
-
-
?
angiotensin I + H2O
?
-
cleavage only in vitro
-
-
?
angiotensin I + H2O
?
-
cleavage only in vitro
-
-
?
angiotensin II
Asp + Arg-Val-Tyr-Ile-His-Pro-Phe
-
-
-
?
angiotensin II
Asp + Arg-Val-Tyr-Ile-His-Pro-Phe
-
-
-
?
angiotensin II + H2O
?
-
-
-
-
?
angiotensin II + H2O
?
-
-
-
?
angiotensin II + H2O
angiotensin III + L-Asp
-
-
-
?
angiotensin II + H2O
angiotensin III + L-Asp
-
-
-
-
?
angiotensin II + H2O
angiotensin III + L-Asp
-
-
-
?
angiotensin II + H2O
angiotensin III + L-Asp
-
-
-
?
angiotensin II + H2O
angiotensin III + L-Asp
-
-
-
?
angiotensin II + H2O
angiotensin III + L-Asp
-
-
-
?
angiotensin II + H2O
Asp + angiotensin III
-
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
-
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 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
-
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 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
Asp + angiotensin III
-
i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe
i.e. Arg-Val-Tyr-Ile-His-Pro-Phe
-
ir
angiotensin II + H2O
aspartic acid + angiotensin III
-
-
-
-
?
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 + H2O
aspartic acid + angiotensin III
-
-
-
-
?
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 II + H2O
L-aspartic acid + angiotensin III
-
-
-
-
?
angiotensin II + H2O
L-aspartic acid + angiotensin III
-
-
-
-
?
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-Ala + H2O
Asp + Ala
-
-
-
?
Asp-Ala + H2O
Asp + Ala
-
-
-
?
Asp-Ala + H2O
Asp + Ala
-
-
-
-
?
Asp-Ala + H2O
Asp + Ala
-
74% of the activity with Glu-Ala
-
-
?
Asp-beta-naphthylamide + H2O
Asp + naphthylamine
-
dog kidney enzyme 3 times more active compared to Glu-beta-naphthylamide
-
-
?
Asp-beta-naphthylamide + H2O
Asp + naphthylamine
-
-
-
-
?
Asp-beta-naphthylamide + H2O
Asp + naphthylamine
-
-
-
-
?
cholecystokinin-8 + H2O
?
-
i.e. CCK8
-
-
?
cholecystokinin-8 + H2O
?
-
cleavage only in vitro
-
-
?
cholecystokinin-8 + H2O
?
-
CCK8
-
-
?
cholecystokinin-8 + H2O
?
-
-
-
?
cholecystokinin-8 + H2O
?
-
cleavage only in vitro
-
-
?
cholecystokinin-8 + H2O
?
-
cleavage only in vitro
-
-
?
cholecystokinin-8 + H2O
?
-
cleavage only in vitro
-
-
?
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
-
-
-
-
?
Glu-4-methylcoumaryl-7-amide + H2O
Glu + 7-amino-4-methylcoumarin
-
low activity in absence of Ca2+
-
-
?
Glu-4-nitroanilide + H2O
Glu + 4-nitroaniline
-
-
-
-
?
Glu-4-nitroanilide + H2O
Glu + 4-nitroaniline
-
-
-
?
Glu-7-amido-4-methylcoumarin + H2O
Glu + 7-amino-4-methylcoumarin
-
-
-
-
?
Glu-7-amido-4-methylcoumarin + H2O
Glu + 7-amino-4-methylcoumarin
-
activity assay
-
-
?
Glu-7-amido-4-methylcoumarin + H2O
Glu + 7-amino-4-methylcoumarin
-
-
-
-
?
Glu-7-amido-4-methylcoumarin + H2O
Glu + 7-amino-4-methylcoumarin
assay for measuring aspartyl aminopeptidase activity
-
-
?
Glu-7-amido-4-methylcoumarin + H2O
Glu + 7-amino-4-methylcoumarin
-
-
-
-
?
Glu-Ala + H2O
Glu + Ala
-
-
-
?
Glu-Ala + H2O
Glu + Ala
-
-
-
?
Glu-Ala + H2O
Glu + Ala
-
-
-
-
?
Glu-Ala + H2O
Glu + Ala
-
high activity
-
-
?
Glu-beta-naphthylamide + H2O
Glu + naphthylamine
-
aminopeptidase A six times more active compared to Asp-beta-naphthylamide
-
-
?
Glu-beta-naphthylamide + H2O
Glu + naphthylamine
-
-
-
-
?
Glu-beta-naphthylamide + H2O
Glu + naphthylamine
-
-
-
-
?
Glu-beta-naphthylamide + H2O
Glu + naphthylamine
-
-
-
-
?
Glu-beta-naphthylamide + H2O
Glu + naphthylamine
-
-
-
-
?
Glu-Gly + H2O
Glu + Gly
-
-
-
?
Glu-Gly + H2O
Glu + Gly
-
-
-
?
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
-
-
-
-
?
Glu-p-nitroanilide + H2O
Glu + p-nitroaniline
-
-
-
-
?
Glu-p-nitroanilide + H2O
Glu + p-nitroaniline
-
-
-
-
?
Glu-p-nitroanilide + H2O
Glu + p-nitroaniline
-
activity assay, cleaved p-nitroanilide is measured
-
-
?
Glu-p-nitroanilide + H2O
Glu + p-nitroaniline
-
-
-
-
?
Glu-p-nitroanilide + H2O
Glu + p-nitroaniline
-
-
-
-
?
Glu-p-nitroanilide + H2O
Glu + p-nitroaniline
-
-
-
-
?
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-Arg-2-naphthylamide + H2O
L-Arg + 2-naphthylamine
-
-
-
-
?
L-Arg-2-naphthylamide + H2O
L-Arg + 2-naphthylamine
-
-
-
-
?
L-Arg-2-naphthylamide + H2O
L-Arg + 2-naphthylamine
-
-
-
-
?
L-Asp-4-nitroanilide + H2O
L-Asp + 4-nitroaniline
-
-
-
?
