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Information on EC 3.4.11.2 - membrane alanyl aminopeptidase and Organism(s) Homo sapiens and UniProt Accession P15144

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.11 Aminopeptidases
                3.4.11.2 membrane alanyl aminopeptidase
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Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: P15144 not found.
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Release of an N-terminal amino acid, Xaa-/-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide
Synonyms
aminopeptidase, aminopeptidase n, dipeptidase, aminopeptidase m, alanine aminopeptidase, apn/cd13, gp150, aminopeptidase-n, anpep, alanyl aminopeptidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alanine aminopeptidase
-
aminopeptidase N
-
alanine aminopeptidase
alanine-specific aminopeptidase
-
-
-
-
alanyl aminopeptidase
alanyl-aminopeptidase
-
-
Alpha-aminoacylpeptide hydrolase
-
-
-
-
amino-oligopeptidase
-
-
-
-
aminopeptidase M
aminopeptidase M II
-
-
-
-
aminopeptidase N
aminopeptidase N/CD13
-
-
aminopeptidase, microsomal
-
-
-
-
aminopeptidase-N
-
-
AP-N
-
-
APN/CD13
-
-
APN1
-
-
-
-
APN2
-
-
-
-
CryIA(C) receptor
-
-
-
-
GP 130
-
-
-
-
GP150
L-alanine aminopeptidase
-
-
-
-
leucine aminopeptidase
-
Leukemia antigen CD13
-
-
-
-
Lys-AP
-
-
-
-
Lysyl aminopeptidase
-
-
-
-
membrane alanyl-aminopeptidase
-
-
Membrane glycoprotein H11
-
-
-
-
Membrane protein p161
-
-
-
-
Microsomal aminopeptidase
microsomal leucine aminopeptidase
-
Myeloid plasma membrane glycoprotein CD13
-
-
-
-
neutral aminopeptidase
-
-
p146
-
-
p161
-
-
particle-bound aminopeptidase
additional information
-
the enzyme belongs to the peptidase family M1
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
PATHWAY SOURCE
PATHWAYS
CAS REGISTRY NUMBER
COMMENTARY hide
9054-63-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-alanine beta-naphthylamide + H2O
L-alanine + beta-naphthylamine
show the reaction diagram
-
-
-
?
9-(L-leucylamino)-5H-benzo[a]phenoxazin-5-iminium + H2O
9-amino-5H-benzo[a]phenoxazin-5-iminium + L-leucine
show the reaction diagram
the substrate displays high selectivity for LAP over various other substances (including biothiols and co-existing enzymes) at their physiological concentrations. It is an excellent specific substrate for enzyme LAP
-
-
ir
Ala-2-naphthylamide + H2O
Ala + 2-naphthylamine
show the reaction diagram
Ala-4-nitroanilide + H2O
Ala + 4-nitroaniline
show the reaction diagram
-
-
-
?
aminoacyl peptide
?
show the reaction diagram
-
-
-
-
?
aminoacyl-2-naphthylamide + H2O
amino acid + 2-naphthylamine
show the reaction diagram
aminoacyl-4-methylcoumarin 7-amide + H2O
amino acid + 7-amino-4-methylcoumarin
show the reaction diagram
-
Ala-, Met-, Tyr-, Leu-, Phe-, Arg-, Lys-, Gly-, Lys-Ala-, Arg-Arg- derivatives, not: Pro-, Pyr-, Gly-Pro-derivatives
-
?
aminoacyl-p-nitroanilide + H2O
amino acid + nitroaniline
show the reaction diagram
-
-
-
?
angiotensin III + H2O
angiotensin IV + Arg
show the reaction diagram
angiotensin III + H2O
angiotensin IV + L-Arg
show the reaction diagram
-
-
-
-
?
bradykinin + H2O
?
show the reaction diagram
-
-
-
-
?
Cys-Gly + H2O
Cys + Gly
show the reaction diagram
-
-
-
-
?
enkephalin + H2O
?
show the reaction diagram
-
hydrolysis of the Tyr1-Gly2 bond
-
-
?
entactin + H2O
?
show the reaction diagram
-
-
-
-
?
Glu-Ala-Ala-4-methoxynaphthylamide + H2O
?
show the reaction diagram
-
-
-
-
?
Gly-4-nitroanilide + H2O
Gly + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
interleukin-8 + H2O
?
show the reaction diagram
-
-
-
-
?
kallidin + H2O
?
show the reaction diagram
-
-
-
-
?
L-Ala-2-naphthylamide + H2O
L-Ala + 2-naphthylamine
show the reaction diagram
-
-
-
-
?
L-Ala-4-nitroanilide + H2O
L-Ala + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
L-Ala-7-amido-4-methylcoumarin + H2O
L-Ala + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
L-Ala-p-nitroanilide + H2O
L-Ala + p-nitroaniline
show the reaction diagram
-
-
-
-
?
L-alaninyl 4-methoxy-2-naphthylamide + H2O
L-alanine + 4-methoxy-2-naphthylamine
show the reaction diagram
-
-
-
?
L-Arg-2-naphthylamide + H2O
L-Arg + 2-naphthylamine
show the reaction diagram
-
-
-
-
?
L-Asn-2-naphthylamide + H2O
L-Asn + 2-naphthylamine
show the reaction diagram
-
-
-
-
?
L-Cys-Gly + H2O
L-Cys + Gly
show the reaction diagram
-
-
-
-
?
L-Gln-2-naphthylamide + H2O
L-Gln + 2-naphthylamine
show the reaction diagram
-
-
-
-
?
L-Glu-2-naphthylamide + H2O
L-Glu + 2-naphthylamine
show the reaction diagram
-
-
-
-
?
L-His-2-naphthylamide + H2O
L-His + 2-naphthylamine
show the reaction diagram
-
-
-
-
?
L-Ile-2-naphthylamide + H2O
L-Ile + 2-naphthylamine
show the reaction diagram
-
-
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroanilide
show the reaction diagram
-
-
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
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-Lys-2-naphthylamide + H2O
L-Lys + 2-naphthylamine
show the reaction diagram
-
-
-
-
?
L-Lys-L-Lys-[Hyp3, CpG5, D-Tic7, CpG8]des-Arg9-bradykinin + H2O
?
show the reaction diagram
-
i.e.B-9958
-
-
?
L-Met-2-naphthylamide + H2O
L-Met + 2-naphthylamine
show the reaction diagram
-
-
-
-
?
L-Phe-2-naphthylamide + H2O
L-Phe + 2-naphthylamine
show the reaction diagram
-
-
-
-
?
L-Thr-2-naphthylamide + H2O
L-Thr + 2-naphthylamine
show the reaction diagram
-
-
-
-
?
L-Tyr-2-naphthylamide + H2O
L-Tyr + 2-naphthylamine
show the reaction diagram
-
-
-
-
?
L-Val-2-naphthylamide + H2O
L-Val + 2-naphthylamine
show the reaction diagram
-
-
-
-
?
Leu-2-naphthylamide + H2O
Leu + 2-naphthylamine
show the reaction diagram
Leu-enkephalin + H2O
Leu + enkephalin
show the reaction diagram
-
-
-
-
?
Leu-enkephalin-L-Tyr-Gly + H2O
Leu + enkephalin-L-Tyr-Gly
show the reaction diagram
-
-
-
-
?
Lys-des-Arg9-bradykinin + H2O
?
show the reaction diagram
-
-
-
-
?
lysyl-bradykinin + H2O
?
show the reaction diagram
-
-
-
-
?
Met-enkephalin + H2O
Met + enkephalin
show the reaction diagram
-
-
-
-
?
Met-enkephalin-L-Tyr-Gly + H2O
Met + enkephalin L-Tyr-Gly
show the reaction diagram
-
-
-
-
?
Met-Lys-bradykinin + H2O
Met + Lys + bradykinin
show the reaction diagram
-
-
-
-
?
monocyte chemotactic protein MCP-1 + H2O
?
show the reaction diagram
-
-
-
-
?
