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Information on EC 3.4.11.1 - leucyl aminopeptidase and Organism(s) Homo sapiens and UniProt Accession Q9NZ08

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.11 Aminopeptidases
                3.4.11.1 leucyl aminopeptidase
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Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: Q9NZ08 not found.
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
release of an N-terminal amino acid, Xaa-/-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolysed, but rates on arylamides are exceedingly low
release of an N-terminal amino acid, Xaa-/-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid mides and methyl esters are also readily hydrolysed, but rates on arylamides are exceedingly low
Synonyms
leucine aminopeptidase, erap2, leucyl aminopeptidase, leucine amino peptidase, l-leucine aminopeptidase, leucinaminopeptidase, pilsap, leucine aminopeptidase 3, leucylaminopeptidase, adipocyte-derived leucine aminopeptidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
adipocyte-derived leucine aminopeptidase
-
-
Aminopeptidase
-
-
Aminopeptidase A/I
-
-
-
-
aminopeptidase I
-
-
aminopeptidase II
-
-
Aminopeptidase III
-
-
aminopeptidase N
-
-
cathepsin III
cytosol aminopeptidase
DR57
-
-
-
-
endoplasmic reticulum aminopeptidase
-
ER-aminopeptidase-1
-
-
FTBL protein
-
-
FTBL proteins
-
-
-
-
L-leucine aminopeptidase
leucinamide aminopeptidase
leucinaminopeptidase
leucine aminopeptidase
leucine aminopeptidase 3
Leucyl aminopeptidase
-
-
-
-
leucyl aminopeptidase (animal)
-
-
leucyl peptidase
peptidase S
PILS-AP
-
-
Placental leucine aminopeptidase
-
-
PLAP
-
-
proline aminopeptidase
-
-
-
-
Prolyl aminopeptidase
-
-
-
-
proteins, specific or class, FTBL
-
-
-
-
puromycin-insensitive leucine specific aminopeptidase
-
-
additional information
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
release of an N-terminal amino acid, Xaa-/-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolysed, but rates on arylamides are exceedingly low
show the reaction diagram
Lys528 is located near the entrance of the substrate pocket and is important for maximal activity by maintaining the appropriate structure of the substrate binding pocket
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
PATHWAY SOURCE
PATHWAYS
CAS REGISTRY NUMBER
COMMENTARY hide
9001-61-0
-
90119-07-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-leucine-7-amido-4-methylcoumarin + H2O
L-leucine + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
amino acid amides + H2O
amino acid + NH3
show the reaction diagram
angiotensin II + H2O
angiotensin IV + ?
show the reaction diagram
-
-
through angiotensin III
?
angiotensin II + H2O
Asp + angiotensin III
show the reaction diagram
-
i.e. Asp-Tyr-Arg-Val-Tyr-Ile-His-Pro-Phe
i.e. Tyr-Arg-Val-Tyr-Ile-His-Pro-Phe
-
?
Arg-Ala-Arg + H2O
Arg + Ala-Arg
show the reaction diagram
-
Ala-p-nitroanilide is used as substrate with very low turnover rate
in the assay hydrolysis of Ala-p-nitroanilide is monitored
-
?
Arg-Ser-Arg + H2O
Arg + Ser-Arg
show the reaction diagram
-
Ala-p-nitroanilide is used as substrate with very low turnover rate
in the assay hydrolysis of Ala-p-nitroanilide is monitored
-
?
dynorphin A + H2O
?
show the reaction diagram
-
-
-
?
kallidin + H2O
?
show the reaction diagram
-
-
-
-
?
kallidin + H2O
Leu + bradykinin
show the reaction diagram
-
i.e. LRPPGFSPFR
i.e. RPPGFSPFR
?
L-amino acid-peptide + H2O
amino acid + peptide
show the reaction diagram
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
L-arginyl-7-amido-4-methylcoumarin + H2O
L-arginine + 7-amino-4-methylcoumarin
show the reaction diagram
ERAP2 preferentially hydrolyzes Arg-aminomethylcoumarin and Lys-aminomethylcoumarin
-
-
?
L-Leu 7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
L-Leu-p-nitroanilide + H2O
L-Leu + p-nitroaniline
show the reaction diagram
-
-
-
-
?
L-Leu-p-nitroanilide + H2O
L-leucine + p-nitroaniline
show the reaction diagram
L-leucine 4-nitroanilide + H2O
L-leucine + 4-nitroaniline
show the reaction diagram
-
-
-
?
L-leucine amide + H2O
L-leucine + NH3
show the reaction diagram
-
-
-
-
?
L-leucine-7-amido-4-methylcoumarin + H2O
L-leucine + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
L-leucyl-7-amido-4-methylcoumarin + H2O
L-leucine + 7-amino-4-methylcoumarin
show the reaction diagram
L-lysyl-7-amido-4-methylcoumarin + H2O
L-lysine + 7-amino-4-methylcoumarin
show the reaction diagram
ERAP2 preferentially hydrolyzes Arg-aminomethylcoumarin and Lys-aminomethylcoumarin
-
-
?
Leu-4-nitroanilide + H2O
Leu + 4-nitroaniline
show the reaction diagram
-
-
-
?
Leu-7-amido-4-methylcoumarin + H2O
leucine + 7-amino-4-methylcoumarin
show the reaction diagram
-
Leu replaced by Met
-
-
?
Leu-enkephalin
?
show the reaction diagram
-
-
-
-
?
Leu-Ser-Ile-Ile-Asn-Phe-Glu-Lys-Leu + H2O
? + Ile-Asn-Phe-Glu-Lys-Leu
show the reaction diagram
-
-
-
-
?
Leu-Ser-Ile-Ile-Asn-Phe-Glu-Lys-Leu + H2O
? + Ile-Ile-Asn-Phe-Glu-Lys-Leu
show the reaction diagram
-
-
-
-
?