L-Asp-4-nitroanilide + H2O
L-Asp + 4-nitroaniline
-
-
-
?
L-Asp-4-nitroanilide + H2O
L-Asp + 4-nitroaniline
-
-
-
-
?
L-Asp-4-nitroanilide + H2O
L-Asp + 4-nitroaniline
-
-
-
-
?
L-Asp-peptide + H2O
L-Asp + peptide
-
-
-
-
?
L-Asp-peptide + H2O
L-Asp + peptide
-
free gamma-carboxyl group of N-terminal amino acid essential
-
-
?
L-Asp-peptide + H2O
L-Asp + peptide
-
-
-
-
?
L-Asp-peptide + H2O
L-Asp + peptide
-
specificity for di- and tri-peptides with Asp or Glu at N-terminal end
-
-
?
L-Glu-2-naphthylamide + H2O
L-Glu + 2-naphthylamine
-
-
-
-
?
L-Glu-2-naphthylamide + H2O
L-Glu + 2-naphthylamine
-
-
-
-
?
L-Glu-2-naphthylamide + H2O
L-Glu + 2-naphthylamine
-
-
-
?
L-Glu-2-naphthylamide + H2O
L-Glu + 2-naphthylamine
-
-
-
-
?
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-4-nitroanilide + H2O
L-Glu + 4-nitroaniline
-
-
-
?
L-Glu-4-nitroanilide + H2O
L-Glu + 4-nitroaniline
-
-
-
?
L-Glu-4-nitroanilide + H2O
L-Glu + 4-nitroaniline
-
-
-
-
?
L-Glu-4-nitroanilide + H2O
L-Glu + 4-nitroaniline
-
-
-
-
?
L-Glu-7-amido-4-methylcoumarin + H2O
L-Glu + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Glu-7-amido-4-methylcoumarin + 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
-
-
-
-
?
L-Glu-peptide + H2O
L-Glu + peptide
-
-
-
-
?
L-Glu-peptide + H2O
L-Glu + peptide
-
specificity for di-and tripeptides with Asp or Glu at N-terminal end
-
-
?
L-glutamic acid gamma-2-naphthylamide + H2O
L-glutamate + 2-naphthylamide
-
-
-
?
L-glutamic acid gamma-2-naphthylamide + H2O
L-glutamate + 2-naphthylamide
-
-
-
?
L-glutamyl beta-naphthylamide + H2O
L-Glu + beta-naphthylamine
-
-
-
?
L-glutamyl beta-naphthylamide + H2O
L-Glu + beta-naphthylamine
-
-
-
?
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-Ala-L-Leu-L-Lys-Arg)-2-naphthylamide + H2O
?
-
-
-
-
?
N-(alpha-L-Ala-L-Leu-L-Lys-Arg)-2-naphthylamide + H2O
?
-
-
-
-
?
N-(alpha-L-Ala-L-Leu-L-Lys-Arg)-2-naphthylamide + H2O
?
-
-
-
-
?
N-(alpha-L-Ala-L-Leu-L-Lys-Arg)-2-naphthylamide + H2O
?
-
-
-
-
?
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)-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
-
-
-
-
?
Ser-Ala + H2O
Ser + Ala
-
-
-
?
Ser-Ala + H2O
Ser + Ala
-
-
-
?
Ser-Ala + H2O
Ser + Ala
-
-
-
-
?
Ser-Ala + H2O
Ser + Ala
-
less than 2% of the activity with Glu-Ala
-
-
?
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
?
-
the wild-type enzyme has a high specificity for N-terminal Asp and Glu. Enzyme specificities of the enzyme-metal variants with different substrates, overview
-
-
?
additional information
?
-
the wild-type enzyme has a high specificity for N-terminal Asp and Glu. Enzyme specificities of the enzyme-metal variants with different substrates, overview
-
-
?
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
?
-
enzyme APA cleaves the N-terminal glutamyl or aspartyl residue from peptide substrates
-
-
?
additional information
?
-
-
enzyme APA cleaves the N-terminal glutamyl or aspartyl residue from peptide substrates
-
-
?
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
?
-
-
-
-
-
?
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
-
-
?
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(1-aminopropane-1,3-diyl)bis(phosphonic acid)
-
(3R)-3-amino-3-phosphonopropanoic acid
-
(4R)-4-amino-5-sulfanylpentanoic acid
a linear competitive inhibitor
(R)-3-amino-4-mercaptobutane-1-sulfonic acid
-
i.e. EC33
(S)-3-amino-4-mercapto-butyl sulfonic acid
(S)-3-amino-4-mercapto-butylsulfonic acid
(S)-3-amino-4-mercaptobutyl sulfonic acid
2,6-diaminohexane-1-thiol
a linear competitive inhibitor
2-amino-4-methylsulfonyl butane thiol
2-mercaptoethanol
-
58% inhibition at 0.01 mM, 96% at 0.1 mM
3-amino-3-[hydroxy(phenyl)phosphoryl]propanoic acid
-
3-amino-4-thio-butyl sulfonate
-
-
3-amino-4-thio-butyl sulfonic acid
-
EC33, specific and selective APA inhibitor
3-[(1-amino-2-carboxyethyl)(hydroxy)phosphoryl]-2-methylpropanoic acid
-
3-[[amino(carboxy)methyl](hydroxy)phosphoryl]-2-methylpropanoic acid
-
4,4'-dithio [bis[(3S)-3-aminobutyl sulfonic acid]]
-
i.e. RB150
4,4'-dithio[bis(3)-aminobutylsulfonic acid]
4,4'-dithio[bis(3-aminobutyl sulfonic acid)]
-
RB150, a prodrug of EC33
4-amino-4-phosphonobutyric acid
a specific and selective APA inhibitor, a linear competitive inhibitor
5-amino-5-phosphonopentanoic acid
-
acetic acid
inactivates at 50% w/v
Ala-PSI[PO2-CH2]-Leu-Ala
-
amastin
-
3% residual activity at a concentration of 0.001 mM
-
amino(phosphono)acetic acid
-
amino[hydroxy(methyl)phosphoryl]acetic acid
-
angiotensin II
-
competitive against Glu-4-methylcoumaryl-7-amide, IC50 is 0.065 mM in presence of Ca2+
angiotensin III
-
