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Information on EC 3.4.11.6 - aminopeptidase B
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3.4.11.6 aminopeptidase BSpecify your search results
Word Map
- 3.4.11.6
-
abductor
- brevis
-
pollicis
-
transcranial
- 2-amino-4-phosphonobutyrate
- retina
-
minimi
-
latency
-
digiti
- bestatin
-
thumb
-
corticospinal
-
voluntary
-
cmaps
- erg
-
intracortical
-
wrist
-
interosseous
- tibialis
-
ulnar
-
thenar
-
motor-evoked
-
flexor
-
electroretinogram
-
amacrine
-
photopic
-
anoxygenic
-
off-center
-
f-waves
- amastatin
-
paired-pulse
-
interstimulus
-
radialis
-
biceps
-
brachii
-
alt-associated
-
dark-adapted
-
electromyographic
- quisqualate
-
antiphase
- beta-naphthylamide
-
carpi
-
3.4.11.1
-
imagery
- drug development
- alpha-fucosidase
-
hallucis
-
interhemispheric
-
light-evoked
-
short-latency
-
puromycin-sensitive
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
release of N-terminal Arg and Lys from oligopeptides when P1' is not Pro. Also acts on arylamides of Arg and Lys
Synonyms
AAP, ACE2, Aminopeptidase, aminopeptidase B, aminopeptidase, arginine, aminopeptidase-B, Ap-B, APB, Arg-AP, Arg/Lys aminopeptidase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AAP
ACE2
aminopeptidase B
aminopeptidase, arginine
-
-
-
-
Ap-B
APB
Arg/Lys aminopeptidase
arginine aminopeptidase
arginyl aminopeptidase
arylamidase II
-
-
-
-
Cl--activated arginine aminopeptidase
-
-
-
-
cytosol aminopeptidase
-
-
-
-
DAP BII
dipeptidyl aminopeptidase BII
L-arginine aminopeptidase
-
-
-
-
leukocyte-derived arginine aminopeptidase
RAP
additional information
arginine aminopeptidase
-
-
-
-
arginyl aminopeptidase
-
-
-
-
additional information
-
the enzyme belongs to the M1 peptidase family
additional information
-
the enzyme belongs to the M1 peptidase family, and is distinct from the leukotriene A4 hydrolase, bleomycin hydrolase, and puromycin-sensitive aminopeptidase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
release of N-terminal Arg and Lys from oligopeptides when P1' is not Pro. Also acts on arylamides of Arg and Lys
release of N-terminal Arg and Lys from oligopeptides when P1' is not Pro. Also acts on arylamides of Arg and Lys
-
-
-
-
release of N-terminal Arg and Lys from oligopeptides when P1' is not Pro. Also acts on arylamides of Arg and Lys
exopeptidase, no endoprotease activity, the enzyme is strictly specific for the removal of N-terminal basic residues from peptides and proteins, no activity with substrates possessing Pro at the P1 position
-
release of N-terminal Arg and Lys from oligopeptides when P1' is not Pro. Also acts on arylamides of Arg and Lys
exopeptidase, the enzyme is strictly specific for the removal of N-terminal basic residues from peptides and proteins, no activity with substrate possessing Pro at the P1 position
-
release of N-terminal Arg and Lys from oligopeptides when P1' is not Pro. Also acts on arylamides of Arg and Lys
exopeptidase, the enzyme is strictly specific for the removal of N-terminal basic residues from peptides and proteins, no activity with substrate possessing Pro at the P1 position
-
release of N-terminal Arg and Lys from oligopeptides when P1' is not Pro. Also acts on arylamides of Arg and Lys
exopeptidase, the enzyme is strictly specific for the removal of N-terminal basic residues from peptides and proteins, no activity with substrate possessing Pro at the P1 position
-
release of N-terminal Arg and Lys from oligopeptides when P1' is not Pro. Also acts on arylamides of Arg and Lys
exopeptidase, the enzyme is strictly specific for the removal of N-terminal basic residues from peptides and proteins, no activity with substrates possessing Pro at the P1 position
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
hydrolysis of peptide bond
-
-
exopeptidase, N-terminus, amino acid
-
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CAS REGISTRY NUMBER
COMMENTARY
9073-92-1
-
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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
Ala-4-nitroanilide + H2O
Ala + 4-nitroaniline
-
4.6% of the activity with Leu-4-nitroanilide
-
?
alpha-Glu-4-nitroanilide + H2O
Glu + 4-nitroaniline
-
564% of the activity with Leu-4-nitroanilide
-
?
Arg-4-methylcoumaryl-7-amide + H2O
Arg + 7-amino-4-methylcoumarin
-
-
?
Arg-Ala + H2O
Arg + Ala
-
82% of the activity with Arg-Arg
-
?
Arg-alpha-atrial natriuretic factor1-20 + H2O
Arg + alpha-atrial natriuretic factor1-20
-
-
-
-
?
Arg-Asp + H2O
Arg + Asp
-
25% of the activity with Arg-Arg
-
?
Arg-beta-atrial natriuretic factor1-20 + H2O
Arg + beta-atrial natriuretic factor1-20
-
-
-
-
?
Arg-beta-naphthylamide + H2O
L-arginine + 2-naphthylamine
-
substrate used in the activity assay
-
-
?
Arg-Gly-Asp-Ser-Pro-Ala-Ser-Ser-Lys-Pro + H2O
Arg + Gly-Asp-Ser-Pro-Ala-Ser-Ser-Lys-Pro
i.e. fibronectin-binding inhibitor
-
?
Arg-Gly-Glu-Ser + H2O
Arg + Gly-Glu-Ser
i.e. platelet aggregation inhibitor
-
?
Arg-Gly-Pro-Phe-Pro-Ile + H2O
Arg + Gly-Pro-Phe-Pro-Ile
i.e. sexual agglutination peptide
-
?
Arg-Ile + H2O
Arg + Ile
-
32% of the activity with Arg-Arg
-
?
Arg-Leu + H2O
Arg + Leu
-
25% of the activity with Arg-Arg
-
?
Arg-Lys + H2O
Arg + Lys
-
88% of the activity with Arg-Arg
-
?
Arg-Lys-somatostatin-14 + H2O
Arg + Lys + somatostatin-14
-
sequential removal of basic N-terminal residues
-
-
?
Arg-Phe-Ala-Arg-Lys-Gly-Ala-Leu-Arg-Gln-Lys-Asn-Val + H2O
Arg + Phe-Ala-Arg-Lys-Gly-Ala-Leu-Arg-Gln-Lys-Asn-Val
i.e. protein kinase C substrate
-
?
Arg-Pro-Lys-Pro-Gln-Gly-Leu-Met + H2O
Arg + Pro-Lys-Pro-Gln-Gly-Leu-Met
i.e. substance P
-
?