Mr 160000 component
?
show the reaction diagram
-
Mr 160000 component of basement membrane, aminopeptidase N plays role in melanoma invasion of basement membrane
-
-
?
N-formyl-Met-Leu-Phe + H2O
?
show the reaction diagram
-
-
-
-
?
Neurokinin A + H2O
?
show the reaction diagram
-
-
-
-
?
Ser-beta-naphthylamide + H2O
Ser + beta-naphthylamine
show the reaction diagram
-
-
-
-
?
somatostatin + H2O
?
show the reaction diagram
-
-
-
-
?
spinorphin + H2O
?
show the reaction diagram
-
-
-
-
?
Substance P + H2O
?
show the reaction diagram
-
-
-
-
?
thymopentin + H2O
?
show the reaction diagram
-
-
-
-
?
tuftsin + H2O
?
show the reaction diagram
Type IV collagen + 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
aminoacyl peptide
?
show the reaction diagram
-
-
-
-
?
angiotensin III + H2O
angiotensin IV + Arg
show the reaction diagram
-
the enzyme is involved in regulation of blood pressure in the renin-angiotensin system in the brain causing hypertension, the enzyme is involved in metabolism of angiotensin II and angiotensin III in the brain, overview
-
-
ir
bradykinin + H2O
?
show the reaction diagram
-
-
-
-
?
interleukin-8 + H2O
?
show the reaction diagram
-
-
-
-
?
kallidin + H2O
?
show the reaction diagram
-
-
-
-
?
Leu-enkephalin + H2O
Leu + enkephalin
show the reaction diagram
-
-
-
-
?
Met-enkephalin + H2O
Met + enkephalin
show the reaction diagram
-
-
-
-
?
Met-Lys-bradykinin + H2O
Met + Lys + bradykinin
show the reaction diagram
-
-
-
-
?
monocyte chemotactic protein MCP-1 + H2O
?
show the reaction diagram
-
-
-
-
?
Mr 160000 component
?
show the reaction diagram
-
Mr 160000 component of basement membrane, aminopeptidase N plays role in melanoma invasion of basement membrane
-
-
?
N-formyl-Met-Leu-Phe + H2O
?
show the reaction diagram
-
-
-
-
?
Neurokinin A + H2O
?
show the reaction diagram
-
-
-
-
?
somatostatin + H2O
?
show the reaction diagram
-
-
-
-
?
spinorphin + H2O
?
show the reaction diagram
-
-
-
-
?
Substance P + H2O
?
show the reaction diagram
-
-
-
-
?
thymopentin + H2O
?
show the reaction diagram
-
-
-
-
?
tuftsin + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
increase of activity
Ni2+
-
reactivation after inhibition by EDTA
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(1-amino-2-anilinoethyl)phosphonic acid
-
(1-amino-2-[[(4-methoxyphenyl)methyl]amino]ethyl)phosphonic acid
-
[1-amino-2-(cyclohexylamino)ethyl]phosphonic acid
-
(+)-4-hydroxypanduratin A
-
54.8% inhibition at 0.03 mM
(+)-isopanduratin A
-
29.3% inhibition at 0.03 mM
(+)-krachaizin A
-
27.9% inhibition at 0.03 mM
(+)-krachaizin B
-
76.2% inhibition at 0.03 mM
(+)-panduratin A
-
61.4% inhibition at 0.03 mM
(-)-4-hydroxypanduratin A
-
39.6% inhibition at 0.03 mM
(-)-isopanduratin A
-
95.3% inhibition at 0.03 mM
(-)-krachaizin A
-
21.7% inhibition at 0.03 mM
(-)-krachaizin B
-
51.0% inhibition at 0.03 mM
(-)-panduratin A
-
95.2% inhibition at 0.03 mM
(1-amino-2-cyclohexylethyl)phosphonic acid
-
-
(1-amino-2-cyclopentylethyl)phosphonic acid
-
-
(1-amino-2-methylpropyl)(1-hydroxy-3-phenylpropyl)phosphinic acid
-
-
(1-amino-2-phenylethyl)(1-hydroxy-3-phenylpropyl)phosphinic acid
-
-
(1-amino-3-cyclohexylpropyl)phosphonic acid
-
-
(1-amino-3-cyclopentylpropyl)phosphonic acid
-
-
(1-amino-3-methylbutyl)(1-hydroxy-3-phenylpropyl)phosphinic acid
-
-
(1-amino-3-methylbutyl)(1-hydroxypentyl)phosphinic acid
-
-
(1-amino-3-methylbutyl)(2-benzyl-3-oxo-3-phenylpropyl)phosphinic acid
-
-
(1-amino-3-methylbutyl)phosphinic acid
-
-
(1-amino-3-methylbutyl)[amino(phenyl)methyl]phosphinic acid
-
-
(1-amino-3-phenylbutyl)phosphonic acid
-
-
(1-amino-3-phenylpropyl)(2-benzyl-3-oxo-3-phenylpropyl)phosphinic acid
-
-
(1-amino-3-phenylpropyl)phosphinic acid
-
-
(1-amino-4-cyclohexylbutyl)phosphonic acid
-
-
(1-amino-5-phenylpentyl)phosphonic acid
-
-
(1-aminobutyl)(1-amino-3-methylbutyl)phosphinic acid
-
-
(1-aminobutyl)(1-hydroxy-2-phenylethyl)phosphinic acid
-
-
(1-aminobutyl)[amino(phenyl)methyl]phosphinic acid
-
-
(1-aminoethyl)(1-amino-3-methylbutyl)phosphinic acid
-
-
(1-aminoethyl)(2-benzyl-3-oxo-3-phenylpropyl)phosphinic acid
-
-
(1-aminoethyl)[amino(phenyl)methyl]phosphinic acid
-
-
(1-aminoethyl)[hydroxy[4-(propan-2-yl)phenyl]methyl]phosphinic acid
-
-
(1-aminohexyl)((2-(methoxycarbonyl)benzyl)carbamothioyl)phosphinic acid
-
-
(1-aminopentyl)(1-hydroxy-2-phenylpropyl)phosphinic acid
-
-
(1-aminopentyl)(1-hydroxy-3-phenylpropyl)phosphinic acid
-
-
(1-aminopentyl)[hydroxy(4-hydroxyphenyl)methyl]phosphinic acid
-
-
(1-aminopropyl)(1-hydroxy-3-phenylpropyl)phosphinic acid
-
-
(1-benzyl-1H-imidazol-4-yl)methyl 6-oxidanyl-6-oxidanylidene-N-[(3,4,5-trimethoxyphenyl)carbonyl]-L-norleucylalaninate
-
-
(1S)-1-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)ethanaminium acetate
-
IC50: 70 nM
(1S)-2-phenyl-1-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)ethanaminium acetate
-
IC50: 50 nM
(1S)-3-methyl-1-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)butan-1-aminium acetate
-
IC50: 74 nM