competitive against Glu-4-methylcoumaryl-7-amide
aspartate hydroxamate
-
-
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+
-
D-glutamate phosphonic acid
-
diisopropylfluorophosphate
-
-
Glu-PSI[PO2-CH2]-Leu-Ala
-
Glu-PSI[PO2-CH2]-Leu-Arg
-
Glu-PSI[PO2-CH2]-Leu-Asp
-
Glu-PSI[PO2-CH2]-Leu-Leu
-
glutamate phosphonic acid
kallidin
-
competitive against Glu-4-methylcoumaryl-7-amide
L-alpha-glutaryl-L-phenylalanine
-
-
L-Glu
-
product inhibition of enzyme Lc-PepA, 8.4% inhibition at 0.1 mM, 17.7% at 10 mM, product inhibition versus substrate L-Asp-4-nitroanilide, and 1.47% inhibition at 0.1 mM, 31.4% at 10 mM, product inhibition versus substrate L-Glu-4-nitroanilide
L-glutamate phosphinic acid
L-glutamate phosphonic acid
-
leupeptin
-
slight inhibition at 1 mM
methionine-thiol
a linear competitive inhibitor
Mg2+
-
inhibits the activity with Glu-substrate moderately
N-(2-aminoethyl)-4-methyl-5-sulfanyl-pentanamide
-
neurokinin B
-
competitive against Glu-4-methylcoumaryl-7-amide,IC50 is 0.060 mM in presence of Ca2+
p-hydroxymercuribenzoate
-
-
parathyroid hormone residues 69-84
-
-
-
pepstatin A
-
slight inhibition
phenylmethylsulfonyl fluoride
-
-
ZnCl2
-
0% residual activity at a concentration of 1 mM
[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]-D-Ile-Asp-OH
-
[[(2R,3R)-3-amino-2-sulfhydryl-5-sulfonate]pentanoyl]-Ile-3-sulfoalanine-OH
-
[[(2R,3R)-3-amino-2-sulfhydryl-5-sulfonate]pentanoyl]-Ile-Asp-OH
-
[[(2R,3R)-3-amino-2-sulfhydryl-5-sulfonate]pentanoyl]-Ile-D-Asp-OH
-
[[(2R,3R)-3-amino-2-sulfhydryl-5-sulfonate]pentanoyl]-Ile-NH2
-
[[(2R,3R)-3-amino-2-sulfhydryl-5-sulfonate]pentanoyl]-Ile-OH
-
[[(2R,3R)-3-amino-2-sulfhydryl-5-sulfonate]pentanoyl]-Tyr-Asp-OH
-
[[(2R,3R)-3-amino-2-sulfhydryl-5-sulfonate]pentanoyl]-Tyr-homosulfoalanine-OH
-
[[(2R,3R)-3-amino-5-carboxylate-2-sulfhydryl]pentanoyl]-Ile-Asp-OH
-
[[(2R,3R)-3-amino-5-phosphonate-2-sulfhydryl]pentanoyl]-Ile-Asp-OH
-
[[(2R,3S)-3-amino-2-sulfhydryl-5-sulfonate]pentanoyl]-Ile-Asp-OH
-
[[(2R,3S)-3-amino-5-carboxylate-2-sulfhydryl]pentanoyl]-Ile-Asp-OH
-
[[(2RS,3RS)-3-amino2-sulfhydryl-5-sulfamoyl]pentane]-Ile-Asp-OH
-
[[(2RS,3RS)-3-amino2-sulfhydryl-5-sulfamoyl]pentanoyl]-Ile-Asp-OH
-
[[(2RS,3RS)-3-amino2-sulfhydryl-5-sulfamoyl]pentanoyl]-Tyr-Asp-OH
-
[[(2S,3R)-3-amino-2-sulfhydryl-5-sulfonate]pentanoyl]-D-Ile-Asp-OH
-
[[(2S,3R)-3-amino-2-sulfhydryl-5-sulfonate]pentanoyl]-Ile-3-sulfoalanine-OH
-
[[(2S,3R)-3-amino-2-sulfhydryl-5-sulfonate]pentanoyl]-Ile-Asp-OH
-
[[(2S,3R)-3-amino-2-sulfhydryl-5-sulfonate]pentanoyl]-Ile-D-Asp-OH
-
[[(2S,3R)-3-amino-2-sulfhydryl-5-sulfonate]pentanoyl]-Ile-NH2
-
[[(2S,3R)-3-amino-2-sulfhydryl-5-sulfonate]pentanoyl]-Ile-OH
-
[[(2S,3R)-3-amino-2-sulfhydryl-5-sulfonate]pentanoyl]-Tyr-Asp-OH
-
[[(2S,3R)-3-amino-2-sulfhydryl-5-sulfonate]pentanoyl]-Tyr-homosulfoalanine-OH
-
[[(2S,3R)-3-amino-5-carboxylate-2-sulfhydryl]pentanoyl]-Ile-Asp-OH
-
[[(2S,3R)-3-amino-5-phosphonate-2-sulfhydryl]pentanoyl]-Ile-Asp-OH
-
[[(2S,3S)-3-amino-2-sulfhydryl-5-sulfonate]pentanoyl]-Ile-Asp-OH
-
[[(2S,3S)-3-amino-5-carboxylate-2-sulfhydryl]pentanoyl]-Ile-Asp-OH
-
(S)-3-amino-4-mercapto-butyl sulfonic acid
i.e. EC33, a selective APA inhibitor, docking analysis in the presence of Ca2+, the ligand interacts with S1 subsite of Arg-878 in murine APA, three-dimensional structure modelling reavealing a change in the volume of the S1 subsite, which may impair the binding and/or the optimal positioning of the substrate in the active site as well as its hydrolysis, overview
(S)-3-amino-4-mercapto-butyl sulfonic acid
i.e. EC33
(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
1,10-phenanthroline
-
-
1,10-phenanthroline
-
0% residual activity at a concentration of 1 mM
1,10-phenanthroline
-
IC50 is 0.06 mM
1,10-phenanthroline
21% at 1.0 mM, complete inhibition at 10 mM
1,10-phenanthroline
-
reactivation by Co2+ or Zn2+
1,10-phenanthroline
-
complete inhibition at 1-10 mM
2-amino-4-methylsulfonyl butane thiol
-
weak inhibitor of aminopeptidase A
2-amino-4-methylsulfonyl butane thiol
-
weak inhibitor of APA
4,4'-dithio[bis(3)-aminobutylsulfonic acid]
-
RB150, a prodrug of EC33
4,4'-dithio[bis(3)-aminobutylsulfonic acid]
-
RB150, a prodrug of EC33
acetone
21.5% inhibition at 4.2% v/v
acetone
-
37.2% inhibition at 4.2% v/v
amastatin
-
-
amastatin
-
stereoisomers and analogues
amastatin
-
inhibits the enzyme and blocks the metabolism of brain angiotensin II and III
amastatin
-
IC50 is 157 nM
amastatin
-
inhibits the enzyme and blocks the metabolism of brain angiotensin II and III
amastatin
-
inhibits APA and APN
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 APA and APN