Arg-Val-Tyr-Ile-His-Pro-Ile + H2O
Arg + Val-Tyr-Ile-His-Pro-Ile
i.e. angiotensin III
-
?
Arg-Val-Tyr-Ile-His-Pro-Phe + H2O
Arg + Val-Tyr-Ile-His-Pro-Phe
-
angiotensin III
-
-
?
azocasein + H2O
protein fragments of azocasein of MW 71 kDa, 83 kDa, and 22 kDa
-
-
-
-
?
Cys-Gly + H2O
Cys + Gly
-
4210% of the activity with Leu-4-nitroanilide
-
?
Gly-4-nitroanilide + H2O
Gly + 4-nitroaniline
-
1.3% of the activity with Leu-4-nitroanilide
-
?
Gly-L-Pro-2-naphthylamide + H2O
Gly-L-Pro + 2-naphthylamine
-
1% activity compared to L-Lys-2-naphthylamide
-
-
?
L-Ala-Ala-Pro-Leu-4-nitroanilide + H2O
L-Ala-Ala-Pro-Leu + 4-nitroaniline
-
-
-
-
?
L-Arg 7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
-
fluorogenic substrate, best substrate
-
-
?
L-Arg-L-Tyr-Gly-Gly-L-Phe-L-Leu + H2O
L-Arg + L-Tyr-Gly-Gly-L-Phe-L-Leu
-
-
-
-
?
L-Arg-peptide + H2O
L-Arg + peptide
-
specific for N-terminal Arg or Lys residues, di-, tri-, and polypeptides
-
-
?
L-arginine-2-naphthylamide + H2O
2-naphthylamine + L-Arg
-
assay at 37°C
-
-
?
L-Asn-7-amido-4-methylcoumarin + H2O
L-Asn + 7-amino-4-methylcoumarin
53% activity compared to L-Arg-7-amido-4-methylcoumarin
-
-
?
L-Asp-7-amido-4-methylcoumarin + H2O
L-Asp + 7-amino-4-methylcoumarin
15% activity compared to L-Arg-7-amido-4-methylcoumarin
-
-
?
L-beta-Asn-2-naphthylamide + H2O
L-beta-Asn + 2-naphthylamine
-
9% activity compared to L-Lys-2-naphthylamide
-
-
?
L-Cys-2-naphthylamide + H2O
L-Cys + 2-naphthylamine
-
1% activity compared to L-Lys-2-naphthylamide
-
-
?
L-Cys-7-amido-4-methylcoumarin + H2O
L-Cys + 7-amino-4-methylcoumarin
-
5% activity compared to L-Arg-7-amido-4-methylcoumarin
-
-
?
L-Gln-7-amido-4-methylcoumarin + H2O
L-Gln + 7-amino-4-methylcoumarin
about 1% activity compared to L-Arg-7-amido-4-methylcoumarin
-
-
?
L-Gly-L-Arg-2-naphthylamide + H2O
L-Gly-L-Arg + 2-naphthylamine
-
250% activity compared to L-Lys-2-naphthylamide
-
-
?
L-His-2-naphthylamide + H2O
L-His + 2-naphthylamine
-
15% activity compared to L-Lys-2-naphthylamide
-
-
?
L-Ile-7-amido-4-methylcoumarin + H2O
L-Ile + 7-amino-4-methylcoumarin
about 1% activity compared to L-Arg-7-amido-4-methylcoumarin
-
-
?
L-Leu 7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
-
fluorogenic substrate
-
-
?
L-Lys-L-Ala-2-naphthylamide + H2O
L-Lys-L-Ala + 2-naphthylamine
-
7% activity compared to L-Lys-2-naphthylamide
-
-
?
L-Lys-peptide + H2O
L-Lys + peptide
-
specific for N-terminal Arg or Lys residues, di-, tri-, and polypeptide
-
-
?
L-Phe-2-naphthylamide + H2O
L-Phe + 2-naphthylamine
-
0.171% activity compared to L-Arg-2-naphthylamide
-
-
?
L-Pro-7-amido-4-methylcoumarin + H2O
L-Pro + 7-amino-4-methylcoumarin
-
7% activity compared to L-Arg-7-amido-4-methylcoumarin
-
-
?
L-Ser-7-amido-4-methylcoumarin + H2O
L-Ser + 7-amino-4-methylcoumarin
15% activity compared to L-Arg-7-amido-4-methylcoumarin
-
-
?
L-Tyr 7-amido-4-methylcoumarin + H2O
L-Tyr + 7-amino-4-methylcoumarin
-
fluorogenic substrate
-
-
?
L-Tyr-7-amido-4-methylcoumarin + H2O
L-Tyr + 7-amino-4-methylcoumarin
about 7% activity compared to L-Arg-7-amido-4-methylcoumarin
-
-
?
L-Val-2-naphthylamide + H2O
L-Val + 2-naphthylamine
-
0.034% activity compared to L-Arg-2-naphthylamide
-
-
?
L-Val-4-nitroanilide + H2O
L-Val + 4-nitroaniline
low activity
-
-
?
L-Val-7-amido-4-methylcoumarin + H2O
L-Val + 7-amino-4-methylcoumarin
about 1% activity compared to L-Arg-7-amido-4-methylcoumarin
-
-
?
Leu-Gly + H2O
Leu + Gly
-
1200% of the activity with Leu-4-nitroanilide
-
?
leukotriene A4 + H2O
L-Arg + leukotriene B4
-
weak in vitro activity
-
-
?
leukotriene A4 + H2O
leukotriene B4 + ?
-
has a residual catalytic ability to hydrolyze leukotriene A4
-
-
?
Lys-4-methylcoumarin 7-amide + H2O
Lys + 7-amino-4-methylcoumarin
-
-
-
-
?
Lys-7-amido-4-methylcoumarin + H2O
Lys + 7-amino-4-methylcoumarin
-
4.3% of the activity with Arg-7-amido-4-methylcoumarin
-
?
Lys-Ala + H2O
Lys + Ala
-
88% of the activity with Arg-Arg
-
?
Lys-Lys + H2O
Lys + Lys
-
30% of the activity with Arg-Arg
-
?
Met-4-nitroanilide + H2O
Met + 4-nitroaniline
-
40.6% of the activity with Leu-4-nitroanilide
-
?
N-p-tosyl-Gly-Pro-Lys-p-nitroanilide + H2O
N-p-tosyl-Gly-Pro-Lys + p-nitroaniline
-
-
-
-
?
N-succinyl-Gly-Pro-Leu-Gly-Pro 7-amido-4-methylcoumarin + H2O
N-succinyl-Gly-Pro-Leu-Gly-Pro + 7-amino-4-methylcoumarin
-
fluorogenic substrate
-
-
?
Val-4-nitroanilide + H2O
Val + 4-nitroaniline
-
1.2% of the activity with Leu-4-nitroanilide
-
?