Leu-Ser-Ile-Ile-Asn-Phe-Glu-Lys-Leu + H2O
L-leucine + Ser-Ile-Ile-Asn-Phe-Glu-Lys-Leu
show the reaction diagram
-
trimming of further model epitope precursors to antigenic peptides are also tested
-
-
?
leucyl-7-amido-4-methylcoumarin + H2O
leucine + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
Neurokinin A + H2O
?
show the reaction diagram
-
-
-
?
Neuromedin B + H2O
?
show the reaction diagram
-
-
-
?
Proteins + H2O
?
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
angiotensin II + H2O
angiotensin IV + ?
show the reaction diagram
-
-
through angiotensin III
?
angiotensin II + H2O
Asp + angiotensin III
show the reaction diagram
-
i.e. Asp-Tyr-Arg-Val-Tyr-Ile-His-Pro-Phe
i.e. Tyr-Arg-Val-Tyr-Ile-His-Pro-Phe
-
?
kallidin + H2O
Leu + bradykinin
show the reaction diagram
-
i.e. LRPPGFSPFR
i.e. RPPGFSPFR
?
Proteins + H2O
?
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
activation
Mn2+
-
activation
Zinc
-
zinc-metallopeptidase, contains the HEXXH motif
additional information
-
metallopeptidase
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-amino-3-(L-tyrosylamino)benzoic acid
-
benzyl N-(3-amino-4-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-tryptophanate
-
benzyl N-[3-amino-4-(L-leucylamino)benzoyl]-L-tryptophanate
-
benzyl N-[3-amino-4-(L-norleucylamino)benzoyl]-L-tryptophanate
-
benzyl N-[3-amino-4-(L-norleucylamino)benzoyl]-L-valinate
-
benzyl N-[3-amino-4-[(O-benzyl-L-tyrosyl)amino]benzoyl]-L-tryptophanate
-
benzyl N-[4-amino-3-(D-norleucylamino)benzoyl]-L-valinate
-
benzyl N-[4-amino-3-(L-norleucylamino)benzoyl]-L-tryptophanate
-
benzyl N-[4-amino-3-(L-tyrosylamino)benzoyl]-L-tryptophanate
-
benzyl N-[4-amino-3-[(O-benzyl-L-tyrosyl)amino]benzoyl]-L-tryptophanate
-
methyl 3-amino-4-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoate
-
methyl 4-amino-3-(L-norleucylamino)benzoate
-
methyl 4-amino-3-[[(2S)-2-amino-4-(4-hydroxyphenyl)butanoyl]amino]benzoate
-
methyl N-(3-amino-4-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-tyrosinate
-
methyl N-(4-amino-3-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-tyrosinate
-
methyl N-[3-amino-4-(L-arginylamino)benzoyl]-L-tyrosinate
-
methyl N-[3-amino-4-(L-norleucylamino)benzoyl]-L-tyrosinate
-
methyl N-[3-amino-4-(L-tyrosylamino)benzoyl]-L-tyrosinate
-
methyl N-[4-amino-3-(D-norleucylamino)benzoyl]-D-tyrosinate
-
methyl N-[4-amino-3-(L-arginylamino)benzoyl]-D-tyrosinate
-
methyl N-[4-amino-3-(L-tyrosylamino)benzoyl]-L-threoninate
-
methyl N-[4-amino-3-(L-tyrosylamino)benzoyl]-L-tyrosinate
-
methyl N2-(3,4-diaminobenzoyl)-L-argininate
-
methyl N2-(3,4-diaminobenzoyl)-L-lysinate
-
methyl N2-(3-amino-4-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-argininate
-
methyl N2-(4-amino-3-[[(2S)-2-amino-4-(4-hydroxyphenyl)butanoyl]amino]benzoyl)-L-lysinate
-
methyl N2-(4-amino-3-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-lysinate
-
methyl N2-[3-amino-4-(L-tyrosylamino)benzoyl]-L-lysinate
-
methyl N2-[4-amino-3-(L-arginylamino)benzoyl]-L-lysinate
-
methyl N2-[4-amino-3-(L-norleucylamino)benzoyl]-D-argininate
-
methyl N2-[4-amino-3-(L-norleucylamino)benzoyl]-L-lysinate
-
methyl N2-[4-amino-3-([(2S)-2-amino-4-[4-(benzyloxy)phenyl]butanoyl]amino)benzoyl]-L-lysinate
-
N-(3,4-diaminobenzoyl)-L-tryptophan
-
N-(3-amino-4-[[(2S)-2-amino-4-(4-hydroxyphenyl)butanoyl]amino]benzoyl)-L-tryptophan
-
N-(4-amino-3-[[(2R)-2-amino-4-(4-hydroxyphenyl)butanoyl]amino]benzoyl)-L-tryptophan
-
N-[3-amino-4-(L-arginylamino)benzoyl]-L-tryptophan
-
N-[3-amino-4-(L-norleucylamino)benzoyl]-L-tryptophan
-
N-[3-amino-4-(L-tyrosylamino)benzoyl]-L-tryptophan
-
N-[4-amino-3-(L-arginylamino)benzoyl]-L-tryptophan
-
N-[4-amino-3-(L-norleucylamino)benzoyl]-L-tryptophan
-
N-[4-amino-3-(L-tyrosylamino)benzoyl]-L-tryptophan
-
N2-[4-amino-3-(L-leucylamino)benzoyl]-L-lysine
-
1,10-phenanthroline
-
-
4-amino-3-(L-arginylamino)benzoic acid
-
4-amino-3-(L-tyrosylamino)benzoic acid
-
amastatin
benzyl N-(3-amino-4-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-tryptophanate
-
benzyl N-(3-amino-4-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-valinate
-
benzyl N-(4-amino-3-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-tryptophanate
-
benzyl N-[3-amino-4-(L-leucylamino)benzoyl]-L-tryptophanate
-
benzyl N-[3-amino-4-(L-norleucylamino)benzoyl]-L-tryptophanate
-
benzyl N-[3-amino-4-(L-norleucylamino)benzoyl]-L-valinate
-
benzyl N-[3-amino-4-([(2S)-2-amino-4-[4-(benzyloxy)phenyl]butanoyl]amino)benzoyl]-L-tryptophanate
-
benzyl N-[3-amino-4-[(O-benzyl-L-tyrosyl)amino]benzoyl]-L-tryptophanate
-
benzyl N-[4-amino-3-(D-norleucylamino)benzoyl]-L-valinate
-
benzyl N-[4-amino-3-(L-norleucylamino)benzoyl]-L-tryptophanate
-
benzyl N-[4-amino-3-(L-tyrosylamino)benzoyl]-L-tryptophanate
-
benzyl N-[4-amino-3-(L-tyrosylamino)benzoyl]-L-valinate
-
benzyl N-[4-amino-3-[(O-benzyl-L-tyrosyl)amino]benzoyl]-L-tryptophanate
-
bestatin
EDTA
-
reactivation by divalent cations
iodoacetic acid
-
-
methyl 3-amino-4-(L-arginylamino)benzoate
-