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
-
38% residual activity at a concentration of 0.03 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
-
broad specificity for various aminopeptidases
bestatin
1 mM, 13% residual activity
bestatin
-
inhibits the enzyme and blocks the metabolism of brain angiotensin II and III
bestatin
-
broad specificity for various aminopeptidases
bestatin
-
inhibits the enzyme and blocks the metabolism of brain angiotensin II and III
Ca2+
-
substrate-specific inhibition, overview
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+
-
substrate-specific inhibition, overview
Ca2+
-
Ca2+ up- or down-regulates the enzyme activity depending on the substrate tested
Ca2+
-
substrate-specific inhibition, overview
Ca2+
-
Ca2+ up- or down-regulates the enzyme activity depending on the substrate tested
Ca2+
-
substrate-specific inhibition, overview
captopril
-
-
Cd2+
-
complete inhibition at 1 mM
Cd2+
complete inhibition at 1 mM
Cd2+
-
complete inhibition at 1 mM
Cu2+
-
complete inhibition at 1 mM
Cu2+
complete inhibition at 1 mM
Cu2+
5 mM, 3.5% residual activiy
Cu2+
-
complete inhibition at 1 mM
dimethylformamide
78.1% inhibition at 4.2% v/v
dimethylformamide
-
84.9% inhibition at 4.2% v/v
dithiothreitol
-
-
DMSO
15.1% inhibition at 4.2% v/v
DMSO
-
13.9% inhibition at 4.2% v/v
DTT
-
32% activity at 0.1 mM
DTT
12% inhibition at 0.1 mM
DTT
-
69% inhibition at 0.001 mM, 94% at 0.1 mM
E64
-
slight inhibition at 1 mM
EC33
-
specific inhibition
EC33
-
highly selective APA inhibitor
EC33
-
highly selective APA inhibitor
EC33
-
highly selective APA inhibitor
EC33
-
specific inhibition
EC33
-
highly selective APA inhibitor
EDTA
-
-
EDTA
-
7% residual activity at a concentration of 5 mM
EDTA
-
83.5% activity at 5 mM
EDTA
-
reactivation by Co2+
EDTA
complete inhibition at 1.0 mM
EDTA
-
reactivation by Co2+
EDTA
-
complete inhibition at 1.0 mM
EDTA
10 mM, 3.7% residual activiy
EDTA
activity is reduced to 14% after incubating with 10 mM EDTA
EGTA
-
-
ethanol
16.3% inhibition at 4.2% v/v
ethanol
-
25.7% inhibition at 4.2% v/v
glutamate phosphonate
0.001 mM, activity of wild-type enzyme is completely abolished
glutamate phosphonate
specific aminopeptidase A inhibitor
glutamate phosphonic acid
-
glutamate phosphonic acid
-
-
Hg2+
-
complete inhibition at 1 mM
Hg2+
complete inhibition at 1 mM
Hg2+
-
complete inhibition at 1 mM
imidazole
34% inhibition at 40 mM
imidazole
-
21% inhibition at 40 mM
L-Asp
39.5% inhibition at 10 mM, no inhibition at 0.1-1.0 mM, product inhibition versus substrate L-Asp-4-nitroanilide, and 33.8% inhibition at 10 mM and no inhibition at 0.1-1.0 mM, product inhibition versus substrate L-Glu-4-nitroanilide
L-Asp
-
21.8% inhibition at 10 mM and no inhibition at 0.1-1.0 mM, product inhibition versus substrate L-Asp-4-nitroanilide, and 24.0% inhibition at 10 mM and no inhibition at 0.1-1.0 mM, product inhibition versus substrate L-Glu-4-nitroanilide
L-glutamate phosphinic acid
-
-
L-glutamate phosphinic acid
-
-
methionine thiol
-
-
Mn2+
-
inhibits the activity with Glu-substrate moderately
Mn2+
5 mM, 15% residual activiy
Ni2+
-
complete inhibition at 1 mM
Ni2+
complete inhibition at 1 mM
Ni2+
-
complete inhibition at 1 mM
o-phenanthroline
-
47.1% activity at 2 mM
o-phenanthroline
activity is reduced to 8.3% after incubating with 20 mM o-phenanthroline
PMSF
35% inhibition at 10 mM
PMSF
-
32% inhibition at 10 mM
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
SDS
73% at 1.0 mM, complete inhibition at 10 mM
SDS
-
63% at 1.0 mM, 97% inhibition at 10 mM
Zn2+
-
complete inhibition at 1 mM
Zn2+
-
68.3% activity at 0.4 mM
Zn2+
-
zinc-metallopeptidase, inhibits the activity with Glu- and Gln-substrates
Zn2+
complete inhibition at 1 mM
Zn2+
Zn2+ abolishes enzyme activity at a concentration of 1 mM
Zn2+
-
complete inhibition at 1 mM
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
-
additional information
enzyme Lb-PepA is not product-inhibited by L-Glu. Lb-PepA activity decreases significantly with metal salt concentrations above the optimum concentrations determined. Poor inhibition at 1.0 mM 2-mercaptoethanol, no inhibition by pepstatin A at 0.1-10 mM
-
additional information
-
enzyme Lb-PepA is not product-inhibited by L-Glu. Lb-PepA activity decreases significantly with metal salt concentrations above the optimum concentrations determined. Poor inhibition at 1.0 mM 2-mercaptoethanol, no inhibition by pepstatin A at 0.1-10 mM
-
additional information
enzyme Lb-PepA is not product inhibited by glutamic acid
-
additional information