[Arg0]-Met-enkephalin + H2O
Met-enkephalin + de-[Tyr]-Met-enkephalin
i.e. RYGGFM
-
-
?
Ala-Ala 4-nitroanilide + H2O
Ala-Ala + 4-nitroaniline
-
-
-
?
Ala-Ala 4-nitroanilide + H2O
Ala-Ala + 4-nitroaniline
-
-
-
?
Arg-4-methylcoumarin 7-amide + H2O
Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Arg-4-methylcoumarin 7-amide + H2O
Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Arg-4-nitroanilide + H2O
Arg + 4-nitroaniline
-
2.5% of the activity with Leu-4-nitroanilide
-
?
Arg-4-nitroanilide + H2O
Arg + 4-nitroaniline
-
as active as Arg-7-amido-4-methylcoumarin
-
?
Arg-7-amido-4-methylcoumarin + H2O
Arg + 7-amino-4-methylcoumarin
-
-
-
?
Arg-peptides + H2O
?
-
attribution to inflammatory and wound healing processes
-
-
?
Arg-peptides + H2O
?
-
takes part in later stages of protein degradation in chloroplasts
-
-
?
Arg-Phe + H2O
Arg + Phe
-
35% of the activity with Arg-Arg
-
?
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg + Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
i.e. bradykinin
-
?
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg + Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
i.e. bradykinin
-
?
Gly-2-naphthylamide + H2O
Gly + 2-naphthylamine
-
1% activity compared to L-Lys-2-naphthylamide
-
-
?
Gly-2-naphthylamide + H2O
Gly + 2-naphthylamine
-
less than 0.02% activity compared to L-Arg-2-naphthylamide
-
-
?
Gly-Phe 4-nitroanilide + H2O
Gly-Phe + 4-nitroaniline
-
-
-
?
Gly-Phe 4-nitroanilide + H2O
Gly-Phe + 4-nitroaniline
-
-
-
?
L-Ala-2-naphthylamide + H2O
L-Ala + 2-naphthylamine
-
0.1% activity compared to L-Arg-2-naphthylamide
-
-
?
L-Ala-2-naphthylamide + H2O
L-Ala + 2-naphthylamine
-
83% activity compared to L-Lys-2-naphthylamide
-
-
?
L-Ala-4-nitroanilide + H2O
L-Ala + 4-nitroaniline
low activity
-
-
?
L-Ala-7-amido-4-methylcoumarin + H2O
L-Ala + 7-amino-4-methylcoumarin
-
best substrate
-
-
?
L-Ala-7-amido-4-methylcoumarin + H2O
L-Ala + 7-amino-4-methylcoumarin
about 2% activity compared to L-Arg-7-amido-4-methylcoumarin
-
-
?
L-Ala-7-amido-4-methylcoumarin + H2O
L-Ala + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Arg-2-naphthylamide + H2O
L-Arg + 2-naphthylamine
-
-
-
-
?
L-Arg-2-naphthylamide + H2O
L-Arg + 2-naphthylamine
-
17% activity compared to L-Lys-2-naphthylamide
-
-
?
L-Arg-4-nitroanilide + H2O
L-Arg + 4-nitroaniline
best substrate
-
-
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
100% activity
-
-
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
-
high activity
-
-
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
Corycaeus anglicus
-
-
-
-
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
100% activity
-
-
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
-
100% activity
-
-
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
-
best substrate
-
-
?
L-Leu-2-naphthylamide + H2O
L-Leu + 2-naphthylamine
-
31% activity compared to L-Lys-2-naphthylamide
-
-
?
L-Leu-7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
28% activity compared to L-Arg-7-amido-4-methylcoumarin
-
-
?
L-Leu-7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Leu-7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
about 1% activity compared to L-Arg-7-amido-4-methylcoumarin
-
-
?
L-Leu-7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Lys-2-naphthylamide + H2O
L-Lys + 2-naphthylamine
-
-
-
-
?
L-Lys-2-naphthylamide + H2O
L-Lys + 2-naphthylamine
-
41% activity compared to L-Arg-2-naphthylamide
-
-
?
L-Lys-7-amido-4-methylcoumarin + H2O
L-Lys + 7-amino-4-methylcoumarin
10% activity compared to L-Arg-7-amido-4-methylcoumarin
-
-
?
L-Lys-7-amido-4-methylcoumarin + H2O
L-Lys + 7-amino-4-methylcoumarin
about 45% activity compared to L-Arg-7-amido-4-methylcoumarin
-
-
?
L-Lys-7-amido-4-methylcoumarin + H2O
L-Lys + 7-amino-4-methylcoumarin
-
17% activity compared to L-Arg-7-amido-4-methylcoumarin
-
-
?
L-Met-2-naphthylamide + H2O
L-Met + 2-naphthylamine
-
2% activity compared to L-Lys-2-naphthylamide
-
-
?
L-Met-7-amido-4-methylcoumarin + H2O
L-Met + 7-amino-4-methylcoumarin
19% activity compared to L-Arg-7-amido-4-methylcoumarin
-
-
?
L-Met-7-amido-4-methylcoumarin + H2O
L-Met + 7-amino-4-methylcoumarin
about 1% activity compared to L-Arg-7-amido-4-methylcoumarin
-
-
?
L-Met-7-amido-4-methylcoumarin + H2O
L-Met + 7-amino-4-methylcoumarin
-
no activity with Z-Met-7-amido-4-methylcoumarin
-
-
?
L-Phe-7-amido-4-methylcoumarin + H2O
L-Phe + 7-amino-4-methylcoumarin
about 5% activity compared to L-Arg-7-amido-4-methylcoumarin
-
-
?
L-Phe-7-amido-4-methylcoumarin + H2O
L-Phe + 7-amino-4-methylcoumarin
-
2% activity compared to L-Arg-7-amido-4-methylcoumarin
-
-
?
L-Phe-7-amido-4-methylcoumarin + H2O
L-Phe + 7-amino-4-methylcoumarin
-
low activity
-
-
?
L-Tyr-2-naphthylamide + H2O
L-Tyr + 2-naphthylamine
-
0.171% activity compared to L-Arg-2-naphthylamide
-
-
?
L-Tyr-2-naphthylamide + H2O
L-Tyr + 2-naphthylamine
-
62% activity compared to L-Lys-2-naphthylamide
-
-
?
Leu-4-nitroanilide + H2O
Leu + 4-nitroaniline
7% of the activity with Arg-4-nitroanilide
-
?
Leu-4-nitroanilide + H2O
Leu + 4-nitroaniline
7% of the activity with Arg-4-nitroanilide
-
?
Lys-2-naphthylamide + H2O
Lys + 2-naphthylamine
-
-
-
-
?
Lys-4-nitroanilide + H2O
Lys + 4-nitroaniline
-
3.6% of the activity with Arg-7-amido-4-methylcoumarin
-
?
