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Information on EC 3.4.11.7 - glutamyl aminopeptidase
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3.4.11.7 glutamyl aminopeptidaseSpecify your search results
Word Map
- 3.4.11.7
- apa
- aminopeptidases
-
renin-angiotensin
- renin
-
dipeptidyl
-
hypertensive
- ras
- amastatin
-
brush
-
angiotensin-converting
-
antihypertensive
-
alanyl
- bestatin
- vasopressin
-
pressor
-
dipeptidylpeptidase
- losartan
-
exopeptidase
- enpep
-
arylamide
-
intracerebroventricularly
- angiotensinogen
- medicine
- sucrase-isomaltase
-
pyroglutamyl
-
3.2.1.20
-
puromycin-sensitive
-
ras-regulating
-
insulin-regulated
- oxytocinase
-
kininase
- beta-naphthylamide
- microvillar
- synthesis
- diagnostics
- drug development
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
release of N-terminal glutamate (and to a lesser extent aspartate) from a peptide
Synonyms
acid aminopeptidase, acidic alpha-aminopeptidase, Aminopeptidase, aminopeptidase A, aminopeptidase A ectopeptidase, aminopeptidase, aspartate, aminopeptidase-A, angiotensinase, angiotensinase A, antigen BP-1/6C3 of mouse B lymphocytes, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acid aminopeptidase
acidic alpha-aminopeptidase
aminopeptidase A
aminopeptidase, aspartate
-
-
-
-
aminopeptidase-A
angiotensinase A
AP A
APA
aspartate aminopeptidase
BP-1/6C3 antigen
BP1/6C3
Ca2+-activated glutamate aminopeptidase
Differentiation antigen gp160
-
-
-
-
EAP
ENPEP
GAP
GluAP
glutamyl (aspartyl)-specific aminopeptidase A
glutamyl aminopeptidase
glutamyl aminopeptidase (Lactococcus)
glutamyl peptidase
-
-
-
-
L-alpha-aspartyl(L-alpha-glutamyl)-peptide hydrolase
-
-
-
-
L-aspartate aminopeptidase
-
-
-
-
Lb-PepA
Lc-PepA
mAPA
membrane aminopeptidase II
MHJ_0125
PepA
additional information
aminopeptidase A
-
-
-
-
aminopeptidase A
-
-
aminopeptidase A
-
-
angiotensinase A
-
-
-
-
APA
-
-
-
-
aspartate aminopeptidase
-
-
-
-
BP-1/6C3 antigen
-
-
-
-
Ca2+-activated glutamate aminopeptidase
-
-
-
-
EAP
-
-
-
-
glutamyl (aspartyl)-specific aminopeptidase A
-
glutamyl (aspartyl)-specific aminopeptidase A
-
-
glutamyl aminopeptidase
-
-
-
-
membrane aminopeptidase II
-
-
-
-
additional information
-
the enzyme belongs to the zinc-metallopeptidase family of zincins
additional information
see also EC 3.4.11.21
-
additional information
-
the enzyme belongs to peptidase family M42
additional information
-
the enzyme belongs to the zinc-metallopeptidase family of zincins
additional information
-
the enzyme belongs to the zinc-metallopeptidase family of zincins
additional information
-
the enzyme belongs to the zinc-metallopeptidase family of zincins
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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
-
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
-
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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 SOURCE
PATHWAYS
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CAS REGISTRY NUMBER
COMMENTARY
9074-83-3
-
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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
alpha-L-aspartate-beta-naphthylamide + H2O
L-aspartate + beta-naphthylamine
high activity
-
-
?
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 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
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
assay for measuring aspartyl aminopeptidase activity
-
-
?
Gly-7-amido-4-methylcoumarin + H2O
Gly + 7-amino-4-methylcoumarin
-
-
-
?
kallidin + H2O
Lys + bradykinin
-
i.e. Lys-bradykinin or KRPPGFSPFR, the reaction is performed only in absence of Ca2+
i.e. RPPGFSPFR
-
?
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-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
L-aspartate-beta-naphthylamide + H2O
L-aspartate + beta-naphthylamine
-
-
-
?
L-glutamyl-beta-naphthylamide + H2O
L-glutamine + beta-naphthylamine
-
-
-
?
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
-
-
?
N-Glu-L-Phe-4-nitroanilide + H2O
L-Glu + L-Phe-4-nitroanilide
-
-
-
-
?
alpha-L-Glu-beta-naphthylamide + H2O
L-Glu + 2-naphthylamine
-
-
-
?