no enzyme inhibition by leptin, but reduction of enzyme level in blood, although not in kidney
-
additional information
-
no enzyme inhibition by leptin, but reduction of enzyme level in blood, although not in kidney
-
additional information
ligand docking study and molecular dynamics simulations with wild-type and mutant enzymes, overview
-
additional information
-
ligand docking study and molecular dynamics simulations with wild-type and mutant enzymes, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.515 - 2.307
alpha-L-Asp-2-naphthylamide
0.243 - 2.687
alpha-L-Glu-2-naphthylamide
0.1 - 5.94
alpha-L-Glu-beta-naphthylamide
0.0391 - 12.5
alpha-L-glutamyl-beta-naphthylamide
0.062 - 2.85
angiotensin II
1.4 - 2.3
Asp-4-methylcoumaryl-7-amide
0.3273 - 0.3848
Asp-7-amido-4-methylcoumarin
0.72 - 0.846
Asp-beta-naphthylamide
-
maternal and normal serum
1.21 - 3.25
cholecystokinin-8
0.6 - 7.1
Gln-4-methylcoumaryl-7-amide
0.4 - 1.2
Glu-4-methylcoumaryl-7-amide
0.1351 - 4.36
Glu-7-amido-4-methylcoumarin
0.031 - 1.2
Glu-beta-naphthylamide
0.87 - 2.05
Glu-p-nitroanilide
0.34 - 1.21
L-Asp-4-nitroanilide
0.159 - 2.034
L-Glu-2-naphthylamide
0.19 - 25.2
L-Glu-4-nitroanilide
0.152 - 1.475
L-Glu-p-nitroanilide
additional information
additional information
-
0.515
alpha-L-Asp-2-naphthylamide
pH 7.4, 37°C, wild-type enzyme
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
0.243
alpha-L-Glu-2-naphthylamide
pH 7.4, 37°C, wild-type enzyme
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
0.1
alpha-L-Glu-beta-naphthylamide
pH 7.4, 25°C
0.16
alpha-L-Glu-beta-naphthylamide
pH 7.4, 37°C, wild-type enzyme
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+
0.87
alpha-L-Glu-beta-naphthylamide
pH 7.4, 37°C, mutant enzyme E215Q
1.5
alpha-L-Glu-beta-naphthylamide
pH 7.4, 37°C, mutant enzyme E215D
2.8
alpha-L-Glu-beta-naphthylamide
pH 7.4, 37°C, mutant enzyme E215A
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+
0.0391
alpha-L-glutamyl-beta-naphthylamide
pH 7.4, temperature not specified in the publication, recombinant His-tagged wild-type enzyme, with 4 mM Ca2+
0.165
alpha-L-glutamyl-beta-naphthylamide
pH 7.4, temperature not specified in the publication, recombinant His-tagged wild-type enzyme
0.221
alpha-L-glutamyl-beta-naphthylamide
pH 7.4, temperature not specified in the publication, recombinant His-tagged mutant R878A, with 4 mM Ca2+
0.269
alpha-L-glutamyl-beta-naphthylamide
pH 7.4, temperature not specified in the publication, recombinant His-tagged mutant R878K, with 4 mM Ca2+
1.5
alpha-L-glutamyl-beta-naphthylamide
pH 7.4, temperature not specified in the publication, recombinant His-tagged mutant R878A
12.5
alpha-L-glutamyl-beta-naphthylamide
pH 7.4, temperature not specified in the publication, recombinant His-tagged mutant R878K
0.062
angiotensin II
pH 7.4, 37°C, mutant enzyme wild-type enzyme N353A
0.073
angiotensin II
pH 7.4, 37°C, wild-type enzyme
0.161
angiotensin II
pH 7.4, 37°C, mutant enzyme wild-type enzyme N353Q
0.84
angiotensin II
-
wild-type, in the presence of 1.0 mM CaCl2
1.18
angiotensin II
-
mutant D221N, in the absence of CaCl2
1.22
angiotensin II
-
mutant D221N, in the presence of 1.0 mM CaCl2
2.85
angiotensin II
-
wild-type, in the absence of CaCl2
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
in the presence of 1 mM cobalt
0.3848
Asp-7-amido-4-methylcoumarin
in the absence of cobalt
0.21
Asp-Ala
-
-
1.21
cholecystokinin-8
-
wild-type, in the presence of 1.0 mM CaCl2
2.9
cholecystokinin-8
-
mutant D221N, in the presence of 1.0 mM CaCl2
2.93
cholecystokinin-8
-
mutant D221N, in the absence of CaCl2
3.25
cholecystokinin-8
-
wild-type, in the absence of CaCl2
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+
0.1351
Glu-7-amido-4-methylcoumarin
in the absence of cobalt
0.1363
Glu-7-amido-4-methylcoumarin
in the presence of 1 mM cobalt
0.5
Glu-7-amido-4-methylcoumarin
-
wild-type, in the presence of 1.0 mM CaCl2
1.54
Glu-7-amido-4-methylcoumarin
-
mutant D221N, in the absence of CaCl2
1.65
Glu-7-amido-4-methylcoumarin
-
mutant D221N, in the presence of 1.0 mM CaCl2
1.67
Glu-7-amido-4-methylcoumarin
-
mutant D221Q, in the absence of CaCl2
1.84
Glu-7-amido-4-methylcoumarin
-
wild-type, in the absence of 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
3.61
Glu-7-amido-4-methylcoumarin
-
mutant D221E, in the absence of CaCl2
4.31
Glu-7-amido-4-methylcoumarin
-
mutant D221A, in the presence of 1.0 mM CaCl2
4.36
Glu-7-amido-4-methylcoumarin
-
mutant D221A, in the absence of CaCl2
0.28
Glu-Ala
-
-
0.031
Glu-beta-naphthylamide
-
-
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
0.87