Lys-4-nitroanilide + H2O
Lys + 4-nitroaniline
5% of the activity with Arg-4-nitroanilide
-
?
additional information
?
-
substrate specificity, 4-nitroanilides of Gly, Glu, Asp, Phe, Pro, and Ala-Pro are poor substrates, overview
-
-
?
additional information
?
-
-
substrate specificity, 4-nitroanilides of Gly, Glu, Asp, Phe, Pro, and Ala-Pro are poor substrates, overview
-
-
?
additional information
?
-
-
no hydrolysis of amino acids with apolar groups, without free alpha-amino group, or anionic amino acids
-
-
?
additional information
?
-
-
the enzyme probably is involved in the final stages of peptide and protein precursor processing and maturation mechanisms via the exopeptidase pathway and thereby in some inflammatory processes and tumour development
-
-
?
additional information
?
-
-
the enzyme from testis preferably removes Arg and/or Lys residues from the N-terminus of various peptides, no activity with substrate possessing Pro at the P1 position
-
-
?
additional information
?
-
no activity with L-Ala-7-amido-4-methylcoumarin, L-Cys-7-amido-4-methylcoumarin, L-Gln-7-amido-4-methylcoumarin, L-Glu-7-amido-4-methylcoumarin, Gly-7-amido-4-methylcoumarin, L-His-7-amido-4-methylcoumarin, L-Ile-7-amido-4-methylcoumarin, L-Phe-7-amido-4-methylcoumarin, L-Pro-7-amido-4-methylcoumarin, L-Thr-7-amido-4-methylcoumarin, L-Trp-7-amido-4-methylcoumarin, L-Tyr-7-amido-4-methylcoumarin, and L-Val-7-amido-4-methylcoumarin
-
-
?
additional information
?
-
-
no activity with L-Ala-7-amido-4-methylcoumarin, L-Cys-7-amido-4-methylcoumarin, L-Gln-7-amido-4-methylcoumarin, L-Glu-7-amido-4-methylcoumarin, Gly-7-amido-4-methylcoumarin, L-His-7-amido-4-methylcoumarin, L-Ile-7-amido-4-methylcoumarin, L-Phe-7-amido-4-methylcoumarin, L-Pro-7-amido-4-methylcoumarin, L-Thr-7-amido-4-methylcoumarin, L-Trp-7-amido-4-methylcoumarin, L-Tyr-7-amido-4-methylcoumarin, and L-Val-7-amido-4-methylcoumarin
-
-
?
additional information
?
-
-
substrate specificity, no activity with benzoyl-Arg-2-naphthylamide, and 2-naphthylamides of Glu, Ser, and Tyr, no activity with Phe-Phe-Ala-2-naphthylamide, Leu-Gly-Gly-4-methoxy-2-naphthylamide, and Gly-Pro-Leu-2-naphthylamide, overview
-
-
?
additional information
?
-
-
substrate specificity, no activity with L-Pro-7-amido-4-methylcoumarin and L-Asp-7-amido-4-methylcoumarin, L-Ser-7-amido-4-methylcoumarin is a poor substrate, overview
-
-
?
additional information
?
-
the enzyme is induced by interferon-gamma, the enzyme can trim the N-terminal extended precursor to antigenic peptides in the endoplasmic reticulum
-
?
additional information
?
-
-
the enzyme is induced by interferon-gamma, the enzyme can trim the N-terminal extended precursor to antigenic peptides in the endoplasmic reticulum
-
?
additional information
?
-
-
the enzyme probably is involved in the final stages of peptide and protein precursor processing and maturation mechanisms via the exopeptidase pathway and thereby in some inflammatory processes and tumour development
-
-
?
additional information
?
-
-
the enzyme from testis preferably removes Arg and/or Lys residues from the N-terminus of various peptides, no activity with substrate possessing Pro at the P1 position
-
-
?
additional information
?
-
-
the enzyme is strictly specific for the removal of N-terminal basic residues from peptides and proteins
-
-
?
additional information
?
-
no activity with L-Cys-7-amido-4-methylcoumarin, L-Asp-7-amido-4-methylcoumarin, and L-Glu-7-amido-4-methylcoumarin
-
-
?
additional information
?
-
-
no activity with L-Cys-7-amido-4-methylcoumarin, L-Asp-7-amido-4-methylcoumarin, and L-Glu-7-amido-4-methylcoumarin
-
-
?
additional information
?
-
the aminopeptidase binding site shares a similar structure to LTA4H (EC 3.3.2.6) at its ligand binding sites
-
-
?
additional information
?
-
-
no activity with Ala-Ala, Ala-Lys, Asp-Ala, Gly-Ala and Leu-Ala. The enzyme exclusively hydrolyzes basic amino acids from the amino termini of peptide substrates. The nature of the amino acid residue at the C-terminus of the dipeptide has an effect on hydrolysis rate. The activity is maximal towards dipeptides with Arg, Lys, or Ala as the C-terminal residue
-
?
additional information
?
-
-
the enzyme probably is involved in the final stages of peptide and protein precursor processing and maturation mechanisms via the exopeptidase pathway and thereby in some inflammatory processes and tumour development
-
-
?
additional information
?
-
-
the enzyme from testis preferably removes Arg and/or Lys residues from the N-terminus of various peptides, no activity with substrate possessing Pro at the P1 position
-
-
?
additional information
?
-
-
the enzyme is strictly specific for the removal of N-terminal basic residues from peptides and proteins
-
-
?
additional information
?
-
the enzyme plays a role in peptide or protein precursor processing, the enzyme expression is up-regulated during ontogenesis
-
-
?
additional information
?
-
-
the enzyme probably is involved in the final stages of peptide and protein precursor processing and maturation mechanisms via the exopeptidase pathway and thereby in some inflammatory processes and tumour development, the enzyme from testis preferably removes Arg and/or Lys residues from the N-terminus of various peptides
-
-
?
additional information
?
-
-
the enzyme probably is involved in the final stages of peptide and protein precursor processing and maturation mechanisms via the exopeptidase pathway and thereby in some inflammatory processes and tumour development, the enzyme from testis preferably removes Arg and/or Lys residues from the N-terminus of various peptides
-
-
?
additional information
?
-
the enzyme catalyzes the N-terminal cleavage of basic residues of peptide or protein substrates
-
-
?
additional information
?
-
-
the enzyme from testis preferably removes Arg and/or Lys residues from the N-terminus of various peptides, no activity with bradykinin, neurotensin precursor and substance P, no activity with substrate possessing Pro at the P1 position
-
-
?
additional information
?
-
-
the enzyme is strictly specific for the removal of N-terminal basic residues from peptides and proteins, no activity with bradykinin, no activity with substrate possessing Pro at the P1 position
-
-
?
additional information
?