(2E)-3-[(1-aminoethyl)(hydroxy)phosphoryl]-2-methylprop-2-enoic acid
-
-
(2R)-N-[5-(4-bromophenyl)-1,3,4-thiadiazol-2-yl]-2-[(benzoyl)amino]-propanamide
-
-
(2R)-N-[5-(4-bromophenyl)-1,3,4-thiadiazol-2-yl]-2-[(phenylacetyl)-amino]-propanamide
-
-
(2R)-N-[5-(4-bromophenyl)-1,3,4-thiadiazol-2-yl]-2-[(phenylsulfonyl)-amino]-propanamide
-
-
(2R)-N-[5-(4-chlorophenyl)-1,3,4-thiadiazol-2-yl]-2-[(benzoyl)amino]-propanamide
-
-
(2R)-N-[5-(4-chlorophenyl)-1,3,4-thiadiazol-2-yl]-2-[(phenylacetyl)-amino]-propanamide
-
-
(2R)-N-[5-(4-chlorophenyl)-1,3,4-thiadiazol-2-yl]-2-[(phenylsulfonyl)-amino]-propanamide
-
-
(2R)-N-[5-(4-fluorophenyl)-1,3,4-thiadiazol-2-yl]-2-[(benzoyl)amino]-propanamide
-
-
(2R)-N-[5-(4-fluorophenyl)-1,3,4-thiadiazol-2-yl]-2-[(phenylacetyl)-amino]-propanamide
-
-
(2R)-N-[5-(4-fluorophenyl)-1,3,4-thiadiazol-2-yl]-2-[(phenylsulfonyl)amino]-propanamide
-
-
(2R)-N-[5-(4-methoxyphenyl)-1,3,4-thiadiazol-2-yl]-2-[(benzoyl)amino]-propanamide
-
-
(2R)-N-[5-(4-methoxyphenyl)-1,3,4-thiadiazol-2-yl]-2-[(phenylacetyl)-amino]-propanamide
-
-
(2R)-N-[5-(4-methoxyphenyl)-1,3,4-thiadiazol-2-yl]-2-[(phenylsulfonyl)amino]-propanamide
-
-
(2R)-N-[5-(4-methylphenyl)-1,3,4-thiadiazol-2-yl]-2-[(benzoyl)amino]-propanamide
-
-
(2R)-N-[5-(4-methylphenyl)-1,3,4-thiadiazol-2-yl]-2-[(phenylacetyl)-amino]-propanamide
-
-
(2R)-N-[5-(4-methylphenyl)-1,3,4-thiadiazol-2-yl]-2-[(phenylsulfonyl)-amino]-propanamide
-
-
(2R)-N-[5-(4-nitrorophenyl)-1,3,4-thiadiazol-2-yl]-2-[(benzoyl)amino]-propanamide
-
-
(2R)-N-[5-(4-nitrorophenyl)-1,3,4-thiadiazol-2-yl]-2-[(phenylacetyl)-amino]-propanamide
-
-
(2R)-N-[5-(4-nitrorophenyl)-1,3,4-thiadiazol-2-yl]-2-[(phenylsulfonyl)-amino]-propanamide
-
-
(2R)-N-[5-phenyl-1,3,4-thiadiazol-2-yl]-2-[(benzoyl)-amino]-propanamide
-
-
(2R)-N-[5-phenyl-1,3,4-thiadiazol-2-yl]-2-[(phenylacetyl)amino]-propanamide
-
-
(2R)-N-[5-phenyl-1,3,4-thiadiazol-2-yl]-2-[(phenylsulfonyl)amino]-propanamide
-
-
(2S)-2-amino-N-[(3S)-1-[2-(hydroxyamino)-2-oxoethyl]-2,6-dioxopiperidin-3-yl]-3-phenylpropanamide
-
-
(2S,3R)-3-amino-2-hydroxy-4-phenyl-N-1,3-thiazol-2-ylbutanamide
-
-
(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl-L-valine
-
-
(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl-L-valyl-L-prolyl-(trans-4-hydroxy-L-proline)
-
i.e. MR387A
(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl-L-valyl-L-prolyl-L-proline
-
i.e. MR378B
(2S,3R)-3-amino-2-hydroxy-N-1H-imidazo[4,5-c]pyridin-4-yl-4-phenylbutanamide
-
-
(2S,3R)-3-amino-N-(2,6-dihydroxypyrimidin-4-yl)-2-hydroxy-4-phenylbutanamide
-
-
(2S,3R)-3-amino-N-(5-amino-1,3-thiazol-2-yl)-2-hydroxy-4-phenylbutanamide
-
-
(2S,3R)-3-amino-N-1,3-benzothiazol-2-yl-2-hydroxy-4-phenylbutanamide
-
-
(2Z)-3-amino-3,4-dihydronaphthalen-2(1H)-one O-(2-phenylethyl)oxime hydrochloride
-
-
(2Z)-3-amino-3,4-dihydronaphthalen-2(1H)-one O-(3-phenylpropyl)oxime hydrochloride
-
-
(2Z)-3-amino-3,4-dihydronaphthalen-2(1H)-one O-(4-phenylbutyl)oxime hydrochloride
-
-
(2Z)-3-amino-3,4-dihydronaphthalen-2(1H)-one O-benzyloxime hydrochloride
-
-
(2Z)-3-amino-3,4-dihydronaphthalen-2(1H)-one O-methyloxime hydrochloride
-
-
(2Z)-3-amino-3,4-dihydronaphthalen-2(1H)-one oxime hydrochloride
-
-
(3S)-3-(D-alanylamino)-2-([[(1S)-1-aminoethyl][(3r)-tricyclo[3.3.1.13,7]dec-1-yloxy]phosphoryl]methyl)-5-methylhexanoic acid
-
-
(3S)-N-hydroxy-2-(phenylsulfonyl)-6,10-dioxa-2-azaspiro[4.5]decane-3-carboxamide
-
-
(3S)-N-hydroxy-2-(phenylsulfonyl)-6,11-dioxa-2-azaspiro[4.6]undecane-3-carboxamide
-
-
(3S)-N-hydroxy-2-(phenylsulfonyl)-6,12-dioxa-2-azaspiro[4.7]dodecane-3-carboxamide
-
-
(3S)-N-hydroxy-2-[(4-methylphenyl)sulfonyl]-6,10-dioxa-2-azaspiro[4.5]decane-3-carboxamide
-
-
(3S)-N-hydroxy-2-[(4-methylphenyl)sulfonyl]-6,11-dioxa-2-azaspiro[4.6]undecane-3-carboxamide
-
-
(3S)-N-hydroxy-2-[(4-methylphenyl)sulfonyl]-6,12-dioxa-2-azaspiro[4.7]dodecane-3-carboxamide
-
-
(4R)-4-(hexanoylamino)-N-hydroxy-1-[(3,4,5-trimethoxyphenyl)carbonyl]-L-prolinamide
(4R)-4-([(2E)-3-(3,4-dimethoxyphenyl)prop-2-enoyl]amino)-N-hydroxy-1-[(3,4,5-trimethoxyphenyl)carbonyl]-L-prolinamide
-
IC50: 2.1 nM
(4R)-4-[[(2E)-3-(3,4-dimethoxyphenyl)prop-2-enoyl]amino]-N-hydroxy-1-[(3,4,5-trimethoxyphenyl)carbonyl]-L-prolinamide
-
-
(aminomethyl)(1-amino-3-methylbutyl)phosphinic acid
-
-
(aminomethyl)[amino(phenyl)methyl]phosphinic acid
-
-
(S)-2-amino-N-((S)-1-(2-(hydroxyamino)-2-oxoethyl)-2,6-dioxopiperidin-3-yl)-3-phenylpropanamide
-
displays a substantial potential inhibitory effect on APN/CD13 activity more potently than bestatin. In the concentration range of 0.0008-0.5 mM, the mean optical density of APN/CD13 activity is reduced by 30%, 53.1%, 63.1%, 68.5%, and 70.8%, respectively, for a 30 min exposure and 37.2%, 56.7%, 66.5%, 73.8%, and 76.2%, respectively, for a 60 min exposure
1,10-phenanthroline
1,2,3,4-tetrahydronaphthalen-2-amine hydrochloride
-
-
1,4-dihydro-3H-isochromen-3-one
-
-
1,4-dihydro-3H-isothiochromen-3-one
-
-
1-(3-amino-1,2,3,4-tetrahydronaphthalen-2-yl)ethanone hydrochloride
-
-
1-amino-2-methylpropyl(benzylcarbamoyl)phosphinic acid