Glu-p-nitroanilide
-
ATA II
2.05
Glu-p-nitroanilide
-
ATA I
0.36
kallidin
-
wild-type, in the absence of CaCl2
0.37
kallidin
-
mutant D221N, in the absence of CaCl2
0.6
kallidin
-
mutant D221N, in the presence of 1.0 mM CaCl2
1.13
kallidin
-
wild-type, in the presence of 1.0 mM CaCl2
0.34
L-Asp-4-nitroanilide
-
pH 6.0, 60°C, recombinant enzyme
1.21
L-Asp-4-nitroanilide
pH 6.0, 60°C, recombinant enzyme
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+
0.19
L-Glu-4-nitroanilide
-
pH 6.0, 60°C, recombinant enzyme
25.2
L-Glu-4-nitroanilide
pH 6.0, 60°C, recombinant enzyme
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
1.84
neurokinin B
-
wild-type, in the presence of 1.0 mM CaCl2
3.97
neurokinin B
-
mutant D221N, in the absence of CaCl2
4.3
neurokinin B
-
mutant D221N, in the presence of 1.0 mM CaCl2
4.94
neurokinin B
-
wild-type, in the absence of CaCl2
additional information
additional information
kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
kinetics and substrate specificity in presence or absence of Ca2+
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
14 - 102
alpha-L-Asp-2-naphthylamide
184 - 404
alpha-L-Glu-2-naphthylamide
1.8 - 1800
alpha-L-Glu-beta-naphthylamide
3.12 - 135
alpha-L-glutamyl-beta-naphthylamide
2.8 - 12.2
Asp-4-methylcoumaryl-7-amide
0.05 - 0.354
Asp-7-amido-4-methylcoumarin
0.031 - 9.95
cholecystokinin-8
9.5 - 14.1
Gln-4-methylcoumaryl-7-amide
13.3 - 33.3
Glu-4-methylcoumaryl-7-amide
0.011 - 5.25
Glu-7-amido-4-methylcoumarin
2 - 640
L-Glu-2-naphthylamide
295 - 720
L-Glu-p-nitroanilide
0.052 - 10.47
neurokinin B
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
102
alpha-L-Asp-2-naphthylamide
pH 7.4, 37°C, wild-type enzyme
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
404
alpha-L-Glu-2-naphthylamide
pH 7.4, 37°C, wild-type enzyme
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+
19
alpha-L-Glu-beta-naphthylamide
pH 7.4, 37°C, mutant enzyme E215D
48
alpha-L-Glu-beta-naphthylamide
pH 7.4, 37°C, mutant enzyme E215A
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+
270
alpha-L-Glu-beta-naphthylamide
pH 7.4, 37°C, wild-type enzyme
1800
alpha-L-Glu-beta-naphthylamide
pH 7.4, 37°C, mutant enzyme E215Q
3.12
alpha-L-glutamyl-beta-naphthylamide
pH 7.4, temperature not specified in the publication, recombinant His-tagged mutant R878K
4.95
alpha-L-glutamyl-beta-naphthylamide
pH 7.4, temperature not specified in the publication, recombinant His-tagged mutant R878A
13.9
alpha-L-glutamyl-beta-naphthylamide
pH 7.4, temperature not specified in the publication, recombinant His-tagged wild-type enzyme
22.4
alpha-L-glutamyl-beta-naphthylamide
pH 7.4, temperature not specified in the publication, recombinant His-tagged mutant R878A, with 4 mM Ca2+
81.7
alpha-L-glutamyl-beta-naphthylamide
pH 7.4, temperature not specified in the publication, recombinant His-tagged wild-type enzyme, with 4 mM Ca2+
135
alpha-L-glutamyl-beta-naphthylamide
pH 7.4, temperature not specified in the publication, recombinant His-tagged mutant R878K, with 4 mM Ca2+
2.4
angiotensin II
pH 7.4, 37°C, mutant enzyme wild-type enzyme N353Q
2.76
angiotensin II
-
wild-type, in the absence of CaCl2
3 - 6
angiotensin II
-
wild-type, in the absence of CaCl2
3.01
angiotensin II
-
wild-type, in the presence of 1.0 mM CaCl2
3.22
angiotensin II
-
mutant D221N, in the presence of 1.0 mM CaCl2
3.88
angiotensin II
-
mutant D221N, in the absence of CaCl2
4.8
angiotensin II
pH 7.4, 37°C, mutant enzyme wild-type enzyme N353A
20
angiotensin II
pH 7.4, 37°C, wild-type enzyme
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+
0.05
Asp-7-amido-4-methylcoumarin
in the absence of cobalt
0.354
Asp-7-amido-4-methylcoumarin
in the presence of 1 mM cobalt
0.031 - 0.51
cholecystokinin-8
-
mutant D221N, in the absence of CaCl2
0.031 - 0.51
cholecystokinin-8
-
wild-type, in the presence of 1.0 mM CaCl2
0.052 - 2.1
cholecystokinin-8
-
mutant D221N, in the presence of 1.0 mM CaCl2
7.71
cholecystokinin-8
-
mutant D221N, in the absence of CaCl2
8.22
cholecystokinin-8
-
wild-type, in the presence of 1.0 mM CaCl2
9.18
cholecystokinin-8
-
wild-type, in the absence of CaCl2
9.95
cholecystokinin-8
-
mutant D221N, 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+
0.011
Glu-7-amido-4-methylcoumarin
in the absence of cobalt
0.33
Glu-7-amido-4-methylcoumarin
in the presence of 1 mM cobalt
0.58
Glu-7-amido-4-methylcoumarin
-
mutant D221A, in the presence of 1.0 mM CaCl2
0.72
Glu-7-amido-4-methylcoumarin
-
mutant D221A, in the absence of CaCl2
0.88
Glu-7-amido-4-methylcoumarin
-
mutant D221E, in the absence of 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