-
-
no activity with L-Ala-7-amido-4-methylcoumarin, L-Asn-7-amido-4-methylcoumarin, L-Gln-7-amido-4-methylcoumarin, L-Glu-7-amido-4-methylcoumarin, Gly-7-amido-4-methylcoumarin, L-His-7-amido-4-methylcoumarin, L-Ile-7-amido-4-methylcoumarin, L-Leu-7-amido-4-methylcoumarin, L-Asp-7-amido-4-methylcoumarin, L-Thr-7-amido-4-methylcoumarin, L-Met-7-amido-4-methylcoumarin, L-Trp-7-amido-4-methylcoumarin, L-Ser-7-amido-4-methylcoumarin, L-Tyr-7-amido-4-methylcoumarin, and L-Val-7-amido-4-methylcoumarin
-
-
?
additional information
?
-
-
no activity with L-alpha-Asn-2-naphthylamide, L-Glu-2-naphthylamide, L-Ile-2-naphthylamide, L-Phe-2-naphthylamide, L-Pro-2-naphthylamide, L-Ser-2-naphthylamide, L-Thr-2-naphthylamide, L-Trp-2-naphthylamide, L-Val-2-naphthylamide, and L-Arg-L-Arg-2-naphthylamide
-
-
?
additional information
?
-
-
no detectable activity with L-Asp-2-naphthylamide
-
-
?
additional information
?
-
proteolysis is restricted to peptides with an arginine residue in the N terminus, with cleavage detected only when a hydrophobic or an uncharged residue occupies the second site
-
?
additional information
?
-
-
proteolysis is restricted to peptides with an arginine residue in the N terminus, with cleavage detected only when a hydrophobic or an uncharged residue occupies the second site
-
?
additional information
?
-
the enzyme may serve as a critical factor for arginine acquisition during nutrient stress in vivo and also in the proteolysis of host proteins and peptides during SBE pathology
-
?
additional information
?
-
-
the enzyme may serve as a critical factor for arginine acquisition during nutrient stress in vivo and also in the proteolysis of host proteins and peptides during SBE pathology
-
?
additional information
?
-
proteolysis is restricted to peptides with an arginine residue in the N terminus, with cleavage detected only when a hydrophobic or an uncharged residue occupies the second site
-
?
additional information
?
-
-
proteolysis is restricted to peptides with an arginine residue in the N terminus, with cleavage detected only when a hydrophobic or an uncharged residue occupies the second site
-
?
additional information
?
-
the enzyme may serve as a critical factor for arginine acquisition during nutrient stress in vivo and also in the proteolysis of host proteins and peptides during SBE pathology
-
?
additional information
?
-
-
the enzyme may serve as a critical factor for arginine acquisition during nutrient stress in vivo and also in the proteolysis of host proteins and peptides during SBE pathology
-
?
additional information
?
-
-
substrate specificity, the enzyme prefers Arg or Lys in N-terminal position, no activity with dipeptide-4-nitroanilides, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Arg-peptides + H2O
?
-
attribution to inflammatory and wound healing processes
-
-
?
Arg-peptides + H2O
?
-
takes part in later stages of protein degradation in chloroplasts
-
-
?
additional information
?
-
-
the enzyme probably is involved in the final stages of peptide and protein precursor processing and maturation mechanisms via the exopeptidase pathway and thereby in some inflammatory processes and tumour development
-
-
?
additional information
?
-
the enzyme is induced by interferon-gamma, the enzyme can trim the N-terminal extended precursor to antigenic peptides in the endoplasmic reticulum
-
?
additional information
?
-
-
the enzyme is induced by interferon-gamma, the enzyme can trim the N-terminal extended precursor to antigenic peptides in the endoplasmic reticulum
-
?
additional information
?
-
-
the enzyme probably is involved in the final stages of peptide and protein precursor processing and maturation mechanisms via the exopeptidase pathway and thereby in some inflammatory processes and tumour development
-
-
?
additional information
?
-
-
the enzyme probably is involved in the final stages of peptide and protein precursor processing and maturation mechanisms via the exopeptidase pathway and thereby in some inflammatory processes and tumour development
-
-
?
additional information
?
-
the enzyme plays a role in peptide or protein precursor processing, the enzyme expression is up-regulated during ontogenesis
-
-
?
additional information
?
-
-
the enzyme probably is involved in the final stages of peptide and protein precursor processing and maturation mechanisms via the exopeptidase pathway and thereby in some inflammatory processes and tumour development, the enzyme from testis preferably removes Arg and/or Lys residues from the N-terminus of various peptides
-
-
?
additional information
?
-
-
the enzyme probably is involved in the final stages of peptide and protein precursor processing and maturation mechanisms via the exopeptidase pathway and thereby in some inflammatory processes and tumour development, the enzyme from testis preferably removes Arg and/or Lys residues from the N-terminus of various peptides
-
-
?
additional information
?
-
the enzyme may serve as a critical factor for arginine acquisition during nutrient stress in vivo and also in the proteolysis of host proteins and peptides during SBE pathology
-
?
additional information
?
-
-
the enzyme may serve as a critical factor for arginine acquisition during nutrient stress in vivo and also in the proteolysis of host proteins and peptides during SBE pathology
-
?
additional information
?
-
the enzyme may serve as a critical factor for arginine acquisition during nutrient stress in vivo and also in the proteolysis of host proteins and peptides during SBE pathology
-
?
additional information
?
-
-
the enzyme may serve as a critical factor for arginine acquisition during nutrient stress in vivo and also in the proteolysis of host proteins and peptides during SBE pathology
-
?