methyl 3-amino-4-(L-leucylamino)benzoate
-
methyl 3-amino-4-(L-norleucylamino)benzoate
-
methyl 3-amino-4-(L-tyrosylamino)benzoate
-
methyl 3-amino-4-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoate
-
methyl 4-amino-3-(L-arginylamino)benzoate
-
methyl 4-amino-3-(L-norleucylamino)benzoate
-
methyl 4-amino-3-(L-tyrosylamino)benzoate
-
methyl N-(3,4-diaminobenzoyl)-L-tyrosinate
-
methyl N-(3-amino-4-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-tyrosinate
-
methyl N-(4-amino-3-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-tyrosinate
-
methyl N-[3-amino-4-(L-arginylamino)benzoyl]-L-tyrosinate
-
methyl N-[3-amino-4-(L-norleucylamino)benzoyl]-L-tyrosinate
-
methyl N-[3-amino-4-(L-tyrosylamino)benzoyl]-L-tyrosinate
-
methyl N-[3-amino-4-[(O-benzyl-L-tyrosyl)amino]benzoyl]-L-tyrosinate
-
methyl N-[4-amino-3-(D-norleucylamino)benzoyl]-D-tyrosinate
-
methyl N-[4-amino-3-(L-arginylamino)benzoyl]-D-tyrosinate
-
methyl N-[4-amino-3-(L-tyrosylamino)benzoyl]-L-threoninate
-
methyl N-[4-amino-3-(L-tyrosylamino)benzoyl]-L-tyrosinate
-
methyl N2-(3-amino-4-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-argininate
-
methyl N2-(4-amino-3-[[(2S)-2-amino-4-(4-hydroxyphenyl)butanoyl]amino]benzoyl)-L-lysinate
-
methyl N2-(4-amino-3-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-lysinate
-
methyl N2-[3-amino-4-(L-arginylamino)benzoyl]-L-lysinate
-
methyl N2-[3-amino-4-(L-norleucylamino)benzoyl]-L-lysinate
-
methyl N2-[3-amino-4-(L-tyrosylamino)benzoyl]-L-lysinate
-
methyl N2-[4-amino-3-(L-arginylamino)benzoyl]-L-lysinate
-
methyl N2-[4-amino-3-(L-leucylamino)benzoyl]-L-lysinate
-
methyl N2-[4-amino-3-(L-norleucylamino)benzoyl]-D-argininate
-
methyl N2-[4-amino-3-(L-norleucylamino)benzoyl]-L-lysinate
-
methyl N2-[4-amino-3-([(2S)-2-amino-4-[4-(benzyloxy)phenyl]butanoyl]amino)benzoyl]-L-lysinate
-
N-(3,4-diaminobenzoyl)-L-tryptophan
-
N-(3-amino-4-[[(2S)-2-amino-4-(4-hydroxyphenyl)butanoyl]amino]benzoyl)-L-tryptophan
-
N-(3-amino-4-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-valine
-
N-(4-amino-3-[[(2R)-2-amino-4-(4-hydroxyphenyl)butanoyl]amino]benzoyl)-L-tryptophan
-
N-ethylmaleimide
-
-
N-[3-amino-4-(L-arginylamino)benzoyl]-L-tryptophan
-
N-[3-amino-4-(L-norleucylamino)benzoyl]-L-tryptophan
-
N-[3-amino-4-(L-norleucylamino)benzoyl]-L-valine
-
N-[3-amino-4-(L-tyrosylamino)benzoyl]-L-tryptophan
-
N-[4-amino-3-(D-norleucylamino)benzoyl]-L-valine
-
N-[4-amino-3-(L-arginylamino)benzoyl]-L-tryptophan
-
N-[4-amino-3-(L-arginylamino)benzoyl]-L-valine
-
N-[4-amino-3-(L-norleucylamino)benzoyl]-L-tryptophan
-
N-[4-amino-3-(L-tyrosylamino)benzoyl]-L-tryptophan
-
N-[4-amino-3-(L-tyrosylamino)benzoyl]-L-valine
-
N2-[4-amino-3-(L-leucylamino)benzoyl]-L-lysine
-
N2-[4-amino-3-(L-phenylalanylamino)benzoyl]-L-lysine
-
N2-[4-amino-3-(L-tyrosylamino)benzoyl]-L-lysine
-
p-chloromercuribenzoate
-
-
p-Hydroxymercuriphenylsulfonate
-
-
puromycin
-
-
purpurin
-
is isolated from the natural product library and inhibits the proliferation of HUVECs in a dose-dependent manner with an IC50 value of 0.03 mM. The proliferation of other types of cells such as HeLa (cervical carcinoma) and C8161 (melanoma) is not significantly inhibited by purpurin at the same concentration range used for HUVEC. Purpurin selectively inhibits the proliferation of endothelial cells over the other types of mammalian cells. Purpurin does not significantly affect the viability of HUVEC up to 0.02 mM treatment. A marginal decrease in the HUVEC viability is observed between 0.04-0.06 mM, and the significant cytotoxicity is observed at over 0.08 mM treatment with purpurin. The treatment of purpurin does not significantly affect the expression level of A-LAP in HUVEC
Thr(OtBu)-Phe-Pro
-
-
ubenimex
suppresses the enzyme activity in vivo in K562-LAP3 cells, detection method development and evaluation, overview
Zn2+
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
concanavalin A
-
activation
-
interferon-gamma
-
induced by
-
phytohaemagglutinin
-
activation
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.28
Leu-4-nitroanilide
-
-
4.02 - 4.2
leucinamide
1.25
leucine-7-amido-4-methylcoumarin
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
inhibition kinetics
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1
4-amino-3-(L-tyrosylamino)benzoic acid
Homo sapiens
pH and temperature not specified in the publication
0.013
benzyl N-(3-amino-4-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-tryptophanate
Homo sapiens
pH and temperature not specified in the publication
0.0089
benzyl N-[3-amino-4-(L-leucylamino)benzoyl]-L-tryptophanate
Homo sapiens
pH and temperature not specified in the publication
0.0025
benzyl N-[3-amino-4-(L-norleucylamino)benzoyl]-L-tryptophanate
Homo sapiens
pH and temperature not specified in the publication
0.1
benzyl N-[3-amino-4-(L-norleucylamino)benzoyl]-L-valinate
Homo sapiens
pH and temperature not specified in the publication
0.0011
benzyl N-[3-amino-4-[(O-benzyl-L-tyrosyl)amino]benzoyl]-L-tryptophanate