2.96
Glu-7-amido-4-methylcoumarin
-
mutant D221Q, in the absence of CaCl2
3.4
Glu-7-amido-4-methylcoumarin
-
mutant D221N, in the absence of CaCl2
3.41
Glu-7-amido-4-methylcoumarin
-
wild-type, in the absence of CaCl2
3.68
Glu-7-amido-4-methylcoumarin
-
mutant D221N, in the presence of 1.0 mM CaCl2
5.25
Glu-7-amido-4-methylcoumarin
-
wild-type, in the presence of 1.0 mM CaCl2
0.7
kallidin
-
wild-type, in the absence of CaCl2
0.79
kallidin
-
wild-type, in the presence of 1.0 mM CaCl2
1.33
kallidin
-
mutant D221N, in the presence of 1.0 mM CaCl2
1.55
kallidin
-
mutant D221N, in the absence of 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
0.052 - 2.1
neurokinin B
-
mutant D221N, in the absence of CaCl2
7.81
neurokinin B
-
wild-type, in the absence of CaCl2
8.87
neurokinin B
-
wild-type, in the presence of 1.0 mM CaCl2
9.8
neurokinin B
-
mutant D221N, in the presence of 1.0 mM CaCl2
10.47
neurokinin B
-
mutant D221N, in the absence of CaCl2
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0044
(1-aminopropane-1,3-diyl)bis(phosphonic acid)
-
0.00034
(3R)-3-amino-3-phosphonopropanoic acid
-
0.000314 - 0.01
(4R)-4-amino-5-sulfanylpentanoic acid
0.000268 - 0.002
(S)-3-amino-4-mercapto-butyl sulfonic acid
0.00025
(S)-3-amino-4-mercaptobutyl sulfonic acid
-
-
0.000118 - 0.0139
2,6-diaminohexane-1-thiol
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
-
0.000074 - 0.0065
4-amino-4-phosphonobutyric acid
0.105
5-amino-5-phosphonopentanoic acid
-
0.0000009
Ala-PSI[PO2-CH2]-Leu-Ala
pH 7.4, 25°C
0.0000059 - 0.0001927
amastatin
0.0271
amino(phosphono)acetic acid
-
0.395
amino[hydroxy(methyl)phosphoryl]acetic acid
-
0.00026 - 0.001297
angiotensin IV
0.0141 - 0.0289
captopril
0.0019 - 0.016
D-glutamate phosphonic acid
0.000194
Glu-PSI[PO2-CH2]-Leu
pH 7.4, 25°C
0.0000008
Glu-PSI[PO2-CH2]-Leu-Ala
pH 7.4, 25°C
0.00003
Glu-PSI[PO2-CH2]-Leu-Arg
pH 7.4, 25°C
0.0000057
Glu-PSI[PO2-CH2]-Leu-Asp
pH 7.4, 25°C
0.000037
Glu-PSI[PO2-CH2]-Leu-Leu
pH 7.4, 25°C
0.000038 - 0.056
glutamate phosphonic acid
0.00038 - 0.00206
glutamate thiol
0.00012 - 0.01
glutamate-thiol
0.000462 - 0.00202
glutamine-thiol
0.000045 - 0.021
L-glutamate phosphonic acid
0.0001 - 0.00394
lysine thiol
0.00046 - 0.0199
lysine-thiol
0.00019 - 0.0084
methionine thiol
0.000475 - 0.00918
methionine-thiol
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
0.00025
[(S)-3-amino-4-mercaptobutyl sulfonic acid]
-
-
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
0.000053 - 0.00047
[[(2R,3R)-3-amino-2-sulfhydryl-5-sulfonate]pentanoyl]-Ile-Asp-OH
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
0.0000032 - 0.000015
[[(2S,3R)-3-amino-2-sulfhydryl-5-sulfonate]pentanoyl]-Ile-Asp-OH
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
-
0.000314
(4R)-4-amino-5-sulfanylpentanoic acid
pH 7.4, temperature not specified in the publication, recombinant His-tagged wild-type enzyme, with 4 mM Ca2+
0.00157
(4R)-4-amino-5-sulfanylpentanoic acid
pH 7.4, temperature not specified in the publication, recombinant His-tagged wild-type enzyme
0.00172
(4R)-4-amino-5-sulfanylpentanoic acid
pH 7.4, temperature not specified in the publication, recombinant His-tagged mutant R878A
0.01
(4R)-4-amino-5-sulfanylpentanoic acid
pH 7.4, temperature not specified in the publication, recombinant His-tagged mutant R878K
0.000268
(S)-3-amino-4-mercapto-butyl sulfonic acid
pH 7.4, temperature not specified in the publication, recombinant His-tagged wild-type enzyme, with 4 mM Ca2+
0.00152
(S)-3-amino-4-mercapto-butyl sulfonic acid
pH 7.4, temperature not specified in the publication, recombinant His-tagged mutant R878K, with 4 mM Ca2+
0.002
(S)-3-amino-4-mercapto-butyl sulfonic acid
pH 7.4, temperature not specified in the publication, recombinant His-tagged mutant R878A, with 4 mM Ca2+
0.000118
2,6-diaminohexane-1-thiol
pH 7.4, temperature not specified in the publication, recombinant His-tagged mutant R878A
0.000317
2,6-diaminohexane-1-thiol
pH 7.4, temperature not specified in the publication, recombinant His-tagged wild-type enzyme
0.000378
2,6-diaminohexane-1-thiol
pH 7.4, temperature not specified in the publication, recombinant His-tagged mutant R878K
0.00751
2,6-diaminohexane-1-thiol
pH 7.4, temperature not specified in the publication, recombinant His-tagged mutant R878A, with 4 mM Ca2+
0.0134
2,6-diaminohexane-1-thiol
pH 7.4, temperature not specified in the publication, recombinant His-tagged wild-type enzyme, with 4 mM Ca2+
0.0139
2,6-diaminohexane-1-thiol
pH 7.4, temperature not specified in the publication, recombinant His-tagged mutant R878K, with 4 mM Ca2+