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
Ca2+
Cd2+
Cl-
Co2+
Cu2+
K+
KCl
Mn2+
Na+
NaCl
Ni2+
Zinc
essential zinc-binding site HEXXH at amino acid residues 370-374 with a second glutamic acid separated by 18 amino acids
Zn2+
additional information
Cl-
-
required for activity
Cl-
-
activates at physiological concentrations around 150 mM, dependent on the target peptide
Co2+
-
activates. Enzyme contains 0.00063 atoms per subunit, wild-type enzyme
Co2+
-
the metal-substituted derivative Co(II)-Ap-B contains almost 1 mol of cobalt(II) ions molecule
Cu2+
-
the metal-substituted derivative Cu(II)-Ap-B contains almost 1 mol of copper(II) ions per molecule
Mn2+
-
activates. Enzyme contains 0.0026 atoms per subunit, wild-type enzyme
Zn2+
-
dependent on, zinc-metallopeptidase, the enzyme contains the binding motif HEXXHX18E
Zn2+
-
dependent on, zinc-metallopeptidase, the enzyme contains the binding motif HEXXHX18E
Zn2+
zinc metalloenzyme, enzyme LTA4H folds into three domains and creates a deep cleft harboring the catalytic Zn2+ site, forming the active site with an L-shaped hydrophobic pocket deep into the protein
Zn2+
-
dependent on, zinc-metallopeptidase, the enzyme contains the binding motif HEXXHX18E
Zn2+
-
dependent on, zinc-metallopeptidase, the enzyme contains the binding motif HEXXHX18E
additional information
-
no evidence for Zn in atomic absorption chromatography
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(S)-2-((2S,3R)-3-amino-2-hydroxy-4-phenylbutanamido)-4-methylpentanoic acid
-
4-(dimethylamino)-N-[7-(hydroxyamino)-7-oxoheptyl]benzamide
enzyme binding structure, overview
kallidin
-
human peptide hormone, 10 microM, Arg 4-methylcoumarin 7-amide hydrolysis: 73.7% (wild-type enzyme)
L-Arg-2-naphthylamide
-
competitive inhibition of hydrolysis of L-Ala-2-naphthylamide, no inhibition vice versa
leuhistin
-
40% inhibition at 0.0003 mM, independent on TGF-beta1 activation
N-alpha-p-tosyl-L-lysine-chloromethyl ketone
-
specific and irreversible inhibitor
N-[(2S,3R)-3-amino-2-hydroxy-5-methylhexanoyl]-L-valyl-L-valyl-L-aspartic acid
-
-
Na+
-
NaCl (0.1-100 mM) has an opposite effect on the EGTA-treated KAP apo-enzyme, it inhibits 13% at 0.1 mM and 100% at 100 mM
o-phenanthroline
-
the native enzyme is inhibited by 76% at 0.5 mM, the recombinant enzyme is inhibited by 80% at 0.5 mM
Substance P
-
human peptide hormone, 100 microM, Arg 4-methylcoumarin 7-amide hydrolysis: 63.8% (wild-type enzyme); human peptide hormone, 10 microM, Arg 4-methylcoumarin 7-amide hydrolysis: 78% (wild-type enzyme)
tert-butyl bestatin
-
i.e. BE17, the BE15 derivative has a dual inhibitory effect of invasion and motility on tumor and endothelial cells
[(2Z)-3-[(7-chloro-4-oxo-1,2,3-benzotriazin-3(4H)-yl)methyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
11.7% inhibition at 0.01 mM
[(2Z)-3-[2-(6-methyl-4-oxo-1,2,3-benzotriazin-3(4H)-yl)ethyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
54.8% inhibition at 0.01 mM
[(2Z)-3-[2-(6-nitro-4-oxo-1,2,3-benzotriazin-3(4H)-yl)ethyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
32.8% inhibition at 0.01 mM
[(2Z)-3-[2-(7-bromo-4-oxo-1,2,3-benzotriazin-3(4H)-yl)ethyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
53.5% inhibition at 0.01 mM
[(2Z)-3-[2-(7-chloro-4-oxo-1,2,3-benzotriazin-3(4H)-yl)ethyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
65.2% inhibition at 0.01 mM
[(2Z)-3-[2-(7-fluoro-4-oxo-1,2,3-benzotriazin-3(4H)-yl)ethyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
36.4% inhibition at 0.01 mM
[(2Z)-3-[4-(6-methyl-4-oxo-1,2,3-benzotriazin-3(4H)-yl)butyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
26.0% inhibition at 0.01 mM
[(2Z)-3-[4-(6-nitro-4-oxo-1,2,3-benzotriazin-3(4H)-yl)butyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
22.2% inhibition at 0.01 mM
[(2Z)-3-[4-(7-bromo-4-oxo-1,2,3-benzotriazin-3(4H)-yl)butyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
26.8% inhibition at 0.01 mM
[(2Z)-3-[4-(7-chloro-4-oxo-1,2,3-benzotriazin-3(4H)-yl)butyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
33.7% inhibition at 0.01 mM
[(2Z)-3-[4-(7-fluoro-4-oxo-1,2,3-benzotriazin-3(4H)-yl)butyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
26.0% inhibition at 0.01 mM
[(2Z)-3-[5-(6-methyl-4-oxo-1,2,3-benzotriazin-3(4H)-yl)pentyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
52.6% inhibition at 0.01 mM
[(2Z)-3-[5-(6-nitro-4-oxo-1,2,3-benzotriazin-3(4H)-yl)pentyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
34.1% inhibition at 0.01 mM
[(2Z)-3-[5-(7-bromo-4-oxo-1,2,3-benzotriazin-3(4H)-yl)pentyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
78.8% inhibition at 0.01 mM
[(2Z)-3-[5-(7-chloro-4-oxo-1,2,3-benzotriazin-3(4H)-yl)pentyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
76.1% inhibition at 0.01 mM
[(2Z)-3-[5-(7-fluoro-4-oxo-1,2,3-benzotriazin-3(4H)-yl)pentyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
54.0% inhibition at 0.01 mM
[(2Z)-3-[6-(5-chloro-4-oxo-1,2,3-benzotriazin-3(4H)-yl)hexyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
37.8% inhibition at 0.01 mM
[(2Z)-3-[6-(6-chloro-4-oxo-1,2,3-benzotriazin-3(4H)-yl)hexyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
68.8% inhibition at 0.01 mM
[(2Z)-3-[6-(6-methyl-4-oxo-1,2,3-benzotriazin-3(4H)-yl)hexyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
62.5% inhibition at 0.01 mM
[(2Z)-3-[6-(6-nitro-4-oxo-1,2,3-benzotriazin-3(4H)-yl)hexyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
36.9% inhibition at 0.01 mM
[(2Z)-3-[6-(7-bromo-4-oxo-1,2,3-benzotriazin-3(4H)-yl)hexyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
70.6% inhibition at 0.01 mM
[(2Z)-3-[6-(7-chloro-4-oxo-1,2,3-benzotriazin-3(4H)-yl)hexyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
80.6% inhibition at 0.01 mM
[(2Z)-3-[6-(7-fluoro-4-oxo-1,2,3-benzotriazin-3(4H)-yl)hexyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
51.7% inhibition at 0.01 mM
