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Information on EC 3.4.11.6 - aminopeptidase B
for references in articles please use BRENDA:EC3.4.11.6
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EC Tree 3 Hydrolases
3.4 Acting on peptide bonds (peptidases)
3.4.11 Aminopeptidases
3.4.11.6 aminopeptidase B
IUBMB Comments
Cytosolic or membrane-associated enzyme from mammalian tissues, activated by chloride ions and low concentrations of thiol compounds. This is one of the activities of the bifunctional enzyme EC 3.3.2.6 (membrane alanyl aminopeptidase family) [4,5].
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
- 3.4.11.6
- brevis
-
pollicis
-
abductor
-
transcranial
- retina
- 2-amino-4-phosphonobutyrate
-
minimi
-
digiti
-
latency
- bestatin
-
thumb
-
corticospinal
- erg
-
interosseous
-
cmaps
-
intracortical
-
voluntary
-
wrist
-
thenar
- tibialis
-
ulnar
-
electroretinogram
-
motor-evoked
-
flexor
-
radialis
-
interstimulus
-
off-center
-
f-waves
-
antiphase
-
amacrine
-
dark-adapted
-
biceps
-
paired-pulse
- beta-naphthylamide
-
alt-associated
-
carpi
-
brachii
-
anoxygenic
-
electromyographic
- quisqualate
-
photopic
- amastatin
-
short-latency
- drug development
-
3.4.11.1
-
interhemispheric
- alpha-fucosidase
-
hallucis
-
light-evoked
-
puromycin-sensitive
-
imagery
Reaction Schemes
showrelease of N-terminal Arg and Lys from oligopeptides when P1' is not Pro. Also acts on arylamides of Arg and Lys
Synonyms
apb, arylamidase, aminopeptidase b, arginine aminopeptidase, cytosol aminopeptidase, arginyl aminopeptidase, aminopeptidase-b, l-rap, dap bii, arginine-aminopeptidase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AAP
ACE2
aminopeptidase B
aminopeptidase BSAP
aminopeptidase, arginine
-
-
-
-
Ap-B
APB
APB-AN
Arg/Lys aminopeptidase
arginine aminopeptidase
arginyl aminopeptidase
arylamidase II
-
-
-
-
Cl--activated arginine aminopeptidase
-
-
-
-
cytosol aminopeptidase
-
-
-
-
DAP BII
dipeptidyl aminopeptidase BII
EC 3.4.13.6
-
-
formerly
-
L-arginine aminopeptidase
-
-
-
-
leukocyte-derived arginine aminopeptidase
RAP
RNPEP
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 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
-
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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
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Ala-2-naphthylamide + H2O
Ala + 2-naphthylamine
-
Substrates: -
Products: -
Products: -
?
alpha-Glu-4-nitroanilide + H2O
Glu + 4-nitroaniline
-
Substrates: 564% of the activity with Leu-4-nitroanilide
Products: -
Products: -
?
Arg 4-methylcoumarin 7-amide + H2O
Arg + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
Arg-4-methylcoumaryl-7-amide + H2O
Arg + 7-amino-4-methylcoumarin
Substrates: -
Products: -
Products: -
?
Arg-Ala + H2O
Arg + Ala
-
Substrates: 82% of the activity with Arg-Arg
Products: -
Products: -
?
Arg-alpha-atrial natriuretic factor1-20 + H2O
Arg + alpha-atrial natriuretic factor1-20
-
Substrates: -
Products: -
Products: -
?
Arg-Asp + H2O
Arg + Asp
-
Substrates: 25% of the activity with Arg-Arg
Products: -
Products: -
?
Arg-beta-atrial natriuretic factor1-20 + H2O
Arg + beta-atrial natriuretic factor1-20
-
Substrates: -
Products: -
Products: -
?
Arg-beta-naphthylamide + H2O
L-arginine + 2-naphthylamine
-
Substrates: substrate used in the activity assay
Products: -
Products: -
?
Arg-Gly-Asp-Ser-Pro-Ala-Ser-Ser-Lys-Pro + H2O
Arg + Gly-Asp-Ser-Pro-Ala-Ser-Ser-Lys-Pro
Substrates: i.e. fibronectin-binding inhibitor
Products: -
Products: -
?
Arg-Gly-Glu-Ser + H2O
Arg + Gly-Glu-Ser
Substrates: i.e. platelet aggregation inhibitor
Products: -
Products: -
?
Arg-Gly-Pro-Phe-Pro-Ile + H2O
Arg + Gly-Pro-Phe-Pro-Ile
Substrates: i.e. sexual agglutination peptide
Products: -
Products: -
?
Arg-Gly-Tyr-Ala-Leu-Gly + H2O
Arg + Gly-Tyr-Ala-Leu-Gly
-
Substrates: -
Products: -
Products: -
?
Arg-Ile + H2O
Arg + Ile
-
Substrates: 32% of the activity with Arg-Arg
Products: -
Products: -
?
Arg-Leu + H2O
Arg + Leu
-
Substrates: 25% of the activity with Arg-Arg
Products: -
Products: -
?
Arg-Leu-enkephalin + H2O
Arg + Leu-enkephalin
-
Substrates: -
Products: -
Products: -
?
Arg-Lys + H2O
Arg + Lys
-
Substrates: 88% of the activity with Arg-Arg
Products: -
Products: -
?
Arg-Lys-somatostatin-14 + 2 H2O
Arg + Lys + somatostatin-14
-
Substrates: sequential removal of basic N-terminal residues
Products: -
Products: -
?
Arg-Lys-somatostatin-14 + H2O
Arg-Lys + somatostatin-14
-
Substrates: -
Products: -
Products: -
?
Arg-Met-enkephalin + H2O
Arg + Met-enkephalin
-
Substrates: -
Products: -
Products: -
?
Arg-neurokinin A + H2O
Arg + neurokinin A
-
Substrates: -
Products: -
Products: -
?
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
Substrates: i.e. protein kinase C substrate
Products: -
Products: -
?
Arg-Pro-Lys-Pro-Gln-Gly-Leu-Met + H2O
Arg + Pro-Lys-Pro-Gln-Gly-Leu-Met
Substrates: i.e. substance P
Products: -
Products: -
?
Arg-Tyr-Leu-Pro-Thr + H2O
Arg + Tyr-Leu-Pro-Thr
-
Substrates: proctolin
Products: -
Products: -
?
Arg-Val-Tyr-Ile-His-Pro-Ile + H2O
Arg + Val-Tyr-Ile-His-Pro-Ile
Substrates: i.e. angiotensin III
Products: -
Products: -
?
Arg-Val-Tyr-Ile-His-Pro-Phe + H2O
Arg + Val-Tyr-Ile-His-Pro-Phe
-
Substrates: angiotensin III
Products: -
Products: -
?
azocasein + H2O
protein fragments of azocasein of MW 71 kDa, 83 kDa, and 22 kDa
-
Substrates: -
Products: -
Products: -
?
benzoyl-Arg-p-nitroanilide + H2O
benzoyl-Arg + p-nitroaniline
-
Substrates: -
Products: -
Products: -
?
Cys-Gly + H2O
Cys + Gly
-
Substrates: 4210% of the activity with Leu-4-nitroanilide
Products: -
Products: -
?
Glu-4-nitroanilide + H2O
Glu + 4-nitroaniline
-
Substrates: 4.3% of the activity as compared to Arg-4-nitroanilide
Products: -
Products: -
?
Gly-4-nitroanilide + H2O
Gly + 4-nitroaniline
-
Substrates: 1.3% of the activity with Leu-4-nitroanilide
Products: -
Products: -
?
Gly-L-Pro-2-naphthylamide + H2O
Gly-L-Pro + 2-naphthylamine
-
Substrates: 1% activity compared to L-Lys-2-naphthylamide
Products: -
Products: -
?
His-4-nitroanilide + H2O
His + 4-nitroaniline
-
Substrates: 11.2% of the activity as compared to Arg-4-nitroanilide
Products: -
Products: -
?
L-Ala-Ala-Pro-Leu-4-nitroanilide + H2O
L-Ala-Ala-Pro-Leu + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
L-Arg 7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
-
Substrates: fluorogenic substrate, best substrate
Products: -
Products: -
?
L-Arg-L-Tyr-Gly-Gly-L-Phe-L-Leu + H2O
L-Arg + L-Tyr-Gly-Gly-L-Phe-L-Leu
-
Substrates: -
Products: -
Products: -
?
L-Arg-peptide + H2O
L-Arg + peptide
-
Substrates: specific for N-terminal Arg or Lys residues, di-, tri-, and polypeptides
Products: -
Products: -
?
L-arginine-2-naphthylamide + H2O
2-naphthylamine + L-Arg
-
Substrates: assay at 37°C
Products: -
Products: -
?
L-Asn-7-amido-4-methylcoumarin + H2O
L-Asn + 7-amino-4-methylcoumarin
Substrates: 53% activity compared to L-Arg-7-amido-4-methylcoumarin
Products: -
Products: -
?
L-Asp-7-amido-4-methylcoumarin + H2O
L-Asp + 7-amino-4-methylcoumarin
Substrates: 15% activity compared to L-Arg-7-amido-4-methylcoumarin
Products: -
Products: -
?
L-beta-Asn-2-naphthylamide + H2O
L-beta-Asn + 2-naphthylamine
-
Substrates: 9% activity compared to L-Lys-2-naphthylamide
Products: -
Products: -
?
L-Cys-2-naphthylamide + H2O
L-Cys + 2-naphthylamine
-
Substrates: 1% activity compared to L-Lys-2-naphthylamide
Products: -
Products: -
?
L-Cys-7-amido-4-methylcoumarin + H2O
L-Cys + 7-amino-4-methylcoumarin
-
Substrates: 5% activity compared to L-Arg-7-amido-4-methylcoumarin
Products: -
Products: -
?
L-Gln-7-amido-4-methylcoumarin + H2O
L-Gln + 7-amino-4-methylcoumarin
Substrates: about 1% activity compared to L-Arg-7-amido-4-methylcoumarin
Products: -
Products: -
?
L-Gly-L-Arg-2-naphthylamide + H2O
L-Gly-L-Arg + 2-naphthylamine
-
Substrates: 250% activity compared to L-Lys-2-naphthylamide
Products: -
Products: -
?
L-His-2-naphthylamide + H2O
L-His + 2-naphthylamine
-
Substrates: 15% activity compared to L-Lys-2-naphthylamide
Products: -
Products: -
?
L-Ile-7-amido-4-methylcoumarin + H2O
L-Ile + 7-amino-4-methylcoumarin
Substrates: about 1% activity compared to L-Arg-7-amido-4-methylcoumarin
Products: -
Products: -
?
L-Leu 7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
-
Substrates: fluorogenic substrate
Products: -
Products: -
?
L-Lys-L-Ala-2-naphthylamide + H2O
L-Lys-L-Ala + 2-naphthylamine
-
Substrates: 7% activity compared to L-Lys-2-naphthylamide
Products: -
Products: -
?
L-Lys-peptide + H2O
L-Lys + peptide
-
Substrates: specific for N-terminal Arg or Lys residues, di-, tri-, and polypeptide
Products: -
Products: -
?
L-lysine-2-naphthylamide + H2O
2-naphthylamine + L-Lys
-
Substrates: assay at 37°C
Products: -
Products: -
?
L-Phe-2-naphthylamide + H2O
L-Phe + 2-naphthylamine
-
Substrates: 0.171% activity compared to L-Arg-2-naphthylamide
Products: -
Products: -
?
L-Pro-7-amido-4-methylcoumarin + H2O
L-Pro + 7-amino-4-methylcoumarin
-
Substrates: 7% activity compared to L-Arg-7-amido-4-methylcoumarin
Products: -
Products: -
?
L-Ser-7-amido-4-methylcoumarin + H2O
L-Ser + 7-amino-4-methylcoumarin
Substrates: 15% activity compared to L-Arg-7-amido-4-methylcoumarin
Products: -
Products: -
?
L-Tyr 7-amido-4-methylcoumarin + H2O
L-Tyr + 7-amino-4-methylcoumarin
-
Substrates: fluorogenic substrate
Products: -
Products: -
?
L-Tyr-7-amido-4-methylcoumarin + H2O
L-Tyr + 7-amino-4-methylcoumarin
Substrates: about 7% activity compared to L-Arg-7-amido-4-methylcoumarin
Products: -
Products: -
?
L-Val-2-naphthylamide + H2O
L-Val + 2-naphthylamine
-
Substrates: 0.034% activity compared to L-Arg-2-naphthylamide
Products: -
Products: -
?
L-Val-4-nitroanilide + H2O
L-Val + 4-nitroaniline
Substrates: low activity
Products: -
Products: -
?
L-Val-7-amido-4-methylcoumarin + H2O
L-Val + 7-amino-4-methylcoumarin
Substrates: about 1% activity compared to L-Arg-7-amido-4-methylcoumarin
Products: -
Products: -
?
Leu-2-naphthylamide + H2O
Leu + 2-naphthylamine
-
Substrates: -
Products: -
Products: -
?
Leu-Gly + H2O
Leu + Gly
-
Substrates: 1200% of the activity with Leu-4-nitroanilide
Products: -
Products: -
?
leukotriene A4 + H2O
L-Arg + leukotriene B4
-
Substrates: weak in vitro activity
Products: -
Products: -
?
leukotriene A4 + H2O
leukotriene B4 + ?
-
Substrates: has a residual catalytic ability to hydrolyze leukotriene A4
Products: -
Products: -
?
Lys 4-methylcoumarin 7-amide + H2O
Lys + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
Lys-4-methylcoumarin 7-amide + H2O
Lys + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
Lys-7-amido-4-methylcoumarin + H2O
Lys + 7-amino-4-methylcoumarin
-
Substrates: 4.3% of the activity with Arg-7-amido-4-methylcoumarin
Products: -
Products: -
?
Lys-Ala + H2O
Lys + Ala
-
Substrates: 88% of the activity with Arg-Arg
Products: -
Products: -
?
Lys-Leu-2-naphthylamide + H2O
Lys + Leu-2-naphthylamide
-
Substrates: -
Products: -
Products: -
?
Lys-Lys + H2O
Lys + Lys
-
Substrates: 30% of the activity with Arg-Arg
Products: -
Products: -
?
N-p-tosyl-Gly-Pro-Lys-p-nitroanilide + H2O
N-p-tosyl-Gly-Pro-Lys + p-nitroaniline
-
Substrates: -
Products: -
Products: -
?
N-succinyl-Gly-Pro-Leu-Gly-Pro 7-amido-4-methylcoumarin + H2O
N-succinyl-Gly-Pro-Leu-Gly-Pro + 7-amino-4-methylcoumarin
-
Substrates: fluorogenic substrate
Products: -
Products: -
?
[Arg0]-Met-enkephalin + H2O
Met-enkephalin + de-[Tyr]-Met-enkephalin
Substrates: i.e. RYGGFM
Products: -
Products: -
?
Ala-4-nitroanilide + H2O
Ala + 4-nitroaniline
-
Substrates: 9.7% of the activity as compared to Arg-4-nitroanilide
Products: -
Products: -
?
Ala-4-nitroanilide + H2O
Ala + 4-nitroaniline
-
Substrates: 4.6% of the activity with Leu-4-nitroanilide
Products: -
Products: -
?
Ala-Ala 4-nitroanilide + H2O
Ala-Ala + 4-nitroaniline
Substrates: -
Products: -
Products: -
?
Ala-Ala 4-nitroanilide + H2O
Ala-Ala + 4-nitroaniline
Substrates: -
Products: -
Products: -
?
angiotensin III + H2O
angiotensin IV + ?
Substrates: the Y409F/Y414F double mutant enzyme shows higher activity and broader substrate specificity than the wild-type enzyme toward angiotensin III and the tested analogs
Products: -
Products: -
?
Arg-4-methoxy-2-naphthylamide
Arg + 4-methoxy-2-naphthylamine
-
Substrates: most preferred substrate
Products: -
Products: -
?
Arg-4-methoxy-2-naphthylamide
Arg + 4-methoxy-2-naphthylamine
Pediococcus acidilactici NCDC 252
-
Substrates: most preferred substrate
Products: -
Products: -
?
Arg-4-methylcoumarin 7-amide + H2O
Arg + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
Arg-4-methylcoumarin 7-amide + H2O
Arg + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
Arg-4-nitroanilide + H2O
Arg + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
Arg-4-nitroanilide + H2O
Arg + 4-nitroaniline
Aspergillus niger CGMCC 3.1454
-
Substrates: -
Products: -
Products: -
?
Arg-4-nitroanilide + H2O
Arg + 4-nitroaniline
-
Substrates: 2.5% of the activity with Leu-4-nitroanilide
Products: -
Products: -
?
Arg-4-nitroanilide + H2O
Arg + 4-nitroaniline
-
Substrates: as active as Arg-7-amido-4-methylcoumarin
Products: -
Products: -
?
Arg-4-nitroanilide + H2O
Arg + 4-nitroaniline
Substrates: -
Products: -
Products: -
?
Arg-4-nitroanilide + H2O
Arg + 4-nitroaniline
Substrates: -
Products: -
Products: -
?
Arg-7-amido-4-methylcoumarin + H2O
Arg + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
Arg-7-amido-4-methylcoumarin + H2O
Arg + 7-amino-4-methylcoumarin
Substrates: -
Products: -
Products: -
?
Arg-7-amido-4-methylcoumarin + H2O
Arg + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
Arg-Arg-4-methoxy-2-naphthylamide
? + 4-methoxy-2-naphthylamine
-
Substrates: 11% of the activity with Arg-4-methoxy-2-naphthylamide
Products: -
Products: -
?
Arg-Arg-4-methoxy-2-naphthylamide
? + 4-methoxy-2-naphthylamine
Pediococcus acidilactici NCDC 252
-
Substrates: 11% of the activity with Arg-4-methoxy-2-naphthylamide
Products: -
Products: -
?
Arg-peptides + H2O
?
-
Substrates: or Lys-peptides, metabolism of kinin
Products: -
Products: -
?
Arg-peptides + H2O
?
-
Substrates: attribution to inflammatory and wound healing processes
Products: -
Products: -
?
Arg-peptides + H2O
?
-
Substrates: takes part in later stages of protein degradation in chloroplasts
Products: -
Products: -
?
Arg-Phe + H2O
Arg + Phe
-
Substrates: 35% of the activity with Arg-Arg
Products: -
Products: -
?
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg + Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
Substrates: i.e. bradykinin
Products: -
Products: -
?
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg + Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
Substrates: i.e. bradykinin
Products: -
Products: -
?
Gly-2-naphthylamide + H2O
Gly + 2-naphthylamine
-
Substrates: less than 0.02% activity compared to L-Arg-2-naphthylamide
Products: -
Products: -
?
Gly-2-naphthylamide + H2O
Gly + 2-naphthylamine
-
Substrates: 1% activity compared to L-Lys-2-naphthylamide
Products: -
Products: -
?
Gly-Phe 4-nitroanilide + H2O
Gly-Phe + 4-nitroaniline
Substrates: -
Products: -
Products: -
?
Gly-Phe 4-nitroanilide + H2O
Gly-Phe + 4-nitroaniline
Substrates: -
Products: -
Products: -
?
L-Ala-2-naphthylamide + H2O
L-Ala + 2-naphthylamine
-
Substrates: -
Products: -
Products: -
?
L-Ala-2-naphthylamide + H2O
L-Ala + 2-naphthylamine
-
Substrates: -
Products: -
Products: -
?
L-Ala-2-naphthylamide + H2O
L-Ala + 2-naphthylamine
-
Substrates: 0.1% activity compared to L-Arg-2-naphthylamide
Products: -
Products: -
?
L-Ala-2-naphthylamide + H2O
L-Ala + 2-naphthylamine
-
Substrates: 83% activity compared to L-Lys-2-naphthylamide
Products: -
Products: -
?
L-Ala-4-nitroanilide + H2O
L-Ala + 4-nitroaniline
Substrates: low activity
Products: -
Products: -
?
L-Ala-4-nitroanilide + H2O
L-Ala + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
L-Ala-4-nitroanilide + H2O
L-Ala + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
L-Ala-7-amido-4-methylcoumarin + H2O
L-Ala + 7-amino-4-methylcoumarin
-
Substrates: best substrate
Products: -
Products: -
?
L-Ala-7-amido-4-methylcoumarin + H2O
L-Ala + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
L-Ala-7-amido-4-methylcoumarin + H2O
L-Ala + 7-amino-4-methylcoumarin
Substrates: about 2% activity compared to L-Arg-7-amido-4-methylcoumarin
Products: -
Products: -
?
L-Ala-7-amido-4-methylcoumarin + H2O
L-Ala + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
L-Arg-(Met)enkephalin + H2O
L-Arg + (Met)enkephalin
Substrates: -
Products: -
Products: -
?
L-Arg-(Met)enkephalin + H2O
L-Arg + (Met)enkephalin
-
Substrates: -
Products: -
Products: -
?
L-Arg-2-naphthylamide + H2O
L-Arg + 2-naphthylamine
-
Substrates: -
Products: -
Products: -
?
L-Arg-2-naphthylamide + H2O
L-Arg + 2-naphthylamine
-
Substrates: -
Products: -
Products: -
?
L-Arg-2-naphthylamide + H2O
L-Arg + 2-naphthylamine
-
Substrates: -
Products: -
Products: -
?
L-Arg-2-naphthylamide + H2O
L-Arg + 2-naphthylamine
-
Substrates: -
Products: -
Products: -
?
L-Arg-2-naphthylamide + H2O
L-Arg + 2-naphthylamine
-
Substrates: -
Products: -
Products: -
?
L-Arg-2-naphthylamide + H2O
L-Arg + 2-naphthylamine
Substrates: -
Products: -
Products: -
?
L-Arg-2-naphthylamide + H2O
L-Arg + 2-naphthylamine
-
Substrates: -
Products: -
Products: -
?
L-Arg-2-naphthylamide + H2O
L-Arg + 2-naphthylamine
-
Substrates: 100% activity
Products: -
Products: -
?
L-Arg-2-naphthylamide + H2O
L-Arg + 2-naphthylamine
-
Substrates: -
Products: -
Products: -
?
L-Arg-2-naphthylamide + H2O
L-Arg + 2-naphthylamine
-
Substrates: 17% activity compared to L-Lys-2-naphthylamide
Products: -
Products: -
?
L-Arg-2-naphthylamide + H2O
L-Arg + 2-naphthylamine
-
Substrates: -
Products: -
Products: -
?
L-Arg-2-naphthylamide + H2O
L-Arg + 2-naphthylamine
-
Substrates: -
Products: -
Products: -
?
L-Arg-2-naphthylamide + H2O
L-Arg + 2-naphthylamine
-
Substrates: -
Products: -
Products: -
?
L-Arg-4-nitroanilide + H2O
L-Arg + 4-nitroaniline
Substrates: best substrate
Products: -
Products: -
?
L-Arg-4-nitroanilide + H2O
L-Arg + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
L-Arg-4-nitroanilide + H2O
L-Arg + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
Substrates: 100% activity
Products: -
Products: -
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
-
Substrates: high activity
Products: -
Products: -
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
Substrates: 100% activity
Products: -
Products: -
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
-
Substrates: 100% activity
Products: -
Products: -
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
-
Substrates: best substrate
Products: -
Products: -
?
L-Leu-2-naphthylamide + H2O
L-Leu + 2-naphthylamine
-
Substrates: -
Products: -
Products: -
?
L-Leu-2-naphthylamide + H2O
L-Leu + 2-naphthylamine
-
Substrates: 31% activity compared to L-Lys-2-naphthylamide
Products: -
Products: -
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
Substrates: -
Products: -
Products: -
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
L-Leu-7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
Substrates: 28% activity compared to L-Arg-7-amido-4-methylcoumarin
Products: -
Products: -
?
L-Leu-7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
L-Leu-7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
Substrates: about 1% activity compared to L-Arg-7-amido-4-methylcoumarin
Products: -
Products: -
?
L-Leu-7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
L-Lys-(Met)enkephalin + H2O
L-Lys + (Met)enkephalin
Substrates: -
Products: -
Products: -
?
L-Lys-(Met)enkephalin + H2O
L-Lys + (Met)enkephalin
-
Substrates: -
Products: -
Products: -
?
L-Lys-2-naphthylamide + H2O
L-Lys + 2-naphthylamine
-
Substrates: -
Products: -
Products: -
?
L-Lys-2-naphthylamide + H2O
L-Lys + 2-naphthylamine
-
Substrates: -
Products: -
Products: -
?
L-Lys-2-naphthylamide + H2O
L-Lys + 2-naphthylamine
-
Substrates: 41% activity compared to L-Arg-2-naphthylamide
Products: -
Products: -
?
L-Lys-2-naphthylamide + H2O
L-Lys + 2-naphthylamine
-
Substrates: -
Products: -
Products: -
?
L-Lys-2-naphthylamide + H2O
L-Lys + 2-naphthylamine
-
Substrates: 100% activity
Products: -
Products: -
?
L-Lys-4-nitroanilide + H2O
L-Lys + 4-nitroaniline
Substrates: -
Products: -
Products: -
?
L-Lys-4-nitroanilide + H2O
L-Lys + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
L-Lys-4-nitroanilide + H2O
L-Lys + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
L-Lys-7-amido-4-methylcoumarin + H2O
L-Lys + 7-amino-4-methylcoumarin
Substrates: 10% activity compared to L-Arg-7-amido-4-methylcoumarin
Products: -
Products: -
?
L-Lys-7-amido-4-methylcoumarin + H2O
L-Lys + 7-amino-4-methylcoumarin
Substrates: about 45% activity compared to L-Arg-7-amido-4-methylcoumarin
Products: -
Products: -
?
L-Lys-7-amido-4-methylcoumarin + H2O
L-Lys + 7-amino-4-methylcoumarin
-
Substrates: 17% activity compared to L-Arg-7-amido-4-methylcoumarin
Products: -
Products: -
?
L-Met-2-naphthylamide + H2O
L-Met + 2-naphthylamine
-
Substrates: -
Products: -
Products: -
?
L-Met-2-naphthylamide + H2O
L-Met + 2-naphthylamine
-
Substrates: 2% activity compared to L-Lys-2-naphthylamide
Products: -
Products: -
?
L-Met-7-amido-4-methylcoumarin + H2O
L-Met + 7-amino-4-methylcoumarin
Substrates: 19% activity compared to L-Arg-7-amido-4-methylcoumarin
Products: -
Products: -
?
L-Met-7-amido-4-methylcoumarin + H2O
L-Met + 7-amino-4-methylcoumarin
Substrates: about 1% activity compared to L-Arg-7-amido-4-methylcoumarin
Products: -
Products: -
?
L-Met-7-amido-4-methylcoumarin + H2O
L-Met + 7-amino-4-methylcoumarin
-
Substrates: no activity with Z-Met-7-amido-4-methylcoumarin
Products: -
Products: -
?
L-Phe-7-amido-4-methylcoumarin + H2O
L-Phe + 7-amino-4-methylcoumarin
Substrates: about 5% activity compared to L-Arg-7-amido-4-methylcoumarin
Products: -
Products: -
?
L-Phe-7-amido-4-methylcoumarin + H2O
L-Phe + 7-amino-4-methylcoumarin
-
Substrates: 2% activity compared to L-Arg-7-amido-4-methylcoumarin
Products: -
Products: -
?
L-Phe-7-amido-4-methylcoumarin + H2O
L-Phe + 7-amino-4-methylcoumarin
-
Substrates: low activity
Products: -
Products: -
?
L-Tyr-2-naphthylamide + H2O
L-Tyr + 2-naphthylamine
-
Substrates: 0.171% activity compared to L-Arg-2-naphthylamide
Products: -
Products: -
?
L-Tyr-2-naphthylamide + H2O
L-Tyr + 2-naphthylamine
-
Substrates: 62% activity compared to L-Lys-2-naphthylamide
Products: -
Products: -
?
Leu-4-nitroanilide + H2O
Leu + 4-nitroaniline
-
Substrates: 6.5% of the activity as compared to Arg-4-nitroanilide
Products: -
Products: -
?
Leu-4-nitroanilide + H2O
Leu + 4-nitroaniline
Substrates: 7% of the activity with Arg-4-nitroanilide
Products: -
Products: -
?
Lys-2-naphthylamide + H2O
Lys + 2-naphthylamine
-
Substrates: -
Products: -
Products: -
?
Lys-2-naphthylamide + H2O
Lys + 2-naphthylamine
-
Substrates: -
Products: -
Products: -
?
Lys-4-nitroanilide + H2O
Lys + 4-nitroaniline
-
Substrates: 74.3% of the activity as compared to Arg-4-nitroanilide
Products: -
Products: -
?
Lys-4-nitroanilide + H2O
Lys + 4-nitroaniline
Aspergillus niger CGMCC 3.1454
-
Substrates: 74.3% of the activity as compared to Arg-4-nitroanilide
Products: -
Products: -
?
Lys-4-nitroanilide + H2O
Lys + 4-nitroaniline
-
Substrates: 3.6% of the activity with Arg-7-amido-4-methylcoumarin
Products: -
Products: -
?
Lys-4-nitroanilide + H2O
Lys + 4-nitroaniline
Substrates: 5% of the activity with Arg-4-nitroanilide
Products: -
Products: -
?
Met-4-nitroanilide + H2O
Met + 4-nitroaniline
-
Substrates: 7.4% of the activity as compared to Arg-4-nitroanilide
Products: -
Products: -
?
Met-4-nitroanilide + H2O
Met + 4-nitroaniline
-
Substrates: 40.6% of the activity with Leu-4-nitroanilide
Products: -
Products: -
?
Phe-4-nitroanilide + H2O
Phe + 4-nitroaniline
-
Substrates: 14.9% of the activity as compared to Arg-4-nitroanilide
Products: -
Products: -
?
Phe-4-nitroanilide + H2O
Phe + 4-nitroaniline
Aspergillus niger CGMCC 3.1454
-
Substrates: 14.9% of the activity as compared to Arg-4-nitroanilide
Products: -
Products: -
?
Trp-4-nitroanilide + H2O
Trp + 4-nitroaniline
-
Substrates: 17.6% of the activity as compared to Arg-4-nitroanilide
Products: -
Products: -
?
Trp-4-nitroanilide + H2O
Trp + 4-nitroaniline
Aspergillus niger CGMCC 3.1454
-
Substrates: 17.6% of the activity as compared to Arg-4-nitroanilide
Products: -
Products: -
?
Tyr-4-nitroanilide + H2O
Tyr + 4-nitroaniline
-
Substrates: 22.1% of the activity as compared to Arg-4-nitroanilide
Products: -
Products: -
?
Tyr-4-nitroanilide + H2O
Tyr + 4-nitroaniline
Aspergillus niger CGMCC 3.1454
-
Substrates: 22.1% of the activity as compared to Arg-4-nitroanilide
Products: -
Products: -
?
Val-4-nitroanilide + H2O
Val + 4-nitroaniline
-
Substrates: 2.7% of the activity as compared to Arg-4-nitroanilide
Products: -
Products: -
?
Val-4-nitroanilide + H2O
Val + 4-nitroaniline
-
Substrates: 1.2% of the activity with Leu-4-nitroanilide
Products: -
Products: -
?
additional information
?
-
Substrates: substrate specificity, 4-nitroanilides of Gly, Glu, Asp, Phe, Pro, and Ala-Pro are poor substrates, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificity, 4-nitroanilides of Gly, Glu, Asp, Phe, Pro, and Ala-Pro are poor substrates, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: specificity for N-terminal Arg, Leu, Lys, Ala and Val
Products: -
Products: -
-
additional information
?
-
-
Substrates: specificity for N-terminal Arg, Leu, Lys, Ala and Val
Products: -
Products: -
-
additional information
?
-
Bacillus subtilis Zj016
-
Substrates: specificity for N-terminal Arg, Leu, Lys, Ala and Val
Products: -
Products: -
-
additional information
?
-
-
Substrates: no hydrolysis of amino acids with apolar groups, without free alpha-amino group, or anionic amino acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme is induced by interferon-gamma, the enzyme can trim the N-terminal extended precursor to antigenic peptides in the endoplasmic reticulum
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is induced by interferon-gamma, the enzyme can trim the N-terminal extended precursor to antigenic peptides in the endoplasmic reticulum
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is strictly specific for the removal of N-terminal basic residues from peptides and proteins
Products: -
Products: -
?
additional information
?
-
Substrates: the aminopeptidase binding site shares a similar structure to LTA4H (EC 3.3.2.6) at its ligand binding sites
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with L-Cys-7-amido-4-methylcoumarin, L-Asp-7-amido-4-methylcoumarin, and L-Glu-7-amido-4-methylcoumarin
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with L-Cys-7-amido-4-methylcoumarin, L-Asp-7-amido-4-methylcoumarin, and L-Glu-7-amido-4-methylcoumarin
Products: -
Products: -
?
additional information
?
-
Substrates: wild-type and Y409F/Y414F double mutant enzymes showed P1'-dependent cleavage of peptide substrates
Products: -
Products: -
-
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is strictly specific for the removal of N-terminal basic residues from peptides and proteins
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificity, the enzyme prefers Arg or Lys in N-terminal position, no activity with dipeptide-4-nitroanilides, overview
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme plays a role in peptide or protein precursor processing, the enzyme expression is up-regulated during ontogenesis
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme catalyzes the N-terminal cleavage of basic residues of peptide or protein substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: no detectable activity with L-Asp-2-naphthylamide
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Arg-peptides + H2O
?
-
Substrates: or Lys-peptides, metabolism of kinin
Products: -
Products: -
?
Arg-peptides + H2O
?
-
Substrates: attribution to inflammatory and wound healing processes
Products: -
Products: -
?
Arg-peptides + H2O
?
-
Substrates: takes part in later stages of protein degradation in chloroplasts
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme is induced by interferon-gamma, the enzyme can trim the N-terminal extended precursor to antigenic peptides in the endoplasmic reticulum
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is induced by interferon-gamma, the enzyme can trim the N-terminal extended precursor to antigenic peptides in the endoplasmic reticulum
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme plays a role in peptide or protein precursor processing, the enzyme expression is up-regulated during ontogenesis
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
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-
the enzyme requires a physiological concentration of chloride anions for optimal 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
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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
NaCl
-
retained maximum activity up to 50 mM NaCl, but further increase was accompanied with decreased enzyme activity
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, 10 microM, Arg 4-methylcoumarin 7-amide hydrolysis: 78% (wild-type enzyme); human peptide hormone, 100 microM, Arg 4-methylcoumarin 7-amide hydrolysis: 63.8% (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 activity 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
0.179
Arg-7-amido-4-methylcoumarin
37°C, pH 7.4, mutant enzyme Y409F/Y414F
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
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.07
Arg-7-amido-4-methylcoumarin
37°C, pH 7.4, mutant enzyme Y409F/Y414F
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
1.56
L-Lys-7-amido-4-methylcoumarin
mutant enzyme F297Y, at pH 7.4 and 37°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
17.2
Arg-7-amido-4-methylcoumarin
37°C, pH 7.4, mutant enzyme Y409F/Y414F
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
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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
64
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
5.5 - 6.5
6.5
7.2
7.4
7.5
8.4
8.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 5.5
-
pH 4.5: about 80% of maximal activity, pH 5.5: about 25% of maximal activity, activity is negligible at pH values beyond pH 4.0 and pH 6.0
5 - 7
5 - 9
6 - 9
additional information
5 - 9
-
pH 5.0: about 55% of maximal activity, pH 9.0: about 60% of maximal activity
6 - 9
-
pH 6.0: about 50% of maximal activity, pH 9.0: about 50% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
40
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15 - 45
-
15°C: about 30% of maximal activity, 25°C: about 75% of maximal activity, 45°C: about 70% of maximal activity
20 - 37
30 - 50
-
30°C: about 45% of maximal activity, 50°C: about 50% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.9
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
35968, 35970, 35972, 35973, 35978, 35981, 35982, 35983, 35992, 35999, 36003, 36004, 36005, 36006, 36007
-
-
brenda
-
35971, 35974, 35980, 35981, 35982, 35986, 35987, 35988, 35989, 35990, 35991, 35993, 35994, 35995, 35996, 35997, 35998, 35999, 36000
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
enzyme expression from embryo to adult rat, neuronal cell, developmental distribution, overview
brenda
additional information
highly expressed in the mouse brain compared to plasma and liver
brenda
-
cortex and anterior brain, striatum and middle brain, posterior brain
brenda
-
cortex and anterior brain, striatum and middle brain, posterior brain
brenda
-
cortex and anterior brain, striatum and middle brain, posterior brain
brenda
-
-
brenda
-
highest enzyme activity, mainly expressed in late spermatids during maturation
brenda
additional information
-
ubiquitous tissue distribution, expression level is tissue- and cell-type-dependent
brenda
additional information
-
the enzyme is up-regulated during long-term activation of normal and lymphoma T-cells
brenda
additional information
-
tissue distribution of enzyme activity, overview
brenda
additional information
developmental expression and activity pattern of Ap-B, in-situ hydridization, overview
brenda
additional information
-
tissue distribution of enzyme activity, overview
brenda
additional information
-
wide tissue distribution, expression level is tissue- and cell-type-dependent
brenda
additional information
-
tissue distribution of enzyme activity, overview
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
of germinal cells, proacrosmic granule of round spermatids
-
brenda
-
or loosly associated with cytoplasmic membrane, enzyme II
-
brenda
-
the enzyme is secreted, in PC-12 cells the active enzyme is associated to the external surface of the plassma mamabrane
-
brenda
present in secretory vesicles that contain cathepsin L with the neuropeptides enkephalin and neuropeptide Y
brenda
-
present in secretory vesicles that contain cathepsin L with the neuropeptides enkephalin and neuropeptide Y
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
LTB4 levels are persistently elevated in bronchoalveolar lavage fluid (BALF) of lipopolysaccharide (LPS)-induced ALI, and the leukotriene levels in pulmonary edema fluid are significantly higher in ALI patients compared to control patients with hydrostatic pulmonary edema. In addition, LTB4 level is increased in lung homogenates, and BALF of patients with IPF and the level of LTB4 correlate with the extent of fibrosis in histological sections
physiological function
additional information
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
physiological function
-
when murine ACE2 is given to mice for 4 weeks, a marked increase in serum ACE2 activity is detected. ACE2 leads to the dissipation of Ang II with formation of Ang (1-7)
physiological function
leukotriene A4 hydrolase (LTA4H) is a bifunctional enzyme that exhibits LTA4H and aminopeptidase activities, it is a key enzyme in the biosynthesis of leukotriene B4 (LTB4). LTA4H is well-known to regulate chemotactic activity of human neutrophils. LTB4 is secreted by neutrophils at inflammation sites in response to formyl peptides, playing an important role in neutrophil activation and migration to formyl peptides
physiological function
leukotriene A4 hydrolase (LTA4H) is a bifunctional enzyme that exhibits LTA4H and aminopeptidase activities
physiological function
one of the key enzymes hydrolyzing LAT1-utilizing amide prodrugs
physiological function
one of the key enzymes hydrolyzing LAT1-utilizing amide prodrugs
physiological function
one of the key enzymes hydrolyzing LAT1-utilizing amide prodrugs
Show AA Sequence and Transmembrane Helices (484 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
110000
52000 - 58000
72000
72000 - 75000
73000
74000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterotrimer
monomer
additional information
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
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
no glycoprotein
phosphoprotein
aminopeptidase B (Ap-B) is phosphorylated in HEK293 cells on at least three differents sites which could be Ser 7, Tyr 409 and Tyr 414. Phosphorylation of the enzyme appears to delay its turnover
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme in complex with inhibitors SAHA or M344, X-ray diffraction structure determination and analysis
crystallized using the hanging-drop vapour diffusion method. X-ray diffraction data to 2.3 A resolution are collected using an orthorhombic crystal form belonging to space group P2(1)2(1)2(1), with unit-cell parameters a = 76.55, b = 130.86, c = 170.87 A
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F297A
the mutant shows no activity with kallidin or [Arg0]-Met-enkephalin
F297Y
the mutation causes a significant decrease in hydrolytic activity toward synthetic and peptide substrates (13fold and 15fold lower catalytic efficiencies with L-Arg-7-amido-4-methylcoumarin and L-Lys-7-amido-4-methylcoumarin, respectively. No activity with kallidin or [Arg0]-Met-enkephalin) as well as chloride anion sensitivity
Q169N
-
mutant shows a significant decrease in hydrolytic activity toward the fluorescent substrate Lys-4-methylcoumaryl-7-amide (MCA). Mutant shows an increase in IC50 values of inhibitors that interact with the catalytic pocket of aminopeptidase B. Km (Arg 4-methylcoumarin 7-amide) similar to wild-type, kcat (Arg 4-methylcoumarin 7-amide) decreased compared to wild-type. Km (Lys 4-methylcoumarin 7-amide) increased compared to wild-type, kcat (Lys 4-methylcoumarin 7-amide) decreased compared to wild-type
Y409F
kcat/Km for Arg-7-amido-4-methylcoumarin of the mutant enzyme is 44.6fold lower than that of the wild-type enzyme
Y409F/Y414F
the double mutant enzyme cleaves peptides with a Pro residue at the P1' site, which is uncommon among the M1 family of aminopeptidases. The Y409F/Y414F double mutant enzyme shows higher activity and broader substrate specificity than the wild-type enzyme toward angiotensin III and the tested analogs. kcat/Km for Arg-7-amido-4-methylcoumarin of the mutant enzyme is 10.4fold lower than that of the wild-type enzyme
Y414F
kcat/Km for Arg-7-amido-4-methylcoumarin of the mutant enzyme is 23.6fold lower than that of the wild-type enzyme
Y229H
-
Km and kcat (L-Arg-2-naphthylamide) decreased compared to wild-type
Y409F
-
Km and kcat (L-Arg-2-naphthylamide) decreased compared to wild-type
Y441F
-
Km and kcat (L-Arg-2-naphthylamide) decreased compared to wild-type
additional information
-
immobilization of enzyme with 1% CaCl2 and 2.5% alginate, increase of in stability for immobilized enzyme
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 8
6 - 9
5 - 8
-
optimal stability at pH 7.0 and retains more than 80% of the maximum activity between pH 5.0 and 8.0 after incubation at 40 °C for 60 min
5 - 8
-
most stable in pH range 5.8-7.8. Retains 50% activity at pH 5.0 and pH 8.0
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
37
40
45
50
55
60
additional information
-
stabilized against heat in the presence of Mn2+ or Co2+
55
-
EDTA-dialyzed enzyme is completely inactivated within 2 min. The enzyme of which the divalent cation has has been replaced with Mn2+ or Co2+ is quite stable up to 10 min. The Mn2+-dialyzed sample gradually loses its activity, only 75% of its original levels remains after 10 min
60
-
immobilized enzyme with 55% remaining enzyme activity at 60°C, free enzyme with 45% remaining activity at 60°C
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
avizafone, a prodrug for diazepam, is a stabilizer to minimize inactivation of the enzyme during lyophilization
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
DMSO
-
immobilized enzyme stable at higher concentrations compared to free enzyme
Ethanol
-
15%, immobilized enzyme still 58% remaining activity, free enzyme inactivated
urea
-
at 1.5 M urea only 10% remaining enzyme acitvity, at 2.0 M urea complete loss of enzyme activity
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0-4°C, citric acid-phosphate buffer or Tris-HCl buffer, 30 days, increase of activity
-
4C, 0.01 M beta,beta-dimethylglutarate buffer, pH 7.2, 0.1 mM DTT
4°C, pH 6.0, 3.5% (NH4)2SO4, aggregation of monomers to polymer during storage, decomposition to monomer by substrate
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
2 forms
279.5fold after heat inactivation, ammonium sulfate fractionation and column chromatographies
-
80.9fold to homogeneity by gel filtration, anion exchange chromatography, and again gel filtration
-
glutathione-Sepharose 4B column chromatography and Q-Sepharose column chromatography
-
glutathione-Sepharose 4B column chromatography and Sephadex G-150 gel filtration
-
native enzyme 159000fold by ammonium sulfate fractionation, ultrafiltration, cation exchange chromatography and gel filtration
-
native enzyme 460fold to homogeneity by ion exchange and hydroxy apatite chromatography, and ion exchange chromatography
-
native enzyme 69.3fold by ammonium sulfate fractionation, anion exchange and hydrophobic interaction chromatography, and gel filtration to homogeneity
-
Ni-NTA column chromatography and DEAE Trisacryl Plus M column chromatography
-
recombinant enzyme 5fold from Escherichia coli by ion exchange chromatography
successive chromatographies on Sephadex G-100 and phenylsepharose CL-4B
-
the recombinant enzyme (APB-AN) is purified to homogeneity by ammonium sulfate precipitation and gel filtration chromatography of the culture supernatant
-
Toyopearl DEAE-650 column chromatography, Mono Q column chromatography, and DEAE-650 column chromatography
-
using a glutathione-Sepharose 4B column, cleaving of the fusion-enzyme by thrombin, using a benzamidine-Sepharose and a Q-Sepharose column
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, phylogenetic analysis
-
DNA and amino acid sequence determination and analysis, the gene encoding the enzyme is localized on chromosome 1, genetic organization and structure, overview
-
expressed in Escherichia coli
expression in Escherichia coli
gene rnpep, DNA and amino acid sequence determination and analysis, localization on chromosome 1q32 in a high transcript density region, genetic organization and structure, overview
-
testis enzyme, DNA and amino acid sequence determination and analysis, genetic organization and structure, overview, expression in Escherichia coli
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
Drug repurposing of histone deacetylase inhibitors that alleviate neutrophilic inflammation in acute lung injury and idiopathic pulmonary fibrosis via inhibiting leukotriene A4 hydrolase and blocking LTB4 biosynthesis
food industry
food industry
-
aminopeptidases have significant application prospects in improving flavor, promoting directional hydrolysis of protein and releasing bioactive substances. Aminopeptidases are mainly applied in the debittering of protein hydrolysates, the deep hydrolysis of protein, and the production of condiments, cheese, and bioactive peptides
food industry
Bacillus subtilis Zj016
-
aminopeptidases have significant application prospects in improving flavor, promoting directional hydrolysis of protein and releasing bioactive substances. Aminopeptidases are mainly applied in the debittering of protein hydrolysates, the deep hydrolysis of protein, and the production of condiments, cheese, and bioactive peptides
-
food industry
-
aminopeptidases have significant application prospects in improving flavor, promoting directional hydrolysis of protein and releasing bioactive substances. Aminopeptidases are mainly applied in the debittering of protein hydrolysates, the deep hydrolysis of protein, and the production of condiments, cheese, and bioactive peptides
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sharma, A.; Padwal-Desai, S.R.; Ninjoor, V.
Intracellular hydrolases of Aspergillus parasiticus and Aspergillus flavus
Biochem. Biophys. Res. Commun.
159
464-471
1989
Aspergillus parasiticus, Aspergillus flavus
brenda
Mendz, G.L.; McCall, M.N.; Kuchel, P.W.
Characterization of leukocyte enzymes involved in the release of amino acids in incubated blood cell lysates
J. Biol. Chem.
264
2108-2117
1989
Homo sapiens
brenda
Schmidt, U.; Weller, D.; Holder, A.; Lieberknecht, A.
Total synthesis of OF4949-III, a natural inhibitor of aminopeptidase B from Ehrlich ascites carcinoma cells
Tetrahedron Lett.
29
3227-3230
1988
Mus musculus
-
brenda
Lauffart, B.; Mantle, D.
Rationalization of aminopeptidase activities in human skeletal muscle soluble extract
Biochim. Biophys. Acta
956
300-306
1988
Homo sapiens
brenda
Harbeson, S.L.; Rich, D.H.
Inhibition of arginine aminopeptidase by bestatin and arphamenine analogues. Evidence for a new mode of binding to aminopeptidases
Biochemistry
27
7301-7310
1988
Rattus norvegicus
brenda
Lauffart, B.; McDermott, J.; Jones, P.; Mantle, D.
Amino acid inhibition of aminopeptidases purified from human cerebral cortex
Biochem. Soc. Trans.
16
849-850
1988
Homo sapiens
-
brenda
Ishiura, S.; Yamamoto, T.; Yamamoto, M.; Nojima, M.; Aoyagi, T.; Sugita, H.
Human skeletal muscle contains two major aminopeptidases: an anion-activated aminopeptidase B and an aminopeptidase M-like enzyme
J. Biochem.
102
1023-1031
1987
Homo sapiens
brenda
Ocain, T.D.; Rich, D.H.
L-Lysinethiol: a subnanomolar inhibitor of aminopeptidase B
Biochem. Biophys. Res. Commun.
145
1038-1042
1987
Rattus norvegicus
brenda
Hiraoka, B.Y.
Immunochemical properties and intracellular localization of two molecular forms of arginine aminopeptidase in Streptococcus mitis ATCC 9811
Biochim. Biophys. Acta
841
166-172
1985
Streptococcus mitis
brenda
Blahovec, J.; Bartik, M.; Kasafirek, E.
Isolation and partial characterization of bovine liver aminopeptidase B
Collect. Czech. Chem. Commun.
50
1249-1257
1985
Bos taurus
-
brenda
Chan, S.A.T.; Toursarkissian, K.; Sweeny, J.P.; Jones, T.H.D.
Dipeptidyl-aminopeptidases and aminopeptidases in Dictyostelium discoideum
Biochem. Biophys. Res. Commun.
127
962-968
1985
Dictyostelium discoideum
brenda
Mantle, D.; Lauffart, B.; Pennington, R.J.T.
Purification and partial characterization of arginine aminopeptidases from human skeletal muscle
Biochem. Soc. Trans.
12
826-827
1984
Homo sapiens
-
brenda
Hiraoka, B.Y.; Fukasawa, K.; Harada, M.
Purification and characterization of two novel arginine aminopeptidases from Streptococcus mitis ATCC 9811
J. Biochem.
94
1201-1208
1983
Streptococcus mitis
brenda
Matsuzawa, T.; Hatsugai, M.
Effect of age on the activity of rat testicular arginine-aminopeptidase
Experientia
39
388-389
1983
Rattus norvegicus
brenda
Soederling, E.; Mkinen, K.K.
Modification of the Cl- -activated arginine aminopeptidases from rat liver and human erythrocytes: a comparative study
Arch. Biochem. Biophys.
220
11-21
1983
Homo sapiens, Rattus norvegicus
brenda
Soederling, E.
Substrate specificities of Cl- -activated arginine aminopeptidases from human and rat origin
Arch. Biochem. Biophys.
220
1-10
1983
Homo sapiens, Rattus norvegicus
brenda
Soederling, E.
Effect of Cl- on the function of the Cl- -activated arginine aminopeptidase purified from human erythrocytes
Arch. Biochem. Biophys.
216
105-115
1982
Homo sapiens
brenda
Kawata, S.; Takayama, S.; Ninimiya, K.; Makisumi, S.
Purification and some properties of porcine liver aminopeptidase B
J. Biochem.
88
1025-1032
1980
Sus scrofa
brenda
Kawata, S.; Takayama, S.; Ninomiya, K.; Makisumi, S.
Porcine liver aminopeptidase B. Substrate specificity and inhibition by amino acids
J. Biochem.
88
1601-1605
1980
Sus scrofa
brenda
Knuuttila, M.; Virtanen, K.; Soederling, E.; Maekinen, K.K.
A chloride-activated aminopeptidase in rat inflammatory exudate: properties and evidence of the origin of the enzyme
Biochem. Biophys. Res. Commun.
81
374-381
1978
Rattus norvegicus
brenda
Aoyagi, T.; Suda, H.; Nagai, M.; Ogawa, K.; Suzuki, J.; Takeuchi, T.; Umezawa, H.
Aminopeptidase activities on the surface of mammalian cells
Biochim. Biophys. Acta
452
131-143
1976
Rattus norvegicus, Platyrrhini, Canis lupus familiaris
brenda
Suda, H.; Aoyagi, T.; Takeuchi, T.; Umezawa, H.
Inhibition of aminopeptidase B and leucine aminopeptidase by bestatin and its stereoisomer
Arch. Biochem. Biophys.
177
196-200
1976
Rattus norvegicus
brenda
Mkinen, P.L.; Mkinen, K.K.
Fractionation and properties of aminopeptidase B during purification and storage
Int. J. Pept. Protein Res.
4
241-255
1972
Rattus norvegicus
brenda
Maekinen, K.K.
Evidence for the aggregation of aminopeptidase B during storage and breakdown of the aggregate by substrate and serum albumin
Biochim. Biophys. Acta
271
413-418
1972
Rattus norvegicus
brenda
Maekinen, K.K.; Maekinen, P.L.
Evidence on erythrocyte aminopeptidase B
Int. J. Pept. Protein Res.
111
41-47
1971
Rattus norvegicus
-
brenda
Maekinen, K.K.; Paunio, K.U.
Demonstration of aminopeptidase B in human periodontal tissues
Acta Chem. Scand.
24
1103-1104
1970
Homo sapiens
brenda
Maekinen, P.L.; Raekallio, J.; Maekinen, K.K.
On the localization of aminopeptidase B and separation of its two molecular forms by automated recycling chromatography
Acta Chem. Scand.
24
1101-1102
1970
Rattus norvegicus
brenda
Maekinen, K.K.; Hopsu-Havu, V.K.
The active centre of aminopeptidase B. I. The effects of various chemical reagents
Enzymologia
32
333-346
1967
Rattus norvegicus
brenda
Maekinen, K.K.; Hopsu-Havu, V.K.
The active centre of aminopeptidase B. II. Kinetic studies
Enzymologia
32
347-363
1967
Rattus norvegicus
brenda
Hopsu, V.K.; Maekinen, K.K.; Glenner, G.G.
Purification of a mammalian peptidase selective for N-terminal arginine and lysine residues: aminopeptidase B
Arch. Biochem. Biophys.
114
557-566
1966
Rattus norvegicus
brenda
Hopsu-Havu, V.K.; Maekinen, K.K.
A simplified method for purification of rat liver aminopeptidase B
Arch. Biochem. Biophys.
118
257-258
1967
Rattus norvegicus
-
brenda
Hopsu, V.K.; Maekinen, K.K.; Glenner, G.G.
Characterization of aminopeptidase B: substrate specificity and affector studies
Arch. Biochem. Biophys.
114
567-575
1966
Rattus norvegicus
brenda
McDonald, J.K.; Barrett, A.J.
Soluble arginyl aminopeptidase
Mammalian Proteases, Academic Press
2
48-55
1986
Homo sapiens, Rattus norvegicus, Sus scrofa
-
brenda
Cadel, S.; Pierotti, A.R.; Foulon, T.; Creminon, C.; Barre, N.; Segretain, D.; Cohen, P.
Aminopeptidase B in the rat testes: isolation, functional properties and cellular localization in the seminiferous tubules
Mol. Cell. Endocrinol.
110
149-160
1995
Rattus norvegicus
brenda
Cadel, S.; Foulon, T.; Viron, A.; Balogh, A.; Midol-Monnet, S.; Noel, N.; Cohen, P.
Aminopeptidase B from the rat testis is a bifunctional enzyme structurally related to leukotriene-A4 hydrolase
Proc. Natl. Acad. Sci. USA
94
2963-2968
1997
Rattus norvegicus (O09175)
brenda
Cook, M.; Adam, Z.
Purification and characterization of an arginyl peptidase from the chloroplast stroma of pea seedlings
Plant Physiol. Biochem.
35
163-168
1997
Lathyrus oleraceus
-
brenda
Toldra, F.; Falkous, G.; Flores, M.; Mantle, D.
Comparison of aminopeptidase inhibition by amino acids in human and porcine skeletal muscle tissues in vitro
Comp. Biochem. Physiol. B
115
445-450
1996
Homo sapiens, Sus scrofa
-
brenda
Fukasawa, K.M.; Fukasawa, K.; Kanai, M.; Fujii, S.; Harada, M.
Molecular cloning and expression of rat liver aminopeptidase B
J. Biol. Chem.
271
30731-30735
1996
Homo sapiens, Rattus norvegicus
brenda
Yamada, M.; Sukenaga, Y.; Fujii, H.; Abe, F.; Takeuchi, T.
Purification and characterization of a ubenimex (Bestatin)-sensitive aminopeptidase B-like enzyme from K562 human chronic myeloid leukemia cells
FEBS Lett.
342
53-56
1994
Homo sapiens
brenda
Belbacene, N.; Mari, B.; Rossi, B.; Auberger, P.
Characterization and purification of T lymphocyte aminopeptidase B: a putative marker of T cell activation
Eur. J. Immunol.
23
1948-1955
1993
Homo sapiens
brenda
Nagata, Y.; Mizutani, S.; Nomura, S.; Kurauchi, O.; Kasugai, M.; Tomoda, Y.
Purification and properties of human placental aminopeptidase B
Enzyme
45
165-173
1991
Homo sapiens
brenda
Floderus, E.; Linder, L.E.; Sund, M.S.
Characterization of membrane-associated arginine aminopeptidase in Streptococcus sanguis 903
Curr. Microbiol.
21
145-149
1990
Streptococcus sanguinis, Streptococcus sanguinis 903
-
brenda
Herranz, R.; Garcia-Lopez, M.T.; Perez, C.
Synergistic inhibition of aminopeptidase B by penicillamine or cysteine and metallic salts
Arch. Pharm.
324
239-241
1991
Mus musculus
brenda
Flores, M.; Aristoy, M.C.; Toldra, F.
Feedback inhibition of porcine muscle alanyl and arginyl aminopeptidases in cured meat products
J. Agric. Food Chem.
46
4982-4986
1998
Sus scrofa
-
brenda
Sanz, Y.; Toldra, F.
Purification and characterization of an arginine aminopeptidase from Lactobacillus sakei
Appl. Environ. Microbiol.
68
1980-1987
2002
Latilactobacillus sakei
brenda
Suzuki, H.; Kamatani, S.; Kumagai, H.
Purification and characterization of aminopeptidase B from Escherichia coli K-12
Biosci. Biotechnol. Biochem.
65
1549-1558
2001
Escherichia coli
brenda
Goldstein, J.M.; Nelson, D.; Kordula, T.; Mayo, J.A.; Travis, J.
Extracellular arginine aminopeptidase from Streptococcus gordonii FSS2
Infect. Immun.
70
836-843
2002
Streptococcus gordonii (Q938E9), Streptococcus gordonii, Streptococcus gordonii FSS2 (Q938E9), Streptococcus gordonii FSS2
brenda
Tanioka, T.; Hattori, A.; Masuda, S.; Nomura, Y.; Nakayama, H.; Mizutani, S.; Tsujimoto, M.
Human leukocyte-derived arginine aminopeptidase. The third member of the oxytocinase subfamily of aminopeptidases
J. Biol. Chem.
278
32275-32283
2003
Homo sapiens (Q6P179), Homo sapiens
brenda
Huston, A.L.; Methe, B.; Deming, J.W.
Purification, characterization, and sequencing of an extracellular cold-active aminopeptidase produced by marine psychrophile Colwellia psychrerythraea strain 34H
Appl. Environ. Microbiol.
70
3321-3328
2004
Colwellia psychrerythraea
brenda
Saitoh, Y.; Koizumi, K.; Minami, T.; Sekine, K.; Sakurai, H.; Saiki, I.
A derivative of aminopeptidase inhibitor (BE15) has a dual inhibitory effect of invasion and motility on tumor and endothelial cells
Biol. Pharm. Bull.
29
709-712
2006
Homo sapiens
brenda
Petrov, V.V.; Fagard, R.H.; Lijnen, P.J.
Arginine-aminopeptidase in rat cardiac fibroblastic cells participates in angiotensin peptide turnover
Cardiovasc. Res.
61
724-735
2004
Rattus norvegicus
brenda
Piesse, C.; Cadel, S.; Gouzy-Darmon, C.; Jeanny, J.C.; Carriere, V.; Goidin, D.; Jonet, L.; Gourdji, D.; Cohen, P.; Foulon, T.
Expression of aminopeptidase B in the developing and adult rat retina
Exp. Eye Res.
79
639-648
2004
Rattus norvegicus (O09175)
brenda
Berthonneau, J.; Rodier, M.H.; El Moudni, B.; Jacquemin, J.L.
Toxoplasma gondii: Purification and characterization of an immunogenic metallopeptidase
Exp. Parasitol.
95
158-162
2000
Toxoplasma gondii
brenda
Mercado-Flores, Y.; Noriega-Reyes, Y.; Ramirez-Zavala, B.; Hernandez-Rodriguez, C.; Villa-Tanaca, L.
Purification and characterization of aminopeptidase (pumAPE) from Ustilago maydis
FEMS Microbiol. Lett.
234
247-253
2004
Mycosarcoma maydis
brenda
Fundoiano-Hershcovitz, Y.; Rabinovitch, L.; Shulami, S.; Reiland, V.; Shoham, G.; Shoham, Y.
The ywad gene from Bacillus subtilis encodes a double-zinc aminopeptidase
FEMS Microbiol. Lett.
243
157-163
2005
Bacillus subtilis (P25152), Bacillus subtilis
brenda
Foulon, T.; Cadel, S.; Piesse, C.; Cohen, P.
Aminopeptidase B
Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds) Academic Press
1
328-332
2004
Rattus norvegicus, Homo sapiens, Mus musculus
-
brenda
Agirregoitia, N.; Laiz-Carrion, R.; Varona, A.; Rio, M.P.; Mancera, J.M.; Irazusta, J.
Distribution of peptidase activity in teleost and rat tissues
J. Comp. Physiol. B
175
433-444
2005
Rattus norvegicus, Oncorhynchus mykiss, Sparus aurata
brenda
Millership, J.J.; Chappell, C.; Okhuysen, P.C.; Snowden, K.F.
Characterization of aminopeptidase activity from three species of microsporidia: Encephalitozoon cuniculi, Encephalitozoon hellem, and Vittaforma corneae
J. Parasitol.
88
843-848
2002
Vittaforma corneae
brenda
Ohishi, K.; Yamamoto, T.; Tomofuji, T.; Tamaki, N.; Watanabe, T.
Isolation and characterization of aminopeptidase from Capnocytophaga granulosa ATCC 51502
Oral Microbiol. Immunol.
20
67-72
2005
Capnocytophaga granulosa
brenda
Gasparello-Clemente, E.; Casis, L.; Varona, A.; Gil, J.; Irazusta, J.; Silveira, P.F.
Aminopeptidases in visceral organs during alterations in body fluid volume and osmolality
Peptides
24
1367-1372
2003
Rattus norvegicus
brenda
Cadel, S.; Piesse, C.; Gouzy-Darmon, C.; Cohen, P.; Foulon, T.
Arginyl aminopeptidase
Proteases in Biology and Disease (Hooper, N. M. ; Lendeckel, U. ) Springer
2
113-126
2004
Rattus norvegicus, Homo sapiens, Mus musculus, Bos taurus
-
brenda
Bellemare, A.; Vernoux, N.; Morisset, D.; Bourbonnais, Y.
Human pre-elafin inhibits a Pseudomonas aeruginosa-secreted peptidase and prevents its proliferation in complex media
Antimicrob. Agents Chemother.
52
483-490
2008
Pseudomonas aeruginosa
brenda
Fukasawa, K.M.; Hirose, J.; Hata, T.; Ono, Y.
Aspartic acid 405 contributes to the substrate specificity of aminopeptidase B
Biochemistry
45
11425-11431
2006
Rattus norvegicus
brenda
Hirose, J.; Ohsaki, T.; Nishimoto, N.; Matuoka, S.; Hiromoto, T.; Yoshida, T.; Minoura, T.; Iwamoto, H.; Fukasawa, K.M.
Characterization of the metal-binding site in aminopeptidase B
Biol. Pharm. Bull.
29
2378-2382
2006
Rattus norvegicus
brenda
Pinyol, M.; Bea, S.; Pla, L.; Ribrag, V.; Bosq, J.; Rosenwald, A.; Campo, E.; Jares, P.
Inactivation of RB1 in mantle-cell lymphoma detected by nonsense-mediated mRNA decay pathway inhibition and microarray analysis
Blood
109
5422-5429
2007
Homo sapiens
brenda
Pham, V.L.; Cadel, M.S.; Gouzy-Darmon, C.; Hanquez, C.; Beinfeld, M.C.; Nicolas, P.; Etchebest, C.; Foulon, T.
Aminopeptidase B, a glucagon-processing enzyme: site directed mutagenesis of the Zn2+-binding motif and molecular modelling
BMC Biochem.
8
21
2007
Rattus norvegicus
brenda
Knotz, S.; Boersma, M.; Saborowski, R.
Microassays for a set of enzymes in individual small marine copepods
Comp. Biochem. Physiol. A
145
406-411
2006
Acartia clausii, Centropages typicus, Ditrichocorycaeus anglicus, Paracalanus parvus, Temora longicornis
brenda
Bolumar, T.; Sanz, Y.; Aristoy, M.; Toldra, F.
Protease (PrA and PrB) and prolyl and arginyl aminopeptidase activities from Debaryomyces hansenii as a function of growth phase and nutrient sources
Int. J. Food Microbiol.
107
20-26
2006
Debaryomyces hansenii, Debaryomyces hansenii CECT 12487
brenda
Hwang, S.R.; ONeill, A.; Bark, S.; Foulon, T.; Hook, V.
Secretory vesicle aminopeptidase B related to neuropeptide processing: molecular identification and subcellular localization to enkephalin- and NPY-containing chromaffin granules
J. Neurochem.
100
1340-1350
2007
Bos taurus (A2T1U6), Bos taurus, Rattus norvegicus
brenda
Banegas, I.; Prieto, I.; Vives, F.; Alba, F.; de Gasparo, M.; Segarra, A.B.; Hermoso, F.; Duran, R.; Ramirez, M.
Brain aminopeptidases and hypertension
J. Renin Angiotensin Aldosterone Syst.
7
129-134
2006
Rattus norvegicus
brenda
Qu, H.Q.; Marchand, L.; Frechette, R.; Bacot, F.; Lu, Y.; Polychronakos, C.
No association of type 1 diabetes with a functional polymorphism of the LRAP gene
Mol. Immunol.
44
2135-2138
2007
Homo sapiens
brenda
Hui, M.; Hui, K.S.
A novel aminopeptidase with highest preference for lysine
Neurochem. Res.
31
95-102
2006
Rattus norvegicus
brenda
Hwang, S.R.; Hook, V.
Zinc regulation of aminopeptidase B involved in neuropeptide production
FEBS Lett.
582
2527-2531
2008
Rattus norvegicus
brenda
Bogra, P.; Singh, J.; Singh, H.
Immobilization of goat brain aminopeptidase B in calcium alginate beads
Biocatal. Biotransform.
27
96-101
2009
Capra aegagrus
-
brenda
Bogra, P.; Singh, J.; Singh, H.
Purification and characterization of aminopeptidase B from goat brain
Process Biochem.
44
776-780
2009
Capra aegagrus
-
brenda
Sakamoto, Y.; Suzuki, Y.; Iizuka, I.; Tateoka, C.; Roppongi, S.; Okada, H.; Nonaka, T.; Morikawa, Y.; Nakamura, K.; Ogasawara, W.; Tanaka, N.
Crystallization and preliminary X-ray crystallographic studies of dipeptidyl aminopeptidase BII from Pseudoxanthomonas mexicana WO24
Acta Crystallogr. Sect. F
70
221-224
2014
Pseudoxanthomonas mexicana (V5YM14), Pseudoxanthomonas mexicana WO24 (V5YM14), Pseudoxanthomonas mexicana WO24
brenda
Ogawa, Y.; Ohnishi, A.; Goto, Y.; Sakuma, Y.; Watanabe, J.; Hattori, A.; Tsujimoto, M.
Role of glutamine-169 in the substrate recognition of human aminopeptidase B
Biochim. Biophys. Acta
1840
1872-1881
2014
Homo sapiens
brenda
Cadel, S.; Darmon, C.; Pernier, J.; Herve, G.; Foulon, T.
The M1 family of vertebrate aminopeptidases: Role of evolutionarily conserved tyrosines in the enzymatic mechanism of aminopeptidase B
Biochimie
109
67-77
2015
Rattus norvegicus
brenda
Ye, M.; Wysocki, J.; Gonzalez-Pacheco, F.R.; Salem, M.; Evora, K.; Garcia-Halpin, L.; Poglitsch, M.; Schuster, M.; Batlle, D.
Murine recombinant angiotensin-converting enzyme 2: effect on angiotensin II-dependent hypertension and distinctive angiotensin-converting enzyme 2 inhibitor characteristics on rodent and human angiotensin-converting enzyme 2
Hypertension
60
730-740
2012
Homo sapiens, Mus musculus
brenda
Cadel, S.; Darmon, C.; Desert, A.; Mahbouli, M.; Piesse, C.; Ghelis, T.; Lafont, R.; Foulon, T.
The effects of curcumin, mangiferin, resveratrol and other natural plant products on aminopeptidase B activity
Biochem. Biophys. Res. Commun.
512
832-837
2019
Rattus norvegicus
brenda
Ohnishi, A.; Watanabe, J.; Ogawa, Y.; Goto, Y.; Hattori, A.; Tsujimoto, M.
Involvement of phenylalanine 297 in the construction of the substrate pocket of human aminopeptidase B
Biochemistry
54
6062-6070
2015
Homo sapiens (Q9H4A4), Homo sapiens
brenda
Zhang, F.; Wu, D.; Wang, G.; Hou, S.; Ou-Yang, P.; Huang, J.; Xu, X.
Synthesis and biological evaluation of novel 1,2,3-benzotriazin-4-one derivatives as leukotriene A4 hydrolase aminopeptidase inhibitors
Chin. Chem. Lett.
28
1044-1048
2017
Homo sapiens (P09960)
-
brenda
Lu, W.; Yao, X.; Ouyang, P.; Dong, N.; Wu, D.; Jiang, X.; Wu, Z.; Zhang, C.; Xu, Z.; Tang, Y.; Zou, S.; Liu, M.; Li, J.; Zeng, M.; Lin, P.; Cheng, F.; Huang, J.
Drug repurposing of histone deacetylase inhibitors that alleviate neutrophilic inflammation in acute lung injury and idiopathic pulmonary fibrosis via inhibiting leukotriene A4 hydrolase and blocking LTB4 biosynthesis
J. Med. Chem.
60
1817-1828
2017
Homo sapiens (P09960)
brenda
Song, P.; Feng, W.
Functional expression and characterization of a novel aminopeptidase B from Aspergillus niger in Pichia pastoris
3 Biotech
11
366
2021
Aspergillus niger, Aspergillus niger CGMCC 3.1454
brenda
Adiceam, E.; Devakumaran, S.; Cadel, S.; Foulon, T.; Ghelis, T.
The aminopeptidase B (Ap-B) is phosphorylated in HEK293cells
Biochimie
201
204-212
2022
Homo sapiens (Q9H4A4)
brenda
Hugele, A.; Loeffler, S.; Molina, B.H.; Guillon, M.; Montaser, A.B.; Auriola, S.; Huttunen, K.M.
Aminopeptidase B can bioconvert L-type amino acid transporter 1 (LAT1)-utilizing amide prodrugs in the brain
Front. Pharmacol.
13
1034964
2022
Homo sapiens (Q9H4A4), Rattus norvegicus (O09175), Mus musculus (Q8VCT3)
brenda
Attri, P.; Jodha, D.; Bansal, P.; Singh, J.; Dhanda, S.
Membrane bound aminopeptidase B of a potential probiotic Pediococcus acidilactici NCDC 252 purification, physicochemical and kinetic characterization
Int. J. Pept. Res. Ther.
27
1641-1655
2021
Pediococcus acidilactici, Pediococcus acidilactici NCDC 252
-
brenda
Ohnishi, A.; Watanabe, J.; Tsujimoto, M.
Importance of Tyr409 and Tyr414 in constructing the substrate pocket of human aminopeptidase B
Mol. Cell. Biochem.
469
1-8
2020
Homo sapiens (Q9H4A4)
brenda
Rautiola, D.; Updyke, J.L.; Nelson, K.M.; Siegel, R.A.
Diazepam prodrug stabilizes human aminopeptidase B during lyophilization
Mol. Pharm.
17
453-460
2020
Homo sapiens (Q9H4A4)
brenda
Wang, Y.; Zhao, P.; Zhou, Y.; Hu, X.; Xiong, H.
From bitter to delicious properties and uses of microbial aminopeptidases
World J. Microbiol. Biotechnol.
39
72
2023
Bacillus subtilis, Bacillus subtilis BR151
brenda
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