Homo sapiens
pH and temperature not specified in the publication
0.1
benzyl N-[4-amino-3-(D-norleucylamino)benzoyl]-L-valinate
Homo sapiens
pH and temperature not specified in the publication
0.00098
benzyl N-[4-amino-3-(L-norleucylamino)benzoyl]-L-tryptophanate
Homo sapiens
pH and temperature not specified in the publication
0.0098
benzyl N-[4-amino-3-(L-tyrosylamino)benzoyl]-L-tryptophanate
Homo sapiens
pH and temperature not specified in the publication
0.1
benzyl N-[4-amino-3-[(O-benzyl-L-tyrosyl)amino]benzoyl]-L-tryptophanate
Homo sapiens
pH and temperature not specified in the publication
0.1
methyl 3-amino-4-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoate
Homo sapiens
pH and temperature not specified in the publication
0.1
methyl 4-amino-3-(L-norleucylamino)benzoate
Homo sapiens
pH and temperature not specified in the publication
0.1
methyl 4-amino-3-[[(2S)-2-amino-4-(4-hydroxyphenyl)butanoyl]amino]benzoate
Homo sapiens
pH and temperature not specified in the publication
0.0094
methyl N-(3-amino-4-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-tyrosinate
Homo sapiens
pH and temperature not specified in the publication
0.0077
methyl N-(4-amino-3-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-tyrosinate
Homo sapiens
pH and temperature not specified in the publication
0.0026
methyl N-[3-amino-4-(L-arginylamino)benzoyl]-L-tyrosinate
Homo sapiens
pH and temperature not specified in the publication
0.1
methyl N-[3-amino-4-(L-norleucylamino)benzoyl]-L-tyrosinate
Homo sapiens
pH and temperature not specified in the publication
0.016
methyl N-[3-amino-4-(L-tyrosylamino)benzoyl]-L-tyrosinate
Homo sapiens
pH and temperature not specified in the publication
0.1
methyl N-[4-amino-3-(D-norleucylamino)benzoyl]-D-tyrosinate
Homo sapiens
pH and temperature not specified in the publication
0.0096
methyl N-[4-amino-3-(L-arginylamino)benzoyl]-D-tyrosinate
Homo sapiens
pH and temperature not specified in the publication
0.1
methyl N-[4-amino-3-(L-tyrosylamino)benzoyl]-L-threoninate
Homo sapiens
pH and temperature not specified in the publication
0.11
methyl N-[4-amino-3-(L-tyrosylamino)benzoyl]-L-tyrosinate
Homo sapiens
pH and temperature not specified in the publication
0.035
methyl N2-(3,4-diaminobenzoyl)-L-argininate
Homo sapiens
pH and temperature not specified in the publication
0.1
methyl N2-(3,4-diaminobenzoyl)-L-lysinate
Homo sapiens
pH and temperature not specified in the publication
0.012
methyl N2-(3-amino-4-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-argininate
Homo sapiens
pH and temperature not specified in the publication
0.1
methyl N2-(4-amino-3-[[(2S)-2-amino-4-(4-hydroxyphenyl)butanoyl]amino]benzoyl)-L-lysinate
Homo sapiens
pH and temperature not specified in the publication
0.002
methyl N2-(4-amino-3-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-lysinate
Homo sapiens
pH and temperature not specified in the publication
0.1
methyl N2-[3-amino-4-(L-tyrosylamino)benzoyl]-L-lysinate
Homo sapiens
pH and temperature not specified in the publication
0.042
methyl N2-[4-amino-3-(L-arginylamino)benzoyl]-L-lysinate
Homo sapiens
pH and temperature not specified in the publication
0.0107
methyl N2-[4-amino-3-(L-norleucylamino)benzoyl]-D-argininate
Homo sapiens
pH and temperature not specified in the publication
0.018
methyl N2-[4-amino-3-(L-norleucylamino)benzoyl]-L-lysinate
Homo sapiens
pH and temperature not specified in the publication
0.1
methyl N2-[4-amino-3-([(2S)-2-amino-4-[4-(benzyloxy)phenyl]butanoyl]amino)benzoyl]-L-lysinate
Homo sapiens
pH and temperature not specified in the publication
0.1
N-(3,4-diaminobenzoyl)-L-tryptophan
Homo sapiens
pH and temperature not specified in the publication
0.008
N-(3-amino-4-[[(2S)-2-amino-4-(4-hydroxyphenyl)butanoyl]amino]benzoyl)-L-tryptophan
Homo sapiens
pH and temperature not specified in the publication
0.038
N-(4-amino-3-[[(2R)-2-amino-4-(4-hydroxyphenyl)butanoyl]amino]benzoyl)-L-tryptophan
Homo sapiens
pH and temperature not specified in the publication
0.0038
N-[3-amino-4-(L-arginylamino)benzoyl]-L-tryptophan
Homo sapiens
pH and temperature not specified in the publication
0.0028
N-[3-amino-4-(L-norleucylamino)benzoyl]-L-tryptophan
Homo sapiens
pH and temperature not specified in the publication
0.019
N-[3-amino-4-(L-tyrosylamino)benzoyl]-L-tryptophan
Homo sapiens
pH and temperature not specified in the publication
0.0012
N-[4-amino-3-(L-arginylamino)benzoyl]-L-tryptophan
Homo sapiens
pH and temperature not specified in the publication
0.0036
N-[4-amino-3-(L-norleucylamino)benzoyl]-L-tryptophan
Homo sapiens
pH and temperature not specified in the publication
0.012
N-[4-amino-3-(L-tyrosylamino)benzoyl]-L-tryptophan
Homo sapiens
pH and temperature not specified in the publication
0.0068
N2-[4-amino-3-(L-leucylamino)benzoyl]-L-lysine
Homo sapiens
pH and temperature not specified in the publication
0.1
4-amino-3-(L-arginylamino)benzoic acid
Homo sapiens
pH and temperature not specified in the publication
0.0032
4-amino-3-(L-tyrosylamino)benzoic acid
Homo sapiens
pH and temperature not specified in the publication
0.011
benzyl N-(3-amino-4-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-tryptophanate
Homo sapiens
pH and temperature not specified in the publication
0.1
benzyl N-(3-amino-4-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-valinate
Homo sapiens
pH and temperature not specified in the publication
0.0239
benzyl N-(4-amino-3-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-tryptophanate
Homo sapiens
pH and temperature not specified in the publication
0.021
benzyl N-[3-amino-4-(L-leucylamino)benzoyl]-L-tryptophanate
Homo sapiens
pH and temperature not specified in the publication
0.000709
benzyl N-[3-amino-4-(L-norleucylamino)benzoyl]-L-tryptophanate
Homo sapiens
pH and temperature not specified in the publication
0.0062
benzyl N-[3-amino-4-(L-norleucylamino)benzoyl]-L-valinate
Homo sapiens
pH and temperature not specified in the publication
0.07
benzyl N-[3-amino-4-([(2S)-2-amino-4-[4-(benzyloxy)phenyl]butanoyl]amino)benzoyl]-L-tryptophanate
Homo sapiens
pH and temperature not specified in the publication
0.02
benzyl N-[3-amino-4-[(O-benzyl-L-tyrosyl)amino]benzoyl]-L-tryptophanate
Homo sapiens
pH and temperature not specified in the publication
0.1
benzyl N-[4-amino-3-(D-norleucylamino)benzoyl]-L-valinate
Homo sapiens
pH and temperature not specified in the publication
0.0016
benzyl N-[4-amino-3-(L-norleucylamino)benzoyl]-L-tryptophanate
Homo sapiens
pH and temperature not specified in the publication
0.04
benzyl N-[4-amino-3-(L-tyrosylamino)benzoyl]-L-tryptophanate
Homo sapiens
pH and temperature not specified in the publication
0.05
benzyl N-[4-amino-3-(L-tyrosylamino)benzoyl]-L-valinate
Homo sapiens
pH and temperature not specified in the publication
0.1
benzyl N-[4-amino-3-[(O-benzyl-L-tyrosyl)amino]benzoyl]-L-tryptophanate
Homo sapiens
pH and temperature not specified in the publication
0.0025
methyl 3-amino-4-(L-arginylamino)benzoate
Homo sapiens
pH and temperature not specified in the publication
0.1
methyl 3-amino-4-(L-leucylamino)benzoate
Homo sapiens
pH and temperature not specified in the publication
0.0011
methyl 3-amino-4-(L-norleucylamino)benzoate
Homo sapiens
pH and temperature not specified in the publication
0.058
methyl 3-amino-4-(L-tyrosylamino)benzoate
Homo sapiens
pH and temperature not specified in the publication
0.058
methyl 3-amino-4-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoate
Homo sapiens
pH and temperature not specified in the publication
0.0037
methyl 4-amino-3-(L-arginylamino)benzoate
Homo sapiens
pH and temperature not specified in the publication
0.0098
methyl 4-amino-3-(L-norleucylamino)benzoate
Homo sapiens
pH and temperature not specified in the publication
0.1
methyl 4-amino-3-(L-tyrosylamino)benzoate
Homo sapiens
pH and temperature not specified in the publication
0.1
methyl N-(3,4-diaminobenzoyl)-L-tyrosinate
Homo sapiens
pH and temperature not specified in the publication
0.0055
methyl N-(3-amino-4-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-tyrosinate
Homo sapiens
pH and temperature not specified in the publication
0.1
methyl N-(4-amino-3-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-tyrosinate
Homo sapiens
pH and temperature not specified in the publication
0.0014
methyl N-[3-amino-4-(L-arginylamino)benzoyl]-L-tyrosinate
Homo sapiens
pH and temperature not specified in the publication
0.000755
methyl N-[3-amino-4-(L-norleucylamino)benzoyl]-L-tyrosinate
Homo sapiens
pH and temperature not specified in the publication
0.015
methyl N-[3-amino-4-(L-tyrosylamino)benzoyl]-L-tyrosinate
Homo sapiens
pH and temperature not specified in the publication
0.016
methyl N-[3-amino-4-[(O-benzyl-L-tyrosyl)amino]benzoyl]-L-tyrosinate
Homo sapiens
pH and temperature not specified in the publication
0.0064
methyl N-[4-amino-3-(D-norleucylamino)benzoyl]-D-tyrosinate
Homo sapiens
pH and temperature not specified in the publication
0.000518
methyl N-[4-amino-3-(L-arginylamino)benzoyl]-D-tyrosinate
Homo sapiens
pH and temperature not specified in the publication
0.039
methyl N-[4-amino-3-(L-tyrosylamino)benzoyl]-L-threoninate
Homo sapiens
pH and temperature not specified in the publication
0.033
methyl N-[4-amino-3-(L-tyrosylamino)benzoyl]-L-tyrosinate
Homo sapiens
pH and temperature not specified in the publication
0.011
methyl N2-(3-amino-4-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-argininate
Homo sapiens
pH and temperature not specified in the publication
0.0048
methyl N2-(4-amino-3-[[(2S)-2-amino-4-(4-hydroxyphenyl)butanoyl]amino]benzoyl)-L-lysinate
Homo sapiens
pH and temperature not specified in the publication
0.0249
methyl N2-(4-amino-3-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-lysinate
Homo sapiens
pH and temperature not specified in the publication
0.011
methyl N2-[3-amino-4-(L-arginylamino)benzoyl]-L-lysinate
Homo sapiens
pH and temperature not specified in the publication
0.03
methyl N2-[3-amino-4-(L-norleucylamino)benzoyl]-L-lysinate
Homo sapiens
pH and temperature not specified in the publication
0.1
methyl N2-[3-amino-4-(L-tyrosylamino)benzoyl]-L-lysinate
Homo sapiens
pH and temperature not specified in the publication
0.017
methyl N2-[4-amino-3-(L-arginylamino)benzoyl]-L-lysinate
Homo sapiens
pH and temperature not specified in the publication
0.052
methyl N2-[4-amino-3-(L-leucylamino)benzoyl]-L-lysinate
Homo sapiens
pH and temperature not specified in the publication
0.0025
methyl N2-[4-amino-3-(L-norleucylamino)benzoyl]-D-argininate
Homo sapiens
pH and temperature not specified in the publication
0.0083
methyl N2-[4-amino-3-(L-norleucylamino)benzoyl]-L-lysinate
Homo sapiens
pH and temperature not specified in the publication
0.013
methyl N2-[4-amino-3-([(2S)-2-amino-4-[4-(benzyloxy)phenyl]butanoyl]amino)benzoyl]-L-lysinate
Homo sapiens
pH and temperature not specified in the publication
0.0019
N-(3,4-diaminobenzoyl)-L-tryptophan
Homo sapiens
pH and temperature not specified in the publication
0.0094
N-(3-amino-4-[[(2S)-2-amino-4-(4-hydroxyphenyl)butanoyl]amino]benzoyl)-L-tryptophan
Homo sapiens
pH and temperature not specified in the publication
0.1
N-(3-amino-4-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-valine
Homo sapiens
pH and temperature not specified in the publication
0.1
N-(4-amino-3-[[(2R)-2-amino-4-(4-hydroxyphenyl)butanoyl]amino]benzoyl)-L-tryptophan
Homo sapiens
pH and temperature not specified in the publication
0.0011
N-[3-amino-4-(L-arginylamino)benzoyl]-L-tryptophan
Homo sapiens
pH and temperature not specified in the publication
0.000237
N-[3-amino-4-(L-norleucylamino)benzoyl]-L-tryptophan
Homo sapiens
pH and temperature not specified in the publication
0.038
N-[3-amino-4-(L-norleucylamino)benzoyl]-L-valine
Homo sapiens
pH and temperature not specified in the publication
0.0048
N-[3-amino-4-(L-tyrosylamino)benzoyl]-L-tryptophan
Homo sapiens
pH and temperature not specified in the publication
0.1
N-[4-amino-3-(D-norleucylamino)benzoyl]-L-valine
Homo sapiens
pH and temperature not specified in the publication
0.000589
N-[4-amino-3-(L-arginylamino)benzoyl]-L-tryptophan
Homo sapiens
pH and temperature not specified in the publication
0.005
N-[4-amino-3-(L-arginylamino)benzoyl]-L-valine
Homo sapiens
pH and temperature not specified in the publication
0.0038
N-[4-amino-3-(L-norleucylamino)benzoyl]-L-tryptophan
Homo sapiens
pH and temperature not specified in the publication
0.1
N-[4-amino-3-(L-tyrosylamino)benzoyl]-L-tryptophan
Homo sapiens
pH and temperature not specified in the publication
0.1
N-[4-amino-3-(L-tyrosylamino)benzoyl]-L-valine
Homo sapiens
pH and temperature not specified in the publication
0.0021
N2-[4-amino-3-(L-leucylamino)benzoyl]-L-lysine
Homo sapiens
pH and temperature not specified in the publication
0.0026
N2-[4-amino-3-(L-phenylalanylamino)benzoyl]-L-lysine
Homo sapiens
pH and temperature not specified in the publication
0.0045
N2-[4-amino-3-(L-tyrosylamino)benzoyl]-L-lysine
Homo sapiens
pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.192
-
purified recombinant enzyme
58
-
substrate L-Leu-amide
additional information
-
233000 mol L-leucine-7-amido-4-methyl coumarin/mol enzyme x min
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10.5
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10.4 - 10.7
-
-
6 - 8
-
almost 70% activity at pH 6.0, 50% activity at pH 8.0
additional information
-
pH profile
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
melanoma cell line
Manually annotated by BRENDA team
melanoma cell line
Manually annotated by BRENDA team
melanoma cell line
Manually annotated by BRENDA team
melanoma cell line
Manually annotated by BRENDA team
melanoma cell line
Manually annotated by BRENDA team
15 EBV-B lymphoblastoid cell lines, overview
Manually annotated by BRENDA team
-
immunohistochemistry analysis of expression levels of LAP3 in breast cancer tissues. Expression of LAP3 in 105 cases of breast cancer is analyzed. The expression rate of LAP3 differs in various pathological histological grades, phenotypes, overview
Manually annotated by BRENDA team
melanoma cell line
Manually annotated by BRENDA team
-
patients with duodenal ulcer. No significant difference of enzyme activity in presence or absence of inflammation
Manually annotated by BRENDA team
15 lymphoblastoid cell lines, overview
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
melanoma cell line
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
melanoma cell line
Manually annotated by BRENDA team
-
IFN-alpha, IFN-beta, or IFN-gamma induce the expression of LAP at the mRNA and protein level. Transfection with the synthetic dsRNA poly(I-C) results in an increase in LAP mRNA levels. Transfection of Huh-7 cells with HCV RNA increases mRNA levels of LAP
Manually annotated by BRENDA team
-
human umbilical vein endothelial cell
Manually annotated by BRENDA team
melanoma cell line
Manually annotated by BRENDA team
melanoma cell line
Manually annotated by BRENDA team
melanoma cell line
Manually annotated by BRENDA team
melanoma cell line
Manually annotated by BRENDA team
melanoma cell line
Manually annotated by BRENDA team
-
enzyme expression during the menstrual cycle, overview
Manually annotated by BRENDA team
melanoma cell line
Manually annotated by BRENDA team
melanoma cell line
Manually annotated by BRENDA team
melanoma cell line
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
-
the enzyme is associated with the proteasome
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ERAP1_HUMAN
941
0
107235
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
-
the molecular mass of PLAP is about 100000 Da after treatment with glycosidases
106000
-
1 * 106000, recombinant enzyme, SDS-PAGE
110000
-
1 * 110000, SDS-PAGE
115000
120000
130000 - 140000
-
the molecular mass of PLAP is about 130000-140000 Da before treatment with glycosidases
268000 - 270000
-
gel filtraton
326000 - 360000
-
non-denaturing PAGE, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
-
3 * ab, a: 53000, b: 65000, SDS-PAGE
monomer
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D375A
-
leukotriene A4 hydrolase mutant
K528A
-
gene A-LAP, site-directed mutagenesis, the mutant enzyme shows reduced activity
K528H
-
gene A-LAP, site-directed mutagenesis, the mutant enzyme shows reduced activity
K528M
-
gene A-LAP, site-directed mutagenesis, the mutant enzyme shows reduced activity
K528R
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 8.5
-
-
95181
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
1 day
4
-
2 weeks
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, 100 mM Tris-HCl buffer, pH 8.0, 6 weeks
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by protein G affinity chromatography
immobilized metal ion affinity chromatography (Ni2+), anion-exchange chromatography
-
recombinant from CHO cells, 5fold to homogeneity
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Sf9 cells using the baculovirus system
a lentivirus is used to induce K-562 cells to overexpress LAP3 (K562-LAP3)
a myc-His-tagged soluble version starting at amino acid position 155 (lacking the putative transmembrane region) expressed in 293F cells
-
expressed in Sf9 cells using the baculovirus system
expression in COS-7 and in CHO cells, secretion from recombinant COS-7 cells
-
from an adipocyte tissue cDNA library
-
genotyping
-
isozyme ERAP1, DNA and amino acid sequence determination and analysis, expression analysis in EBV-B and tumor cell lines, recombinant expression in HeLa cells
isozyme ERAP2, DNA and amino acid sequence determination and analysis, expression analysis in EBV-B and tumor cell lines, recombinant expression in HeLa cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Appel, W.
Aminopeptidasen und Aminosaeurearylamidasen
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
1
987-1015
1974
Bos taurus, Brassica sp., Oryctolagus cuniculus, Homo sapiens, Proteus vulgaris, Rattus norvegicus, Sus scrofa, trout
-
Manually annotated by BRENDA team
Lauffart, B.; McDermott, J.; Gibson, A.; Mantle, D.
Purification and characterization of leucine aminopeptidase from human cerebral cortex
Biochem. Soc. Trans.
16
850-851
1988
Homo sapiens
-
Manually annotated by BRENDA team
Kohno, H.; Kanda, S.; Kanno, T.
Immunoaffininty purification and characterization of leucine aminopeptidase from human liver
J. Biol. Chem.
61
10744-10748
1986
Homo sapiens
Manually annotated by BRENDA team
Kohno, H.; Kanno, T.
Properties and activities of aminopeptidases in normal and mitogen-stimulated human lymphocytes
Biochem. J.
226
59-65
1985
Homo sapiens
Manually annotated by BRENDA team
Harris, C.A.; Hunte, B.; Krauss, M.R.; Taylor, A.; Epstein, L.B.
Induction of leucine aminopeptidase by interferon-gamma
J. Biol. Chem.
267
6865-6869
1992
Homo sapiens
Manually annotated by BRENDA team
Jones, D.D.; Williams, G.; Prochazka, B.
Multiple molecular forms of enzymes hydrolyzing L-leucyl-beta-naphtylamide during gestation
Enzymologia
43
325-332
1972
Homo sapiens
-
Manually annotated by BRENDA team
Kumagai, Y.; Watanabe, Y.; Fujimoto, Y.
Purification and characterization of leucine-specific aminopeptidase from the soluble fraction of human placenta
Biochem. Med. Metab. Biol.
46
110-118
1991
Homo sapiens
Manually annotated by BRENDA team
Gibson, A.M.; Biggins, J.A.; Lauffart, B.; Mantle, D.; McDermott, J.R.
Human brain leucyl aminopeptidase: Isolation, characterization and specificity against some neuropeptide
Neuropeptides
19
163-168
1991
Homo sapiens
Manually annotated by BRENDA team
Hattori, A.; Kitatani, K.; Matsumoto, H.; Miyazawa, S.; Rogi, T.; Tsuruoka, N.; Mizutani, S.; Natori, Y.; Tsujimoto, M.
Characterization of recombinant human adipocyte-derived leucine aminopeptidase expressed in chinese hamster ovary cells
J. Biochem.
128
755-762
2000
Homo sapiens
Manually annotated by BRENDA team
Mitsui, T.; Nomura, S.; Itakura, A.; Mizutani, S.
Role of aminopeptidases in the blood pressure regulation
Biol. Pharm. Bull.
27
768-771
2004
Homo sapiens
Manually annotated by BRENDA team
Hattori, A.; Tsujimoto, M.
Processing of antigenic peptides by aminopeptidases
Biol. Pharm. Bull.
27
777-780
2004
Homo sapiens
Manually annotated by BRENDA team
Goto, Y.; Hattori, A.; Ishii, Y.; Tsujimoto, M.
Reduced activity of the hypertension-associated Lys528Arg mutant of human adipocyte-derived leucine aminopeptidase (A-LAP)/ER-aminopeptidase-1
FEBS Lett.
580
1833-1838
2006
Homo sapiens
Manually annotated by BRENDA team
Harata, T.; Ando, H.; Iwase, A.; Nagasaka, T.; Mizutani, S.; Kikkawa, F.
Localization of angiotensin II, the AT1 receptor, angiotensin-converting enzyme, aminopeptidase A, adipocyte-derived leucine aminopeptidase, and vascular endothelial growth factor in the human ovary throughout the menstrual cycle
Fertil. Steril.
86
433-439
2006
Homo sapiens
Manually annotated by BRENDA team
Straeter, N.; Lipscomb, W.N.
Leucyl aminopeptidase (animal)
Handbook of Proteolytic Enzymes (2nd Edition)
1
896-901
2004
Bos taurus, Homo sapiens, Sus scrofa
-
Manually annotated by BRENDA team
Fruci, D.; Ferracuti, S.; Limongi, M.Z.; Cunsolo, V.; Giorda, E.; Fraioli, R.; Sibilio, L.; Carroll, O.; Hattori, A.; Van Endert, P.M.; Giacomini, P.
Expression of endoplasmic reticulum aminopeptidases in EBV-B cell lines from healthy donors and in leukemia/lymphoma, carcinoma, and melanoma cell lines
J. Immunol.
176
4869-4879
2006
Homo sapiens, Homo sapiens (Q6P179)
Manually annotated by BRENDA team
Fernandes, V.L.; Bhasin, D.K.; Rana, S.V.
Study of enzyme activities in the descending part of the duodenum in patients of duodenal ulcer
Indian J. Clin. Biochem.
21(1)
169-172
2006
Homo sapiens
Manually annotated by BRENDA team
Shin, E.; Seifert, U.; Urban, S.; Truong, K.; Feinstone, S.M.; Rice, C.M.; Kloetzel, P.; Rehermann, B.
Proteasome activator and antigen-processing aminopeptidases are regulated by virus-induced type I interferon in the hepatitis C virus-infected liver
J. Interferon Cytokine Res.
27
985-990
2008
Homo sapiens, Pan troglodytes
Manually annotated by BRENDA team
Tholander, F.; Haeggstroem, J.Z.
Assay for rapid analysis of the tri-peptidase activity of LTA4 hydrolase
Proteins
67
1113-1118
2007
Homo sapiens
Manually annotated by BRENDA team
Kawai, M.; Araragi, K.; Shimizu, Y.; Hara, Y.
Identification of placental leucine aminopeptidase and triton-slowed aminopeptidase N in serum of pregnant women
Clin. Chim. Acta
400
37-41
2009
Homo sapiens
Manually annotated by BRENDA team
Alasbahi, R.; Melzig, M.F.
Screening of some Yemeni medicinal plants for inhibitory activity against peptidases
Pharmazie
63
86-88
2008
Homo sapiens
Manually annotated by BRENDA team
Georgiadou, D.; Hearn, A.; Evnouchidou, I.; Chroni, A.; Leondiadis, L.; York, I.A.; Rock, K.L.; Stratikos, E.
Placental leucine aminopeptidase efficiently generates mature antigenic peptides in vitro but in patterns distinct from endoplasmic reticulum aminopeptidase 1
J. Immunol.
185
1584-1592
2010
Homo sapiens
Manually annotated by BRENDA team
Papakyriakou, A.; Zervoudi, E.; Tsoukalidou, S.; Mauvais, F.X.; Sfyroera, G.; Mastellos, D.C.; van Endert, P.; Theodorakis, E.A.; Vourloumis, D.; Stratikos, E.
3,4-diaminobenzoic acid derivatives as inhibitors of the oxytocinase subfamily of m1 aminopeptidases with immune-regulating properties
J. Med. Chem.
58
1524-1543
2015
Homo sapiens (Q6P179), Homo sapiens (Q9NZ08), Homo sapiens
Manually annotated by BRENDA team
Park, H.; Shim, J.S.; Kim, B.S.; Jung, H.J.; Huh, T.L.; Kwon, H.J.
Purpurin inhibits adipocyte-derived leucine aminopeptidase and angiogenesis in a zebrafish model
Biochem. Biophys. Res. Commun.
450
561-567
2014
Danio rerio, Homo sapiens
Manually annotated by BRENDA team
Wu, H.; Jiang, W.; Li, B.; Yang, H.; Zhao, X.; Zhang, H.; Wang, S.; Peng, L.; Wang, L.; Wang, X.; Dai, G.; Fang, C.
A new method to evaluate the enzyme-suppressing activity of a leucine aminopeptidase 3 inhibitor
Drug Discov. Ther.
13
17-21
2019
Homo sapiens (P28838), Homo sapiens
Manually annotated by BRENDA team
Fang, C.; Zhang, J.; Yang, H.; Peng, L.; Wang, K.; Wang, Y.; Zhao, X.; Liu, H.; Dou, C.; Shi, L.; Zhao, C.; Liang, S.; Li, D.; Wang, X.
Leucine aminopeptidase 3 promotes migration and invasion of breast cancer cells through upregulation of fascin and matrix metalloproteinases-2/9 expression
J. Cell. Biochem.
120
3611-3620
2019
Homo sapiens
Manually annotated by BRENDA team