[(2Z)-3-[6-(7-methoxy-4-oxo-1,2,3-benzotriazin-3(4H)-yl)hexyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
50.3% inhibition at 0.01 mM
[(2Z)-3-[6-(7-nitro-4-oxo-1,2,3-benzotriazin-3(4H)-yl)hexyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
34.6% inhibition at 0.01 mM
[(2Z)-3-[6-(8-chloro-4-oxo-1,2,3-benzotriazin-3(4H)-yl)hexyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
37.9% inhibition at 0.01 mM
[(2Z)-4-oxo-3-[(4-oxo-1,2,3-benzotriazin-3(4H)-yl)methyl]-1,3-thiazolidin-2-ylidene]cyanamide
over 10.0% inhibition at 0.01 mM
[(2Z)-4-oxo-3-[2-(4-oxo-1,2,3-benzotriazin-3(4H)-yl)ethyl]-1,3-thiazolidin-2-ylidene]cyanamide
30.2% inhibition at 0.01 mM
[(2Z)-4-oxo-3-[2-[4-oxo-6-(trifluoromethyl)-1,2,3-benzotriazin-3(4H)-yl]ethyl]-1,3-thiazolidin-2-ylidene]cyanamide
55.6% inhibition at 0.01 mM
[(2Z)-4-oxo-3-[4-[4-oxo-6-(trifluoromethyl)-1,2,3-benzotriazin-3(4H)-yl]butyl]-1,3-thiazolidin-2-ylidene]cyanamide
41.6% inhibition at 0.01 mM
[(2Z)-4-oxo-3-[5-[4-oxo-6-(trifluoromethyl)-1,2,3-benzotriazin-3(4H)-yl]pentyl]-1,3-thiazolidin-2-ylidene]cyanamide
50.1% inhibition at 0.01 mM
[(2Z)-4-oxo-3-[6-[4-oxo-6-(trifluoromethyl)-1,2,3-benzotriazin-3(4H)-yl]hexyl]-1,3-thiazolidin-2-ylidene]cyanamide
60.1% inhibition at 0.01 mM
[(2Z)-4-oxo-3-[[4-oxo-6-(trifluoromethyl)-1,2,3-benzotriazin-3(4H)-yl]methyl]-1,3-thiazolidin-2-ylidene]cyanamide
15.8% inhibition at 0.01 mM
3,4-dichloroisocoumarin
-
0.1 mM, 12% inhibition. 1.0 mM, 16% inhibition
actinonin
-
40% inhibition at 0.0003 mM, independent on TGF-beta1 activation
amastatin
-
50-70% inhibition at 0.0003 mM, dependent on TGF-beta1 activation
Arphamenine A
-
the native enzyme is completely inhibited at 0.001 mM, the recombinant enzyme is completely inhibited at 0.001 mM
Arphamenine B
-
the native enzyme is completely inhibited at 0.001 mM, the recombinant enzyme is completely inhibited at 0.001 mM
bestatin
orally applicated inhibits the melanoma cell-induced angiogenesis in mice air sacs
bestatin
-
the native enzyme is completely inhibited at 0.05 mM, the recombinant enzyme is completely inhibited at 0.1 mM
EDTA
-
the native enzyme is inhibited by 95% at 10 mM, the recombinant enzyme is inhibited by 71% at 10 mM
N-ethylmaleimide
-
the native enzyme is inhibited by 45% at 1 mM, the recombinant enzyme is inhibited by 71% at 1 mM
Zn2+
-
Zn2+ inhibits AP-B reversibly at micromolar concentrations (0.005-0.05 mM), AP-B with 0.25 Zn2+ becomes susceptible to degradation by trypsin suggesting that Zn2+ alters enzyme conformation, complete inhibition occurs at 0.050-0.080 mM
additional information
-
inhibitory potency of bestatin and derivatives on enzyme activity, umbilical vein endothelial cell vessel formation, and cell invasion and migration, overview
-
additional information
synthesis and evaluation of a series of 1,2,3-benzotriazin-4-one derivatives as inhibitors of leukotriene A4 hydrolase aminopeptidase actvity of the enzyme in vitro, overview. Molecular docking and structure-activity relationship of the inhibitors, IC50 values for cytotoxic effects on THP-1 cells
-
additional information
drug repurposing of histone deacetylase (HDAC) inhibitors that alleviate neutrophilic inflammation in acute lung injury and idiopathic pulmonary fibrosis via inhibiting leukotriene A4 hydrolase and blocking LTB4 biosynthesis, overview. Analysis of potential inhibitors of LTA4H across a panel of 18 HDAC inhibitors, using enzymatic assay, thermofluor assay, and X-ray crystallographic investigation. Detailed mechanisms of down-regulation of proinflammatory cytokines by SAHA or M344 are determined in vivo. Cotreatment of N-(6-(2-aminophenylamino)-6-oxyhexyl)-4-methylbenzamide and (S)-2-((2S,3R)-3-amino-2-hydroxy-4-phenylbutanamido)-4-methylpentanoic acid synergistically represses the migration of neutrophil and LTB4-induced neutrophil migration is not affected by these treatments. Molecular modeling of HDAC inhibitors against LTA4H hydrolase and aminopeptidase
-
additional information
-
no or poor inhibition of L-Arg-2-naphthylamide hydrolysis by puromycin at 1 mM, aprotinin, pepstatin A, E64, chymostatin, imipramine, phosphoramidon, lisinopril, and apstatin
-
additional information
-
insensitive to L-Arg-hydroxamate, L-Lys-hydroxamate, puromycin, and amastatin
-
additional information
-
At 0.2 mM, no significant inhibitory effect is observed with caffeic, chlorogenic, ferulic, salicylic and sinapic acids as well as with resveratrol
-
additional information
-
no inhibition by phosphoramidon, E64, antipaine, and TLCK
-
additional information
-
no inhibition by epibestatin, and by E64, chymostatin, leupeptin, and antipain
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NaCl
the enzyme requires a physiological concentration of NaCl (150 mM) for optimal activity
EDTA
-
0.1 mM, activation to 128% of control. 1.0 mM, activation to 146% of control
Zn2+
-
low levels of Zn2+ at 0.00025-0.002 mM result in some activation of AP-B activity up to 25-40% above controls (without Zn2+)
additional information
-
the enzyme is up-regulated during long-term activation of normal and lymphoma T-cells
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000183
L-Arg-2-naphthylamide
-
metal-substituted enzyme form Co(II)-Ap-B, at pH 7.4 and 25°C
0.0529
L-Arg-7-amido-4-methylcoumarin
wild type enzyme, at pH 7.4 and 37°C
0.208
L-Arg-7-amido-4-methylcoumarin
mutant enzyme F297Y, at pH 7.4 and 37°C
0.323
L-Lys-7-amido-4-methylcoumarin
wild type enzyme, at pH 7.4 and 37°C
0.598
L-Lys-7-amido-4-methylcoumarin
mutant enzyme F297Y, at pH 7.4 and 37°C
additional information
additional information
-
dependency on pH and temperature
-
additional information
additional information
-
dependency on chloride concentration
-
additional information
additional information
-
dependency on chloride concentration
-
additional information
additional information
-
comparison of values for various peptide substrates and enzyme sources
-
additional information
additional information