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
Latilactobacillus curvatus DBPZ1009
-
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
Lactiplantibacillus paraplantarum DBPZ0997
-
peptidase activity assay
-
-
?
Glu-p-nitroanilide + H2O
glutamic acid + p-nitroaniline
-
peptidase activity assay
-
-
?
Glu-p-nitroanilide + H2O
glutamic acid + p-nitroaniline
Lactiplantibacillus pentosus DBPZ0984
-
peptidase activity assay
-
-
?
Glu-p-nitroanilide + H2O
glutamic acid + p-nitroaniline
-
peptidase activity assay
-
-
?
Glu-p-nitroanilide + H2O
glutamic acid + p-nitroaniline
Lactiplantibacillus plantarum DBPZ0987
-
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-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
Lactococcus lactis ssp. lactis DSM 20481
-
-
-
-
?
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-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
Lactococcus lactis ssp. lactis DSM 20481
-
-
-
-
?
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
-
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-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)-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
?
-
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
?
-
-
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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NATURAL SUBSTRATE
NATURAL 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 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+
Cu2+
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
Ca2+
localized at the bottom of the S1 subsite, activates the enzyme and plays a key role of Arg878 together with Ca2 + in APA substrate specificity for N-terminal acidic amino acid residues by ensuring the optimal positioning of acidic substrates during catalysis. The Ca2+ atom interacts with the acidic side chains of Asp213 and Asp218, the carbonyl group of Glu215 and three water molecules, one of them being engaged in a hydrogen bond with the negatively charged carboxylate side chains of the inhibitors. Ca2+ activation profile of purified recombinant wild-type and mutated His-mAPAs, using an acidic substrate alpha-L-glutamyl-beta-naphthylamide, overview. Enzyme residue Arg878 does not contribute to Ca2+ binding in the S1 subsite
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+
a zinc metalloprotease, Zn2+ atom is coordinated by the two histidine residues, His385 and His389, of the HEXXH motif, a water molecule, Glu408 of the WLNEG motif and either by one of the oxygen atoms of the phosphate of GluPO3H2, three-dimensional structure modelling
Zn2+
-
zinc-metallopeptidase, the enzyme contains the zinc-binding motif HEXXH
additional information
Lb-PepA activity decreases significantly with metal salt concentrations above the optimum concentrations determined
additional information
-
Lb-PepA activity decreases significantly with metal salt concentrations above the optimum concentrations determined
additional information
PepA ia a metallopeptidase. The metal center can be described as [M1M2-enzyme], where M1 and M2 indicate the type of metal ion in site 1 and site 2. The activity and reaction kinetics, as well as the pH and temperature profile differ depending on the metal ion used in the reaction or reactivation. Quantification of activity of reactivated recombinant apo-PepA with different metal ions, overview
additional information
-
Lc-PepA activity decreases only slightly or is almost constant with metal salt concentrations above the optimum concentrations determined
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INHIBITOR
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
-
3-[[amino(carboxy)methyl](hydroxy)phosphoryl]-2-methylpropanoic acid
-
4-amino-4-phosphonobutyric acid
a specific and selective APA inhibitor, a linear competitive inhibitor
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+
-
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
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]-Ile-3-sulfoalanine-OH
-
[[(2R,3R)-3-amino-2-sulfhydryl-5-sulfonate]pentanoyl]-Tyr-homosulfoalanine-OH
-
[[(2S,3R)-3-amino-2-sulfhydryl-5-sulfonate]pentanoyl]-Ile-3-sulfoalanine-OH
-
[[(2S,3R)-3-amino-2-sulfhydryl-5-sulfonate]pentanoyl]-Tyr-homosulfoalanine-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-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
21% at 1.0 mM, complete inhibition at 10 mM
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
dimethylformamide
78.1% inhibition at 4.2% v/v
EDTA
activity is reduced to 14% after incubating with 10 mM EDTA
glutamate phosphonate
0.001 mM, activity of wild-type enzyme is completely abolished
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
o-phenanthroline
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
SDS
73% at 1.0 mM, complete inhibition at 10 mM
Zn2+
-
zinc-metallopeptidase, inhibits the activity with Glu- and Gln-substrates
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
-
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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
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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+
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
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
0.6
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
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
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+
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
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
-
kinetics and substrate specificity in presence or absence of Ca2+
-
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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+
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+
2.8
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
in the presence of 1 mM cobalt
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
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
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kcat/KM VALUE [1/mMs-1]
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