0.000074
4-amino-4-phosphonobutyric acid
pH 7.4, temperature not specified in the publication, recombinant His-tagged wild-type enzyme, with 4 mM Ca2+
0.000619
4-amino-4-phosphonobutyric acid
pH 7.4, temperature not specified in the publication, recombinant His-tagged mutant R878K, with 4 mM Ca2+
0.0065
4-amino-4-phosphonobutyric acid
pH 7.4, temperature not specified in the publication, recombinant His-tagged mutant R878A, with 4 mM Ca2+
0.0000059
amastatin
-
mutant D221, in the presence of 1 mM CaCl2
0.0000177
amastatin
-
mutant D221, in the absence of CaCl2
0.0000243
amastatin
-
wild-type enzyme, in the absence of CaCl2
0.0001927
amastatin
-
wild-type enzyme, in the presence of 1 mM CaCl2
0.00026
angiotensin IV
-
mutant D221, in the absence of CaCl2
0.000324
angiotensin IV
-
mutant D221, in the presence of 1 mM CaCl2
0.000386
angiotensin IV
-
wild-type enzyme, in the absence of CaCl2
0.001297
angiotensin IV
-
wild-type enzyme, in the presence of 1 mM CaCl2
0.0141
captopril
pH 7.4, 37°C, mutant enzyme N363Q
0.0248
captopril
pH 7.4, 37°C, mutant enzyme N363A
0.0289
captopril
pH 7.4, 37°C, wild-type enzyme
0.0019
D-glutamate phosphonic acid
pH 7.4, 37°C, wild-type enzyme
0.00331
D-glutamate phosphonic acid
pH 7.4, 37°C, wild-type enzyme
0.00489
D-glutamate phosphonic acid
pH 7.4, 37°C, mutant enzyme N363Q
0.005
D-glutamate phosphonic acid
pH 7.4, 37°C, mutant enzyme E215D
0.011
D-glutamate phosphonic acid
pH 7.4, 37°C, mutant enzyme E215A
0.0112
D-glutamate phosphonic acid
pH 7.4, 37°C, mutant enzyme N363A
0.016
D-glutamate phosphonic acid
pH 7.4, 37°C, mutant enzyme E215Q
0.000038
glutamate phosphonic acid
pH 7.4, 37°C, wild-type enzyme, 4 mM Ca2+
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+
0.00287
glutamate phosphonic acid
pH 7.4, 37°C, wild-type enzyme, no 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+
0.00012
glutamate-thiol
pH 7.4, 37°C, wild-type enzyme, 4 mM Ca2+
0.000147
glutamate-thiol
pH 7.4, 37°C, wild-type enzyme
0.000216
glutamate-thiol
pH 7.4, 37°C, wild-type enzyme
0.00034
glutamate-thiol
pH 7.4, 37°C, mutant enzyme E215Q
0.00036
glutamate-thiol
pH 7.4, 37°C, wild-type enzyme, 0.025 mM Ca2+
0.00137
glutamate-thiol
pH 7.4, 37°C, mutant enzyme N363Q
0.00167
glutamate-thiol
pH 7.4, 37°C, wild-type enzyme, no Ca2+
0.002
glutamate-thiol
pH 7.4, 37°C, mutant enzyme N363A
0.00227
glutamate-thiol
pH 7.4, 37°C, mutant enzyme H450F, 4 mM Ca2+
0.00524
glutamate-thiol
pH 7.4, 37°C, mutant enzyme H450F, 0.025 mM Ca2+
0.0072
glutamate-thiol
pH 7.4, 37°C, mutant enzyme E215D
0.01
glutamate-thiol
pH 7.4, 37°C, mutant enzyme E215A
0.000462
glutamine-thiol
pH 7.4, 37°C, wild-type enzyme
0.00199
glutamine-thiol
pH 7.4, 37°C, mutant enzyme N363A
0.00202
glutamine-thiol
pH 7.4, 37°C, mutant enzyme N363Q
0.000045
L-glutamate phosphonic acid
pH 7.4, 37°C, wild-type enzyme
0.00006
L-glutamate phosphonic acid
pH 7.4, 37°C, wild-type enzyme
0.000214
L-glutamate phosphonic acid
pH 7.4, 37°C, mutant enzyme N363Q
0.00026
L-glutamate phosphonic acid
pH 7.4, 37°C, mutant enzyme E215Q
0.000395
L-glutamate phosphonic acid
pH 7.4, 37°C, mutant enzyme N363A
0.012
L-glutamate phosphonic acid
pH 7.4, 37°C, mutant enzyme E215D
0.021
L-glutamate phosphonic acid
pH 7.4, 37°C, mutant enzyme E215A
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+
0.00046
lysine-thiol
pH 7.4, 37°C, wild-type enzyme, Ca2+
0.00047
lysine-thiol
pH 7.4, 37°C, wild-type enzyme, 0.025 mM Ca2+
0.0012
lysine-thiol
pH 7.4, 37°C, mutant enzyme H450F, 0.025 mM Ca2+
0.0072
lysine-thiol
pH 7.4, 37°C, wild-type enzyme, 4 mM Ca2+
0.0199
lysine-thiol
pH 7.4, 37°C, mutant enzyme H450F, 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+
0.000475
methionine-thiol
pH 7.4, temperature not specified in the publication, recombinant His-tagged mutant R878A
0.00075
methionine-thiol
pH 7.4, temperature not specified in the publication, recombinant His-tagged wild-type enzyme
0.00125
methionine-thiol
pH 7.4, temperature not specified in the publication, recombinant His-tagged mutant R878K
0.00322
methionine-thiol
pH 7.4, temperature not specified in the publication, recombinant His-tagged mutant R878A
0.00514
methionine-thiol
pH 7.4, temperature not specified in the publication, recombinant His-tagged mutant R878K
0.00918
methionine-thiol
pH 7.4, temperature not specified in the publication, recombinant His-tagged wild-type enzyme, with 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
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A soluble aspartate aminopeptidase from dog kidney
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