-
comparison of values for various peptide substrates and enzyme sources
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
69.47
L-Arg-2-naphthylamide
-
metal-substituted enzyme form Co(II)-Ap-B, at pH 7.4 and 25°C
2.95
L-Arg-7-amido-4-methylcoumarin
mutant enzyme F297Y, at pH 7.4 and 37°C
9.64
L-Arg-7-amido-4-methylcoumarin
wild type enzyme, at pH 7.4 and 37°C
1.56
L-Lys-7-amido-4-methylcoumarin
mutant enzyme F297Y, at pH 7.4 and 37°C
12.9
L-Lys-7-amido-4-methylcoumarin
wild type enzyme, at pH 7.4 and 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
14.2
L-Arg-7-amido-4-methylcoumarin
mutant enzyme F297Y, at pH 7.4 and 37°C
2.61
L-Lys-7-amido-4-methylcoumarin
mutant enzyme F297Y, at pH 7.4 and 37°C
39.9
L-Lys-7-amido-4-methylcoumarin
wild type enzyme, at pH 7.4 and 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0125
arphamemine B
-
at 37°C in Bicine buffer complemented with 0.2 M NaCl
0.024
Leucine hydroxamate
-
at 37°C in Bicine buffer complemented with 0.2 M NaCl
0.00054
leucinthiol
-
at 37°C in Bicine buffer complemented with 0.2 M NaCl
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0003
4-(dimethylamino)-N-[7-(hydroxyamino)-7-oxoheptyl]benzamide
Homo sapiens
pH and temperature not specified in the publication
0.01
abexinostat
Homo sapiens
above, pH and temperature not specified in the publication
0.01
belinostat
Homo sapiens
above, pH and temperature not specified in the publication
0.01
entinostat
Homo sapiens
above, pH and temperature not specified in the publication
0.01
givinostat
Homo sapiens
above, pH and temperature not specified in the publication
0.01
JNJ-26481585
Homo sapiens
above, pH and temperature not specified in the publication
0.01
mocetinostat
Homo sapiens
above, pH and temperature not specified in the publication
0.01
N-(6-(2-aminophenylamino)-6-oxyhexyl)-4-methylbenzamide
Homo sapiens
above, pH and temperature not specified in the publication
0.01
panobinostat
Homo sapiens
above, pH and temperature not specified in the publication
0.01
pracinostat
Homo sapiens
above, pH and temperature not specified in the publication
0.01
resminostat
Homo sapiens
above, pH and temperature not specified in the publication
0.01
rocilinostat
Homo sapiens
above, pH and temperature not specified in the publication
0.00167
suberanilohydroxamic acid
Homo sapiens
pH and temperature not specified in the publication
-
0.01
trichostatin A
Homo sapiens
above, pH and temperature not specified in the publication
0.01
Valproate
Homo sapiens
above, pH and temperature not specified in the publication
7.77
[(2Z)-3-[2-(6-methyl-4-oxo-1,2,3-benzotriazin-3(4H)-yl)ethyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
Homo sapiens
pH 7.5, 22°C
7.9
[(2Z)-3-[2-(7-bromo-4-oxo-1,2,3-benzotriazin-3(4H)-yl)ethyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
Homo sapiens
pH 7.5, 22°C
7.39
[(2Z)-3-[2-(7-chloro-4-oxo-1,2,3-benzotriazin-3(4H)-yl)ethyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
Homo sapiens
pH 7.5, 22°C
12.09
[(2Z)-3-[5-(6-methyl-4-oxo-1,2,3-benzotriazin-3(4H)-yl)pentyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
Homo sapiens
pH 7.5, 22°C
1.71
[(2Z)-3-[5-(7-bromo-4-oxo-1,2,3-benzotriazin-3(4H)-yl)pentyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
Homo sapiens
pH 7.5, 22°C
2.17
[(2Z)-3-[5-(7-chloro-4-oxo-1,2,3-benzotriazin-3(4H)-yl)pentyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
Homo sapiens
pH 7.5, 22°C
7.9
[(2Z)-3-[5-(7-fluoro-4-oxo-1,2,3-benzotriazin-3(4H)-yl)pentyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
Homo sapiens
pH 7.5, 22°C
3.87
[(2Z)-3-[6-(6-chloro-4-oxo-1,2,3-benzotriazin-3(4H)-yl)hexyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
Homo sapiens
pH 7.5, 22°C
7.19
[(2Z)-3-[6-(6-methyl-4-oxo-1,2,3-benzotriazin-3(4H)-yl)hexyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
Homo sapiens
pH 7.5, 22°C
6.82
[(2Z)-3-[6-(7-bromo-4-oxo-1,2,3-benzotriazin-3(4H)-yl)hexyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
Homo sapiens
pH 7.5, 22°C
1.3
[(2Z)-3-[6-(7-chloro-4-oxo-1,2,3-benzotriazin-3(4H)-yl)hexyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
Homo sapiens
pH 7.5, 22°C
12.27
[(2Z)-3-[6-(7-fluoro-4-oxo-1,2,3-benzotriazin-3(4H)-yl)hexyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
Homo sapiens
pH 7.5, 22°C
13.53
[(2Z)-3-[6-(7-methoxy-4-oxo-1,2,3-benzotriazin-3(4H)-yl)hexyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
Homo sapiens
pH 7.5, 22°C
10.11
[(2Z)-4-oxo-3-[2-[4-oxo-6-(trifluoromethyl)-1,2,3-benzotriazin-3(4H)-yl]ethyl]-1,3-thiazolidin-2-ylidene]cyanamide
Homo sapiens
pH 7.5, 22°C
14.89
[(2Z)-4-oxo-3-[5-[4-oxo-6-(trifluoromethyl)-1,2,3-benzotriazin-3(4H)-yl]pentyl]-1,3-thiazolidin-2-ylidene]cyanamide
Homo sapiens
pH 7.5, 22°C
7.7
[(2Z)-4-oxo-3-[6-[4-oxo-6-(trifluoromethyl)-1,2,3-benzotriazin-3(4H)-yl]hexyl]-1,3-thiazolidin-2-ylidene]cyanamide
Homo sapiens
pH 7.5, 22°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0016
-
normal healthy rats and rats treated/deprived with salt and water, soluble fraction of adrenal gland
0.0018
-
normal healthy rats and rats treated/deprived with salt and water, soluble fraction of lung
0.002
-
normal healthy rats and rats treated/deprived with salt and water, soluble fraction of heart
0.0024
-
normal healthy rats and rats treated/deprived with salt and water, soluble fraction of kidney cortex
0.0042
-
normal healthy rats and rats treated/deprived with salt and water, soluble fraction of kidney medulla
0.1
12.5
140
26
9.9
additional information
0.1
-
metal-substituted enzyme form Cu(II)-Ap-B, using L-Arg-2-naphthylamide as a substrate, at pH 7.4 and 25°C
12.5
-
recombinant Ap-B, using L-Arg-2-naphthylamide as a substrate, at pH 7.4 and 25°C
26
-
purified enzyme, substrate N-succinyl-Gly-Pro-Leu-Gly-Pro 7-amido-4-methylcoumarin
9.9
-
metal-substituted enzyme form Co(II)-Ap-B, using L-Arg-2-naphthylamide as a substrate, at pH 7.4 and 25°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE