Any feedback?
Information on EC 3.4.11.6 - aminopeptidase B and Organism(s) Homo sapiens
for references in articles please use BRENDA:EC3.4.11.6Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
3.4.11.6 aminopeptidase BSpecify your search results
Word Map
- 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
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
release of N-terminal Arg and Lys from oligopeptides when P1' is not Pro. Also acts on arylamides of Arg and Lys
Synonyms
apb, arylamidase, aminopeptidase b, arginine aminopeptidase, cytosol aminopeptidase, arginyl aminopeptidase, aminopeptidase-b, l-rap, dap bii, arginine-aminopeptidase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aminopeptidase, arginine
-
-
-
-
APB
arginine aminopeptidase
-
-
-
-
arginyl aminopeptidase
arylamidase II
-
-
-
-
Cl--activated arginine aminopeptidase
-
-
-
-
cytosol aminopeptidase
-
-
-
-
L-arginine aminopeptidase
-
-
-
-
leukocyte-derived arginine aminopeptidase
additional information
arginyl aminopeptidase
-
-
-
-
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
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
-
CAS REGISTRY NUMBER
COMMENTARY
9073-92-1
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Arg-4-methylcoumarin 7-amide + H2O
Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Arg-4-methylcoumaryl-7-amide + H2O
Arg + 7-amino-4-methylcoumarin
-
-
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
100% activity
-
-
?
L-Gln-7-amido-4-methylcoumarin + H2O
L-Gln + 7-amino-4-methylcoumarin
about 1% activity compared to L-Arg-7-amido-4-methylcoumarin
-
-
?
L-Ile-7-amido-4-methylcoumarin + H2O
L-Ile + 7-amino-4-methylcoumarin
about 1% activity compared to L-Arg-7-amido-4-methylcoumarin
-
-
?
L-Leu-7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
about 1% activity compared to L-Arg-7-amido-4-methylcoumarin
-
-
?
L-Lys-7-amido-4-methylcoumarin + H2O
L-Lys + 7-amino-4-methylcoumarin
about 45% activity compared to L-Arg-7-amido-4-methylcoumarin
-
-
?
L-Met-7-amido-4-methylcoumarin + H2O
L-Met + 7-amino-4-methylcoumarin
about 1% activity compared to L-Arg-7-amido-4-methylcoumarin
-
-
?
L-Phe-7-amido-4-methylcoumarin + H2O
L-Phe + 7-amino-4-methylcoumarin
about 5% activity compared to L-Arg-7-amido-4-methylcoumarin
-
-
?
L-Tyr-7-amido-4-methylcoumarin + H2O
L-Tyr + 7-amino-4-methylcoumarin
about 7% activity compared to L-Arg-7-amido-4-methylcoumarin
-
-
?
L-Val-7-amido-4-methylcoumarin + H2O
L-Val + 7-amino-4-methylcoumarin
about 1% activity compared to L-Arg-7-amido-4-methylcoumarin
-
-
?
Lys-4-methylcoumarin 7-amide + H2O
Lys + 7-amino-4-methylcoumarin
-
-
-
-
?
[Arg0]-Met-enkephalin + H2O
Met-enkephalin + de-[Tyr]-Met-enkephalin
i.e. RYGGFM
-
-
?
Arg-peptides + H2O
?
-
attribution to inflammatory and wound healing processes
-
-
?
L-Ala-7-amido-4-methylcoumarin + H2O
L-Ala + 7-amino-4-methylcoumarin
about 2% activity compared to L-Arg-7-amido-4-methylcoumarin
-
-
?
additional information
?
-
the enzyme is induced by interferon-gamma, the enzyme can trim the N-terminal extended precursor to antigenic peptides in the endoplasmic reticulum
-
?
additional information
?
-
-
the enzyme is induced by interferon-gamma, the enzyme can trim the N-terminal extended precursor to antigenic peptides in the endoplasmic reticulum
-
?
additional information
?
-
-
the enzyme probably is involved in the final stages of peptide and protein precursor processing and maturation mechanisms via the exopeptidase pathway and thereby in some inflammatory processes and tumour development
-
-
?
additional information
?
-
-
the enzyme from testis preferably removes Arg and/or Lys residues from the N-terminus of various peptides, no activity with substrate possessing Pro at the P1 position
-
-
?
additional information
?
-
-
the enzyme is strictly specific for the removal of N-terminal basic residues from peptides and proteins
-
-
?
additional information
?
-
no activity with L-Cys-7-amido-4-methylcoumarin, L-Asp-7-amido-4-methylcoumarin, and L-Glu-7-amido-4-methylcoumarin
-
-
?
additional information
?
-
-
no activity with L-Cys-7-amido-4-methylcoumarin, L-Asp-7-amido-4-methylcoumarin, and L-Glu-7-amido-4-methylcoumarin
-
-
?
additional information
?
-
the aminopeptidase binding site shares a similar structure to LTA4H (EC 3.3.2.6) at its ligand binding sites
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Arg-peptides + H2O
?
-
attribution to inflammatory and wound healing processes
-
-
?
additional information
?
-
the enzyme is induced by interferon-gamma, the enzyme can trim the N-terminal extended precursor to antigenic peptides in the endoplasmic reticulum
-
?
additional information
?
-
-
the enzyme is induced by interferon-gamma, the enzyme can trim the N-terminal extended precursor to antigenic peptides in the endoplasmic reticulum
-
?
additional information
?
-
-
the enzyme probably is involved in the final stages of peptide and protein precursor processing and maturation mechanisms via the exopeptidase pathway and thereby in some inflammatory processes and tumour development
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cl-
Zinc
essential zinc-binding site HEXXH at amino acid residues 370-374 with a second glutamic acid separated by 18 amino acids
Zn2+
Cl-
-
required for activity
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
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)
Substance P
-
human peptide hormone, 100 microM, Arg 4-methylcoumarin 7-amide hydrolysis: 63.8% (wild-type enzyme); human peptide hormone, 10 microM, Arg 4-methylcoumarin 7-amide hydrolysis: 78% (wild-type enzyme)
tert-butyl bestatin
-
i.e. BE17, the BE15 derivative has a dual inhibitory effect of invasion and motility on tumor and endothelial cells
[(2Z)-3-[(7-chloro-4-oxo-1,2,3-benzotriazin-3(4H)-yl)methyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
11.7% inhibition at 0.01 mM
[(2Z)-3-[2-(6-methyl-4-oxo-1,2,3-benzotriazin-3(4H)-yl)ethyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
54.8% inhibition at 0.01 mM
[(2Z)-3-[2-(6-nitro-4-oxo-1,2,3-benzotriazin-3(4H)-yl)ethyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
32.8% inhibition at 0.01 mM
[(2Z)-3-[2-(7-bromo-4-oxo-1,2,3-benzotriazin-3(4H)-yl)ethyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
53.5% inhibition at 0.01 mM
[(2Z)-3-[2-(7-chloro-4-oxo-1,2,3-benzotriazin-3(4H)-yl)ethyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
65.2% inhibition at 0.01 mM
[(2Z)-3-[2-(7-fluoro-4-oxo-1,2,3-benzotriazin-3(4H)-yl)ethyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
36.4% inhibition at 0.01 mM
[(2Z)-3-[4-(6-methyl-4-oxo-1,2,3-benzotriazin-3(4H)-yl)butyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
26.0% inhibition at 0.01 mM
[(2Z)-3-[4-(6-nitro-4-oxo-1,2,3-benzotriazin-3(4H)-yl)butyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
22.2% inhibition at 0.01 mM
[(2Z)-3-[4-(7-bromo-4-oxo-1,2,3-benzotriazin-3(4H)-yl)butyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
26.8% inhibition at 0.01 mM
[(2Z)-3-[4-(7-chloro-4-oxo-1,2,3-benzotriazin-3(4H)-yl)butyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
33.7% inhibition at 0.01 mM
[(2Z)-3-[4-(7-fluoro-4-oxo-1,2,3-benzotriazin-3(4H)-yl)butyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
26.0% inhibition at 0.01 mM
[(2Z)-3-[5-(6-methyl-4-oxo-1,2,3-benzotriazin-3(4H)-yl)pentyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
52.6% inhibition at 0.01 mM
[(2Z)-3-[5-(6-nitro-4-oxo-1,2,3-benzotriazin-3(4H)-yl)pentyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
34.1% inhibition at 0.01 mM
[(2Z)-3-[5-(7-bromo-4-oxo-1,2,3-benzotriazin-3(4H)-yl)pentyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
78.8% inhibition at 0.01 mM
[(2Z)-3-[5-(7-chloro-4-oxo-1,2,3-benzotriazin-3(4H)-yl)pentyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
76.1% inhibition at 0.01 mM
[(2Z)-3-[5-(7-fluoro-4-oxo-1,2,3-benzotriazin-3(4H)-yl)pentyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
54.0% inhibition at 0.01 mM
[(2Z)-3-[6-(5-chloro-4-oxo-1,2,3-benzotriazin-3(4H)-yl)hexyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
37.8% inhibition at 0.01 mM
[(2Z)-3-[6-(6-chloro-4-oxo-1,2,3-benzotriazin-3(4H)-yl)hexyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
68.8% inhibition at 0.01 mM
[(2Z)-3-[6-(6-methyl-4-oxo-1,2,3-benzotriazin-3(4H)-yl)hexyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
62.5% inhibition at 0.01 mM
[(2Z)-3-[6-(6-nitro-4-oxo-1,2,3-benzotriazin-3(4H)-yl)hexyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
36.9% inhibition at 0.01 mM
[(2Z)-3-[6-(7-bromo-4-oxo-1,2,3-benzotriazin-3(4H)-yl)hexyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
70.6% inhibition at 0.01 mM
[(2Z)-3-[6-(7-chloro-4-oxo-1,2,3-benzotriazin-3(4H)-yl)hexyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
80.6% inhibition at 0.01 mM
[(2Z)-3-[6-(7-fluoro-4-oxo-1,2,3-benzotriazin-3(4H)-yl)hexyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
51.7% inhibition at 0.01 mM
[(2Z)-3-[6-(7-methoxy-4-oxo-1,2,3-benzotriazin-3(4H)-yl)hexyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
50.3% inhibition at 0.01 mM
[(2Z)-3-[6-(7-nitro-4-oxo-1,2,3-benzotriazin-3(4H)-yl)hexyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
34.6% inhibition at 0.01 mM
[(2Z)-3-[6-(8-chloro-4-oxo-1,2,3-benzotriazin-3(4H)-yl)hexyl]-4-oxo-1,3-thiazolidin-2-ylidene]cyanamide
37.9% inhibition at 0.01 mM
[(2Z)-4-oxo-3-[(4-oxo-1,2,3-benzotriazin-3(4H)-yl)methyl]-1,3-thiazolidin-2-ylidene]cyanamide
over 10.0% inhibition at 0.01 mM
[(2Z)-4-oxo-3-[2-(4-oxo-1,2,3-benzotriazin-3(4H)-yl)ethyl]-1,3-thiazolidin-2-ylidene]cyanamide
30.2% inhibition at 0.01 mM
[(2Z)-4-oxo-3-[2-[4-oxo-6-(trifluoromethyl)-1,2,3-benzotriazin-3(4H)-yl]ethyl]-1,3-thiazolidin-2-ylidene]cyanamide
55.6% inhibition at 0.01 mM
[(2Z)-4-oxo-3-[4-[4-oxo-6-(trifluoromethyl)-1,2,3-benzotriazin-3(4H)-yl]butyl]-1,3-thiazolidin-2-ylidene]cyanamide
41.6% inhibition at 0.01 mM
[(2Z)-4-oxo-3-[5-[4-oxo-6-(trifluoromethyl)-1,2,3-benzotriazin-3(4H)-yl]pentyl]-1,3-thiazolidin-2-ylidene]cyanamide
50.1% inhibition at 0.01 mM
[(2Z)-4-oxo-3-[6-[4-oxo-6-(trifluoromethyl)-1,2,3-benzotriazin-3(4H)-yl]hexyl]-1,3-thiazolidin-2-ylidene]cyanamide
60.1% inhibition at 0.01 mM
[(2Z)-4-oxo-3-[[4-oxo-6-(trifluoromethyl)-1,2,3-benzotriazin-3(4H)-yl]methyl]-1,3-thiazolidin-2-ylidene]cyanamide
15.8% inhibition at 0.01 mM
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NaCl
the enzyme requires a physiological concentration of NaCl (150 mM) for optimal activity
additional information
-
the enzyme is up-regulated during long-term activation of normal and lymphoma T-cells
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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 chloride concentration
-
additional information
additional information
-
comparison of values for various peptide substrates and enzyme sources
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
14.2
L-Arg-7-amido-4-methylcoumarin
mutant enzyme F297Y, at pH 7.4 and 37°C
2.61
L-Lys-7-amido-4-methylcoumarin
mutant enzyme F297Y, at pH 7.4 and 37°C
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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.2
7.4
7.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
-
the enzyme is up-regulated during long-term activation of normal and lymphoma T-cells
additional information
-
ubiquitous tissue distribution, expression level is tissue- and cell-type-dependent
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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
leukotriene A4 hydrolase (LTA4H) is a bifunctional enzyme that exhibits LTA4H and aminopeptidase activities
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). AMPB_HUMAN
650
0
72596
Swiss-Prot
Mitochondrion (Reliability: 3)
Q7RU04_HUMAN
658
0
73498
TrEMBL
Mitochondrion (Reliability: 4)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
72000 - 75000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme in complex with inhibitors SAHA or M344, X-ray diffraction structure determination and analysis
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Lauffart, B.; Mantle, D.
Rationalization of aminopeptidase activities in human skeletal muscle soluble extract
Biochim. Biophys. Acta
956
300-306
1988
Homo sapiens
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
-
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
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
-
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
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
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
Maekinen, K.K.; Paunio, K.U.
Demonstration of aminopeptidase B in human periodontal tissues
Acta Chem. Scand.
24
1103-1104
1970
Homo sapiens
McDonald, J.K.; Barrett, A.J.
Soluble arginyl aminopeptidase
Mammalian Proteases, Academic Press
2
48-55
1986
Homo sapiens, Rattus norvegicus, Sus scrofa
-
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
-
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
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
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
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
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
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
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
Homo sapiens, Mus musculus, Rattus norvegicus
-
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
Bos taurus, Homo sapiens, Mus musculus, Rattus norvegicus
-
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
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
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
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
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
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)
-
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)
EXTERNAL LINKS (specific for EC-Number 3.4.11.6)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