-
-
1-amino-2-methylpropyl(hexylcarbamothioyl)phosphinic acid
-
-
1-amino-2-methylpropyl(isobutylcarbamothioyl)phosphinic acid
-
-
1-amino-2-methylpropyl(methylcarbamothioyl)phosphinic acid
-
-
1-amino-2-methylpropyl(phenylcarbamoyl)phosphinic acid
-
-
1-amino-3-methylbutyl(2-(methoxycarbonyl)benzylcarbamothioyl)phosphinic acid
-
-
1-amino-3-methylbutyl(benzylcarbamothioyl)phosphinic acid
-
-
1-amino-3-methylbutyl(hexylcarbamothioyl)phosphinic acid
-
-
1-amino-3-methylbutyl(methylcarbamothioyl)phosphinic acid
-
-
1-amino-3-methylbutyl(phenethylcarbamothioyl)phosphinic acid
-
-
1-amino-3-phenylpropyl(3-(methylthio)propylcarbamothioyl)phosphinic acid
-
-
1-amino-3-phenylpropyl(4-(ethoxycarbonyl)benzylcarbamothioyl)phosphinic acid
-
-
1-amino-3-phenylpropyl(4-methoxybenzylcarbamothioyl)phosphinic acid
-
-
1-amino-3-phenylpropyl(benzylcarbamothioyl)phosphinic acid
-
-
1-amino-3-phenylpropyl(propylcarbamothioyl)phosphinic acid
-
-
1-amino-4-methylpentyl(benzylcarbamoyl)phosphinic acid
-
-
1-amino-4-methylpentyl(phenylcarbamoyl)phosphinic acid
-
-
1-aminobutyl(2-(methoxycarbonyl)phenethylcarbamothioyl)phosphinic acid
-
-
1-aminobutyl(3-(methylthio)propylcarbamothioyl)phosphinic acid
-
-
1-aminobutyl(4-(ethoxycarbonyl)phenethylcarbamothioyl)phosphinic acid
-
-
1-aminobutyl(4-methoxybenzylcarbamothioyl)phosphinic acid
-
-
1-aminobutyl(4-methoxyphenethylcarbamothioyl)phosphinic acid
-
-
1-aminobutyl(benzylcarbamothioyl)phosphinic acid
-
-
1-aminobutyl(phenethylcarbamothioyl)phosphinic acid
-
-
1-aminoethyl(3-(methylthio)propylcarbamothioyl)phosphinic acid
-
-
1-aminoethyl(4-(ethoxycarbonyl)benzylcarbamothioyl)phosphinic acid
-
-
1-aminoethyl(4-methoxybenzylcarbamothioyl)phosphinic acid
-
-
1-aminoethyl(benzylcarbamothioyl)phosphinic acid
-
-
1-aminoethyl(phenethylcarbamothioyl)phosphinic acid
-
-
1-aminopentyl(2-(methoxycarbonyl)benzylcarbamothioyl)phosphinic acid
-
-
1-aminopentyl(3-(methylthio)propylcarbamothioyl)phosphinic acid
-
-
1-aminopentyl(4-methoxybenzylcarbamothioyl)phosphinic acid
-
-
1-aminopentyl(benzylcarbamothioyl)phosphinic acid
-
-
1-aminopentyl(phenethylcarbamothioyl)phosphinic acid
-
-
1-aminopropyl(3-(methylthio)propylcarbamothioyl)phosphinic acid
-
-
1-methyl cyclohexan bestatin
-
i.e. BE15, strong inhibition
2',3-dinitro-3'-methoxy-flavone-8-acetic acid
-
75% inhibition at 1 mM
2',3-dinitro-5'-methoxy-flavone-8-acetic acid
-
80% inhibition at 1 mM
2',3-dinitroflavone-8-acetic acid
2'-nitro-flavone-8-acetic acid
-
highly cytotoxic, 83% inhibition at 1 mM
2(S)-amino-5-methylpentanal
-
-
2,2'-bipyridine
-
90% inhibition at 5 mM
2,4-dihydroxy-6-phenethylbenzoic acid methyl ester
-
22.8% inhibition at 0.03 mM
2,6-dihydroxy-4-methoxydihydrochalcone
-
14.8% inhibition at 0.03 mM
2-(1-ethylcyclopentyl)ethanamine-CO-Tyr-Ile-His-Pro-Phe-OH
-
low potency inhibitor
2-([[(3S)-2,6-dioxo-3-[[(3,4,5-trimethoxyphenyl)carbonyl]amino]piperidin-1-yl]acetyl]amino)propaneperoxoic acid
-
-
2-amino-1,4-dihydroisoquinolin-3(2H)-one
-
-
2-amino-1,4-dihydrophenanthren-3(2H)-one hydrochloride
-
-
2-amino-2-phenylethanethiol
-
IC50: 25 nM
2-amino-3-(benzyloxy)propane-1-thiol
-
IC50: 56 nM
2-amino-3-(methylsulfanyl)propane-1-thiol
-
IC50: 20 nM
2-amino-3-(methylsulfinyl)propane-1-thiol
-
IC50: 21 nM
2-amino-3-(tert-butylsulfanyl)propane-1-thiol
-
IC50: 40 nM
2-amino-3-cyclohexylpropane-1-thiol
-
IC50: 45 nM
2-amino-3-phenylpropane-1-thiol
-
IC50: 30 nM
2-amino-4-(methylsulfanyl)butane-1-thiol
-
IC50: 11 nM
2-amino-4-(methylsulfinyl)butane-1-thiol
-
IC50: 20 nM
2-amino-4-methylpentane-1-thiol
-
IC50: 22 nM
2-hydroxy-1,4-dihydroisoquinolin-3(2H)-one
-
-
2-mercaptoethane sulfonic acid
-
80% residual activity at 10 mM
2-[[(1-amino-3-methylbutyl)(hydroxy)phosphoryl]amino]-4-methylpentanoic acid
-
-
2-[[(1-amino-3-methylbutyl)(hydroxy)phosphoryl]methyl]-4-methylpentanoic acid
-
-
2-[[(1-amino-3-phenylpropyl)(hydroxy)phosphoryl]methyl]-4-methylpentanoic acid
-
-
2-{[(1-aminoethyl)(hydroxy)phosphoryl]methyl}decanoic acid
-
-
3,3'-dinitro-4'-methoxy-flavone-8-acetic acid
-
61% inhibition at 1 mM
3,3'-dinitroflavone-8-acetic acid
-
44% inhibition at 1 mM
3,4'-dinitroflavone-8-acetic acid
-
63% inhibition at 1 mM
3,4-dihydronaphthalen-2(1H)-one
-
-
3-(hydroperoxy(hydroxy)phosphino)-1,2,3,4-tetrahydronaphthalen-2-amine
-
-
3-amino-1-(2-phenylethyl)-3,4-dihydronaphthalen-2(1H)-one hydrochloride
-
-
3-amino-1-hydroxypropan-2-one derivatives
-
-
-
3-amino-2-(2-hydroxyphenyl)-4-oxo-4H-1-benzopyran-8-acetic acid methoxymethyl ester
-
highly cytotoxic, 19% inhibition at 1 mM
3-amino-2-hydroxypropionaldehyde derivatives
-
-
-
3-amino-2-tetralone derivatives
-
-
3-amino-2-tetralones
-
-
3-amino-3,4-dihydroquinolin-2(1H)-one hydrochloride
-
-
3-amino-flavone-8-acetic acid
-
33% inhibition at 1 mM
3-amino-N-hydroxy-1,2,3,4-tetrahydronaphthalene-2-carboxamide hydrochloride
-
-
3-nitro-2'-benzyloxy-flavone-8-acetic acid
-
cytotoxic, 76% inhibition at 1 mM
3-nitro-2'-carboxybenzyl-flavone-8-acetic acid
-
cytotoxic, 77% inhibition at 1 mM
3-nitro-2'-carboxymethyl-flavone-8-acetic acid
-
slightly cytotoxic, 66% inhibition at 1 mM
3-nitro-2'-chloro-flavone-8-acetic acid
-
slightly cytotoxic, 76% inhibition at 1 mM
3-nitro-2-(2-benzyloxyphenyl)-4-oxo-4H-1-benzopyran-8-acetic acid methoxymethyl ester
-
highly cytotoxic, 32% inhibition at 1 mM
3-nitro-2-(2-nitrophenyl)-4-oxo-4H-1-benzopyran-8-acetic acid methoxymethyl ester
-
highly cytotoxic, 48% inhibition at 1 mM
3-nitro-4'-methoxy-flavone-8-acetic acid
-
cytotoxic, 64% inhibition at 1 mM
3-nitro-flavone
-
30% inhibition at 1 mM
3-nitro-flavone-8-acetaldehyde
-
cytotoxic, 51% inhibition at 1 mM
3-nitroflavone-8-acetic acid
-
68% inhibition at 1 mM
3-[(1-amino-3-methylbutyl)(hydroxy)phosphoryl]propanoic acid
-
-
3-[(1-amino-3-phenylpropyl)(hydroxy)phosphoryl]-2-(4-hydroxybenzyl)propanoic acid
-
-
3-[(1-amino-3-phenylpropyl)(hydroxy)phosphoryl]-2-benzylpropanoic acid
-
-
3-[(1-aminoethyl)(hydroxy)phosphoryl]-2-methylpropanoic acid
-
-
4-(2-(((1-aminobutyl)(hydroxy)phosphoryl)methanethioamido)ethyl)benzoic acid
-
-
4-(2-amino-3-sulfanylpropyl)phenol
-
IC50: 45 nM
4-hydroxybestatin
-
-
5,6-dehydrokawain
-
17.7% inhibition at 0.03 mM
5,7-dihydroxy-8-geranylflavanone
-
28.9% inhibition at 0.03 mM
6-hydroxy-6-oxo-N-1,3-thiazol-2-yl-N2-[(3,4,5-trimethoxyphenyl)carbonyl]-L-norleucinamide
-
-
6-hydroxy-N-(methoxycarbonyl)-6-oxo-N2-[(3,4,5-trimethoxyphenyl)carbonyl]-L-norleucinamide
-
-
6-hydroxy-N-(methoxycarbonyl)-N-methyl-6-oxo-N2-[(3,4,5-trimethoxyphenyl)carbonyl]-L-norleucinamide
-
-
6-oxidanyl-6-oxidanylidene-N-[(3,4,5-trimethoxyphenyl)carbonyl]-L-norleucyl-N-hydroxyglycinamide
-
-
7,4'-dihydroxy-5-methoxyflavanone
-
14.4% inhibition at 0.03 mM
7-methoxy-5-hydroxy-8-geranylflavanone
-
17.0% inhibition at 0.03 mM
8-hydroxyquinoline
actinonin
adhesion/signaling-inducing antibody 452
-
-
-
alanine
-
-
alkyl D-cysteinats
-
-
alpha-thiolbestatin
-
-
alpha1-amino-3-phenylpropyl(alpha2-hydroxy-3-phenylpropyl)phosphinic acid
-
very potent inhibitor of APN
alpinetin
-
36.4% inhibition at 0.03 mM
amastatin
ammonia
-
-
Ammonium oxalate
-
-
angiotensin 4-8
-
-
angiotensin II
-
-
angiotensin III
-
-
angiotensin IV
anti-CD antibody WM15
-
-
-
anti-CD13 antibody WM15
-
anti-CD13 monoclonl antibody WM15
-
antipain
-
47% inhibition at 0.1 mM
apigenin
-
26% inhibition at 0.1 mM, 42% at 0.3 mM
arginine
-
-
arphamenine A
-
42% inhibition at 0.5 mM
baicalein
-
42% inhibition at 0.3 mM
benzo[c]phenanthridine derivatives
-
natural inhibitors
-
bestatin
bestatin thioamide
-
-
beta-amino-alpha-hydroxyphenylbutanoic acid
-
i.e. AHPA, or AHPA-VAl, natural inhibitor isolated from Streptomyces neyagawaensis strain SL-387, IC50: 0.0012-0.0056 mM
betulinic acid
bis(1-amino-3-methylbutyl)phosphinic acid
-
-
bis(1-amino-3-phenylpropyl)phosphinic acid
-
-
bis[amino(phenyl)methyl]phosphinic acid
-
-
bradykinin
Ca2+
-
-
cardamonin
-
37.2% inhibition at 0.03 mM
Cd2+
-
98% inhibition at 1 mM
chelerythrine
-
-
chymostatin
-
72% inhibition at 0.1 mM
coronavirus infection inhibitor Y2-K
-
-
-
Cu2+
-
96% inhibition at 1 mM
curcumin
cyclohexylmethyl N-[(2S)-3-amino-2-hydroxy-4-phenylbutanoyl]-L-leucinate
-
-
D-Arg-L-Lys-[Hyp3, CpG5, D-Tic7, CpG8]des-Arg9-bradykinin
-
competitive to L-Ala-4-nitroanilide, additionally inhibitory to kinin B1 receptor
divalinal
-
-
EC27
-
selective APN inhibitor
epsilon-amino-n-caproic acid
-
70% inhibition at 100 mM
ethyl D-cysteinate
-
strong, competitive inhibition, IC50: 350 nM
ezetimibe
-
-
flavone
-
5% inhibition at 1 mM
flavone-8-acetic acid
-
30% inhibition at 1 mM
flavone-8-acetic acid derivatives
-
-
-
geraniol
-
7.6% inhibition at 0.03 mM
geranyl-2,4-dihydroxy-6-phenylbenzoate
-
89.4% inhibition at 0.03 mM
glutamine
-
-
glycyl-N1-[(2R)-2-amino-3-phenylpropyl]-L-cysteinamide hydrochloride
-
-
glycyl-N1-[(2R)-2-amino-3-phenylpropyl]-L-leucinamide hydrochloride
-
-
H-(R)-beta2-homo-Val-Tyr-Ile-His-Pro-beta3-homo-Phe-OH
-
low potency inhibitor
H-(R)-beta2-homo-Val-Tyr-Ile-His-Pro-Phe-OH
-
low potency inhibitor
H-(S)-beta2-homo-Val-Tyr-Ile-His-Pro-Phe-OH
-
low potency inhibitor
H-beta2-homo-Leu-Tyr-Ile-His-Pro-beta3-homo-Phe-OH
-
low potency inhibitor
H-beta2-homo-Nle-Tyr-Ile-His-Pro-Phe-OH
-
low potency inhibitor
H-beta3-homo-Val-Tyr-Ile-His-Pro-Phe-OH
-
low potency inhibitor
H-Val-beta2-homo-Tyr-Ile-His-Pro-Phe-OH
-
low potency inhibitor
H-Val-beta3-homo-Tyr-Ile-His-Pro-Phe-OH
-
low potency inhibitor
H-Val-Tyr-beta2-homo-Leu-His-Pro-Phe-OH
-
low potency inhibitor
H-Val-Tyr-beta3-homo-Ile-His-Pro-Phe-OH
-
low potency inhibitor
H-Val-Tyr-Ile-beta3-homo-His-Pro-Phe-OH
-
low potency inhibitor
H-Val-Tyr-Ile-His-(R)-beta2-homo-Pro-Phe-OH
-
low potency inhibitor
H-Val-Tyr-Ile-His-beta3-homo-Pro-Phe-OH
-
low potency inhibitor
H-Val-Tyr-Ile-His-Pro-beta2-homo-Pro-Phe-OH
-
low potency inhibitor
H-Val-Tyr-Ile-His-Pro-beta3-homo-Phe-OH
-
low potency inhibitor
H-Val-Tyr-Ile-His-Pro-Phe-OH
-
low potency inhibitor
Hg2+
-
71% inhibition at 1 mM
icatibant
-
-
iodoacetamide
-
IC50: 0.098 mM, kidney enzyme
kaempferol
-
13.7% inhibition at 0.03 mM
kaempferol 3-O-beta -D-glucopyranosyl-(1-'4)-a -L-rhamnopyranosyl-7-O-alpha -L-rhamnopyranoside
-
13.8% inhibition at 0.03 mM
kaempferol 3-O-beta-D-(3''-acetylglucopyranosyl)-7-O-alpha-L-2'''-O-[(S)-2-methylbutanoyl]rhamnopyranoside
-
16.4% inhibition at 0.03 mM
kaempferol 3-O-beta-D-(3''-O-acetylglucopyranocyl)-7-O-alpha-L-3'''-O-[(S)-2-methylbutanoyl]rhamnopyranoside
-
23.7% inhibition at 0.03 mM
kaempferol 3-O-beta-D-(3''-O-acetylglucopyranosyl)-7-O-alpha-L-(2'''-O-isobutyryl)rhamnopyranoside
-
21.7% inhibition at 0.03 mM
kaempferol 3-O-beta-D-glucopyranoside
-
31.7% inhibition at 0.03 mM
kaempferol 3-O-beta-D-glucopyranosyl-7-O-(3''-O-isobutyryl)rhamnopyranoside
-
26.9% inhibition at 0.03 mM
kaempferol 3-O-beta-D-glucopyranosyl-7-O-alpha-L-rhamnopyranoside
-
19.1% inhibition at 0.03 mM
kaempferol 7-O-alpha-L-rhamnopyranoside
-
12.5% inhibition at 0.03 mM
Kelatorphan
-
-
L-Ala
-
at micromolar concentrations
L-alanyl-N1-[(2R)-2-amino-3-phenylpropyl]-L-leucinamide hydrochloride
-
-
L-Arg
-
at micromolar concentrations
L-cysteinyl-N-[(2R)-2-amino-3-phenylpropyl]-L-phenylalaninamide hydrochloride
-
-
L-cysteinyl-N1-[(2R)-2-amino-3-phenylpropyl]-L-cysteinamide hydrochloride
-
-
L-Glu
-
at micromolar concentrations
L-iso-glutamine inhibitors
-
diverse derivatives, IC50 of 0.016-0.053 mM
-
L-isoleucyl-N1-[(2R)-2-amino-3-phenylpropyl]-L-cysteinamide hydrochloride
-
-
L-isoleucyl-N1-[(2R)-2-amino-3-phenylpropyl]-L-leucinamide hydrochloride
-
-
L-isoleucyl-N1-[(2R)-2-amino-3-phenylpropyl]-L-phenylalaninamide hydrochloride
-
-
L-leucyl-N1-[(2R)-2-amino-3-phenylpropyl]-L-leucinamide hydrochloride
-
-
L-leucyl-N1-[(2R)-2-amino-3-phenylpropyl]-L-phenylalaninamide hydrochloride
-
-
L-leucyl-N1-[(2R)-2-amino-3-phenylpropyl]-Lcysteinamide hydrochloride
-
-
L-Lys-L-Lys-[Hyp3, CpG5, D-Tic7, CpG8]des-Arg9-bradykinin
-
competitive to L-Ala-4-nitroanilide
L-lysyl-N1-[(2R)-2-amino-3-phenylpropyl]-L-cysteinamide hydrochloride
-
-
L-lysyl-N1-[(2R)-2-amino-3-phenylpropyl]-L-phenylalaninamide hydrochloride
-
-
L-Met
-
at micromolar concentrations
L-methionyl-N-[(2R)-2-amino-3-phenylpropyl]-L-phenylalaninamide hydrochloride
-
-
L-methionyl-N1-[(2R)-2-amino-3-phenylpropyl]-L-cysteinamide hydrochloride
-
-
L-methionyl-N1-[(2R)-2-amino-3-phenylpropyl]-L-leucinamide hydrochloride
-
-
L-ornithyl-N1-[(2R)-2-amino-3-phenylpropyl]-L-cysteinamide hydrochloride
-
-
L-phenylalanyl-N-[(2R)-2-amino-3-phenylpropyl]-L-phenylalaninamide
-
-
L-phenylalanyl-N1-[(2R)-2-amino-3-phenylpropyl]-L-cysteinamide hydrochloride
-
-
L-tyrosyl-N1-[(2R)-2-amino-3-phenylpropyl]-L-leucinamide hydrochloride
-
-
L-Val-L-Tyr-L-Ile-2-aminomethylphenylacetic acid
-
inhibits both IRAP, EC 3.4.11.2, and aminopeptidase N and induces proliferation of stem cells at low concentrations
L-valyl-N-[(2R)-2-amino-3-phenylpropyl]-L-phenylalaninamide hydrochloride
-
-
L-valyl-N1-[(2R)-2-amino-3-phenylpropyl]-L-cysteinamide hydrochloride
-
-
lapstatin
Leu
-
at micromolar concentrations
leucine
-
-
leuhistin
leupeptin
-
24% inhibition at 0.1 mM
luteolin
-
60.2% inhibition at 0.03 mM
LVV-hemorphin 7
-
-
LVV-hemorphin-7
-
-
Methicillin
-
Ki: 4.61 mM
methionine
methyl (2S)-1-(methylsulfonyl)-4-oxopyrrolidine-2-carboxylate
-
-
methyl (2S)-1-[(4-methylphenyl)sulfonyl]-4-oxopyrrolidine-2-carboxylate
-
-
methyl (2S)-4-oxo-1-(phenylsulfonyl)pyrrolidine-2-carboxylate
-
-
methyl (2S,4R)-4-hydroxy-1-(methylsulfonyl)pyrrolidine-2-carboxylate
-
-
methyl (2S,4R)-4-hydroxy-1-(phenylsulfonyl)pyrrolidine-2-carboxylate
-
-
methyl (2S,4R)-4-hydroxy-1-[(4-methylphenyl)sulfonyl]pyrrolidine-2-carboxylate
-
-
methyl (4R)-4-([(2E)-3-(3,4-dihydroxyphenyl)prop-2-enoyl]amino)-1-[(3,4,5-trimethoxyphenyl)carbonyl]-L-prolinate
-
IC50: 0.9 nM
methyl (4R)-4-[[(2E)-3-(3,4-dihydroxyphenyl)prop-2-enoyl]amino]-1-[(3,4,5-trimethoxyphenyl)carbonyl]-L-prolinate
-
-
methyl 2-([[(3S)-2,6-dioxo-3-[[(3,4,5-trimethoxyphenyl)carbonyl]amino]piperidin-1-yl]acetyl]amino)-4-(methylperoxy)-4-oxobutanoate
-
-
methyl 2-chloro-N-[[(3S)-2,6-dioxo-3-[[(3,4,5-trimethoxyphenyl)carbonyl]amino]piperidin-1-yl]acetyl]alaninate
-
-
methyl 6-oxidanyl-6-oxidanylidene-N-[(3,4,5-trimethoxyphenyl)carbonyl]-L-norleucyl-(4R)-4-(benzyloxy)prolinate
-
-
methyl 6-oxidanyl-6-oxidanylidene-N-[(3,4,5-trimethoxyphenyl)carbonyl]-L-norleucyl-L-methioninate
-
-
methyl 6-oxidanyl-6-oxidanylidene-N-[(3,4,5-trimethoxyphenyl)carbonyl]-L-norleucylserinate
-
-
methyl bestatin
-
-
methyl N-[[(3S)-2,6-dioxo-3-[[(3,4,5-trimethoxyphenyl)carbonyl]amino]piperidin-1-yl]acetyl]-D-phenylalaninate
-
-
methyl N-[[(3S)-2,6-dioxo-3-[[(3,4,5-trimethoxyphenyl)carbonyl]amino]piperidin-1-yl]acetyl]-L-phenylalaninate
-
-
methyl N-[[(3S)-2,6-dioxo-3-[[(3,4,5-trimethoxyphenyl)carbonyl]amino]piperidin-1-yl]acetyl]cysteinate
-
-
methyl N-[[(3S)-2,6-dioxo-3-[[(3,4,5-trimethoxyphenyl)carbonyl]amino]piperidin-1-yl]acetyl]glycinate
-
-
methyl N-[[(3S)-2,6-dioxo-3-[[(3,4,5-trimethoxyphenyl)carbonyl]amino]piperidin-1-yl]acetyl]histidinate
-
-
methyl N-[[(3S)-2,6-dioxo-3-[[(3,4,5-trimethoxyphenyl)carbonyl]amino]piperidin-1-yl]acetyl]isoleucinate
-
-
methyl N-[[(3S)-2,6-dioxo-3-[[(3,4,5-trimethoxyphenyl)carbonyl]amino]piperidin-1-yl]acetyl]leucinate
-
-
methyl N-[[(3S)-2,6-dioxo-3-[[(3,4,5-trimethoxyphenyl)carbonyl]amino]piperidin-1-yl]acetyl]methioninate
-
-
methyl N-[[(3S)-2,6-dioxo-3-[[(3,4,5-trimethoxyphenyl)carbonyl]amino]piperidin-1-yl]acetyl]threoninate
-
-
methyl N-[[(3S)-2,6-dioxo-3-[[(3,4,5-trimethoxyphenyl)carbonyl]amino]piperidin-1-yl]acetyl]tryptophanate
-
-
methyl N-[[(3S)-2,6-dioxo-3-[[(3,4,5-trimethoxyphenyl)carbonyl]amino]piperidin-1-yl]acetyl]tyrosinate
-
-
methyl N-[[(3S)-2,6-dioxo-3-[[(3,4,5-trimethoxyphenyl)carbonyl]amino]piperidin-1-yl]acetyl]valinate
-
-
methyl N2-[[(3S)-2,6-dioxo-3-[[(3,4,5-trimethoxyphenyl)carbonyl]amino]piperidin-1-yl]acetyl]-N5-(nitrocarbamimidoyl)ornithinate
-
-
methyl N2-[[(3S)-2,6-dioxo-3-[[(3,4,5-trimethoxyphenyl)carbonyl]amino]piperidin-1-yl]acetyl]lysinate
-
-
methyl [(3S)-2,6-dioxo-3-[[(3,4,5-trimethoxyphenyl)carbonyl]amino]piperidin-1-yl]acetate
-
-
Mg2+
-
not inhibitory at 1 mM
morphiceptin
-
-
MR-387 A
-
-
Mr-387 B
-
-
multiflorin B
-
32.8% inhibition at 0.03 mM
multinoside A
-
15.3% inhibition at 0.03 mM
myricetin
-
48% inhibition at 0.3 mm
N-(4-aminophenyl)-6-hydroxy-6-oxo-N2-[(3,4,5-trimethoxyphenyl)carbonyl]-L-norleucinamide
-
-
N-(4-chlorophenyl)-6-hydroxy-6-oxo-N2-[(3,4,5-trimethoxyphenyl)carbonyl]-L-norleucinamide
-
-
N-hydroxy-2-(2-methylpropyl)-N'-(4-phenylbutyl)propanediamide
-
-
N-hydroxy-2-(naphthalen-2-ylsulfanyl)-acetamide
-
-
N-hydroxy-2-(naphthalene-2-ylsulfanyl)acetamide
-
-
N-[(2S)-2-(([(1R)-1-amino-2-phenylethyl](hydroxy)phosphoryl)methyl)-4-methylpentanoyl]-L-phenylalanine
-
IC50: 2.3 nM
N-[(2S)-3-([(1R)-1-amino-2-phenylethyl](hydroxy)phosphoryl)-2-(biphenyl-4-ylmethyl)propanoyl]-L-alanine
-
IC50: 5.3 nM
N-[(2S)-3-([(1R)-1-amino-2-phenylethyl](hydroxy)phosphoryl)-2-benzylpropanoyl]phenylalanine
-
IC50: 1.5 nM
N-[(2S)-3-([(1R)-1-aminoethyl](hydroxy)phosphoryl)-2-(4-bromobenzyl)propanoyl]-L-alanine
-
IC50: 1.9 nM
N-[(2S)-3-([(1R)-1-aminoethyl](hydroxy)phosphoryl)-2-(biphenyl-4-ylmethyl)propanoyl]alanine
-
IC50: 2.9 nM
N-[(2S)-3-([(R)-amino(phenyl)methyl](hydroxy)phosphoryl)-2-(biphenyl-4-ylmethyl)propanoyl]-L-alanine
-
IC50: 4.8 nM
N-[(2S)-3-([(R)-amino(phenyl)methyl](hydroxy)phosphoryl)-2-(biphenyl-4-ylmethyl)propanoyl]-L-serine
-
IC50: 4.9 nM
N-[(2S)-3-([(R)-amino(phenyl)methyl](hydroxy)phosphoryl)-2-(biphenyl-4-ylmethyl)propanoyl]-L-threonine
-
IC50: 10.2 nM
N-[(2S)-3-([(R)-amino(phenyl)methyl](hydroxy)phosphoryl)-2-(biphenyl-4-ylmethyl)propanoyl]glycine
-
IC50: 32.8 nM
N-[(2S)-3-([(R)-amino(phenyl)methyl](hydroxy)phosphoryl)-2-benzylpropanoyl]-L-phenylalanine
-
IC50: 4.2 nM
N-[(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl]benzamide
-
-
N-[(3S)-1-[2-(hydroxyamino)-2-oxoethyl]-2,6-dioxopiperidin-3-yl]-3,4,5-trimethoxybenzamide
-
-
N1-[(2R)-2-amino-3-phenylpropyl]-N-(2,4-dichlorobenzoyl)-L-cysteinamide hydrochloride
-
-
N1-[(2R)-2-amino-3-phenylpropyl]-N-(2,4-dichlorobenzoyl)-L-phenylalaninamide hydrochloride
-
-
N1-[(2R)-2-amino-3-phenylpropyl]-N-(3,5-dinitrobenzoyl)-L-phenylalaninamide hydrochloride
-
-
N1-[(2R)-2-amino-3-phenylpropyl]-N-(3-phenylpropanoyl)-L-phenylalaninamide hydrochloride
-
-
N1-[(2R)-2-amino-3-phenylpropyl]-N-(4-chlorobutanoyl)-L-phenylalaninamide hydrochloride
-
-
N1-[(2R)-2-amino-3-phenylpropyl]-N-(4-methoxybenzoyl)-L-phenylalaninamide hydrochloride
-
-
N1-[(2R)-2-amino-3-phenylpropyl]-N-(4-nitrobenzoyl)-Lphenylalaninamide hydrochloride
-
-
N1-[(2R)-2-amino-3-phenylpropyl]-N-(6-aminohexanoyl)-L-cysteinamide hydrochloride
-
-
N1-[(2R)-2-amino-3-phenylpropyl]-N-(6-aminohexanoyl)-L-leucinamide hydrochloride
-
-
N1-[(2R)-2-amino-3-phenylpropyl]-N-(6-aminohexanoyl)-L-phenylalaninamide hydrochloride
-
-
N6-[(benzyloxy)carbonyl]-N-hydroxy-N2-(pyrazin-2-ylcarbonyl)-L-lysinamide
-
-
N6-[(benzyloxy)carbonyl]-N-hydroxy-N2-(pyridin-3-ylcarbonyl)-L-lysinamide
-
-
N6-[(benzyloxy)carbonyl]-N-hydroxy-N2-[(2E)-3-phenylprop-2-enoyl]-L-lysinamide
-
-
N6-[(benzyloxy)carbonyl]-N-hydroxy-N2-[(3-nitrophenyl)carbonyl]-L-lysinamide
-
-
N6-[(benzyloxy)carbonyl]-N2-(pyrazin-2-ylcarbonyl)-L-lysine
-
-
N6-[(benzyloxy)carbonyl]-N2-(pyridin-3-ylcarbonyl)-L-lysine
-
-
N6-[(benzyloxy)carbonyl]-N2-[(2,4-dichlorophenyl)carbonyl]-L-lysine
-
-
N6-[(benzyloxy)carbonyl]-N2-[(2,4-dichlorophenyl)carbonyl]-N-hydroxy-L-lysinamide
-
-
N6-[(benzyloxy)carbonyl]-N2-[(2E)-3-phenylprop-2-enoyl]-L-lysine
-
-
N6-[(benzyloxy)carbonyl]-N2-[(3-nitrophenyl)carbonyl]-L-lysine
-
-
N6-[(benzyloxy)carbonyl]-N2-[(4-bromophenyl)carbonyl]-L-lysine
-
-
N6-[(benzyloxy)carbonyl]-N2-[(4-bromophenyl)carbonyl]-N-hydroxy-L-lysinamide
-
-
NaN3
-
-
Ni2+
-
-
PAQ-22
phebestin
phenylalanine
pinocembrin
-
13.3% inhibition at 0.03 mM
pinostrobin
-
10.5% inhibition at 0.03 mM
PIQ-22
-
-
PMSF
-
4.5% inhibition at 1 mM
Pro
-
at micromolar concentrations
probestin
psammaplin A
pseudoglutamyl aminophosphinic peptides
-
-
-
puromycin
quercetin
-
18.1% inhibition at 0.03 mM
quercetin 3-O-beta-D-glucopyranosyl-7-O-alpha-L-3'''-O-[(2S)-2-methylbutanoyl]-rhamnopyranoside
-
36.2% inhibition at 0.03 mM
quercetin 3-O-glucoside
-
41.8% inhibition at 0.03 mM
quercetin-3-O-beta-D-glucopyranosyl-7-O-alpha-L-rhamnopyranoside
-
12.6% inhibition at 0.03 mM
ranatachykinin
-
-
-
RB101
-
-
RB120
-
-
RB129
-
-
RB3014
-
IC50: 0.000025 mM, kidney enzyme
RB38A
-
-
S-carboxymethyl-L-cysteine
-
33% residual activity at 10 mM
S-carboxymethyl-L-cysteinyl-glycine
-
57% residual activity at 10 mM
S-carboxymethyl-L-glutathione
-
75% residual activity at 10 mM
sinocrassoside A1
-
31.4% inhibition at 0.03 mM
sinocrassoside A10
-
28.7% inhibition at 0.03 mM
sinocrassoside A2
-
35.7% inhibition at 0.03 mM
sinocrassoside A4
-
26.9% inhibition at 0.03 mM
sinocrassoside A5
-
21.7% inhibition at 0.03 mM
sinocrassoside A6
-
16.4% inhibition at 0.03 mM
sinocrassoside A7
-
23.7% inhibition at 0.03 mM
sinocrassoside A9
-
19.9% inhibition at 0.03 mM
sinocrassoside B1
-
33.9% inhibition at 0.03 mM
sinocrassoside B2
-
39.4% inhibition at 0.03 mM
sinocrassoside B3
-
36.2% inhibition at 0.03 mM
sinocrassoside B4
-
32.1% inhibition at 0.03 mM
sinocrassoside B5
-
28.3% inhibition at 0.03 mM
sinocrassoside C1
-
12.4% inhibition at 0.03 mM
sinocrassoside D1
-
35.1% inhibition at 0.03 mM
sinocrassoside D3
-
23.2% inhibition at 0.03 mM
SL-387
-
i.e. AHPA-Val
Substance P
substance P1-4
-
-
tert-butyl bestatin
-
i.e. BE17, the BE15 derivative has a dual inhibitory effect on invasion and motility on tumor and endothelial cells
tert-butyl N-[(2S)-3-amino-2-hydroxy-4-phenylbutanoyl]-L-leucinate
-
-
tryptophan
-
63% inhibition at 5 mM
tyrosine
-
59% inhibition at 2.25 mM
ubenimex
[(3S)-2,6-dioxo-3-[[(3,4,5-trimethoxyphenyl)carbonyl]amino]piperidin-1-yl]acetic acid
-
-
[1-amino-3-(4-hydroxyphenyl)propyl]phosphonic acid
-
-
[3-nitro-2-(2-nitrophenyl)-4-oxo-4H-chromen-8-yl]acetic acid
-
IC50: 0.025 mM
[amino(cyclobutyl)methyl]phosphonic acid
-
-
[amino(cyclohexyl)methyl]phosphonic acid
-
-
[amino(cyclopropyl)methyl]phosphonic acid
-
-
[amino(phenyl)methyl](1-amino-3-phenylpropyl)phosphinic acid
-
-
[amino(phenyl)methyl](1-hydroxy-3-methylbutyl)phosphinic acid
-
-
[amino(phenyl)methyl](1-hydroxy-3-phenylpropyl)phosphinic acid
-
-
[amino(phenyl)methyl](1-hydroxyethyl)phosphinic acid
-
-
[amino(phenyl)methyl](1-hydroxypentyl)phosphinic acid
-
-
[amino(phenyl)methyl][hydroxy(phenyl)methyl]phosphinic acid
-
-
[amino[4-(1-methylethyl)phenyl]methyl]phosphonic acid
-
-
[[(1-amino-3-methylbutyl)(hydroxy)phosphoryl]amino]acetic acid
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
transforming growth factor-beta1
-
transforming growth factor-beta1 at physiological concentrations (0.16 to 2.5 ng/ml) increases expression of CD13 both at mRNA and membrane protein level in a time- and concentration-dependent manner, increased membrane CD13 expression is associated with an increase of its enzyme activity, actinomycin-D abrogates the transforming growth factor-beta1-induced up-regulation of CD13
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0467
9-(L-leucylamino)-5H-benzo[a]phenoxazin-5-iminium
37°C, pH 7.4
0.087 - 0.256
Ala-2-naphthylamide
0.1 - 0.33
amino acyl-4-methylcoumarin 7-amide
-
Ala-, Met-, Tyr-, Leu-, Phe-, Arg-, Lys-, Gly-derivatives
0.74
Gly-4-nitroanilide
-
-
0.075 - 0.088
L-Arg-2-naphthylamide
0.785
L-Asn-2-naphthylamide
-
-
-
0.117
L-Gln-2-naphthylamide
-
-
2.33
L-Glu-2-naphthylamide
-
-
0.367
L-His-2-naphthylamide
-
-
0.092
L-Ile-2-naphthylamide
-
-
0.25 - 0.6
L-Leu-4-nitroanilide
0.02 - 0.068
L-Met-2-naphthylamide
0.617
L-Thr-2-naphthylamide
-
-
-
0.07
L-Val-2-naphthylamide
-
-
0.067 - 0.095
Leu-2-naphthylamide
0.647
Leu-p-nitroanilide
-
-
0.025 - 0.054
Lys-2-naphthylamide
0.202 - 0.327
Phe-2-naphthylamide
0.108
Ser-2-naphthylamide
-
-
0.329
Tyr-2-naphthylamide
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
303
Ala-2-naphthylamide
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000341
(1-amino-2-anilinoethyl)phosphonic acid
pH not specified in the publication, temperature not specified in the publication
0.000065
(1-amino-2-[[(4-methoxyphenyl)methyl]amino]ethyl)phosphonic acid
pH not specified in the publication, temperature not specified in the publication
0.00069
[1-amino-2-(cyclohexylamino)ethyl]phosphonic acid
pH not specified in the publication, temperature not specified in the publication
0.0547
(1-amino-2-cyclohexylethyl)phosphonic acid
-
-
0.0477
(1-amino-2-cyclopentylethyl)phosphonic acid
-
-
0.0371
(1-amino-3-cyclohexylpropyl)phosphonic acid
-
-
0.0185
(1-amino-3-cyclopentylpropyl)phosphonic acid
-
-
0.0369
(1-amino-3-phenylbutyl)phosphonic acid
-
-
0.0416
(1-amino-4-cyclohexylbutyl)phosphonic acid
-
-
0.00369
(1-amino-5-phenylpentyl)phosphonic acid
-
-
0.067
1,10-phenanthroline
-
-
0.0002
actinonin
-
-
0.0094
bradykinin
-
-
0.0022
D-Arg-L-Lys-[Hyp3, CpG5, D-Tic7, CpG8]des-Arg9-bradykinin
-
-
0.00487
L-Lys-L-Lys-[Hyp3, CpG5, D-Tic7, CpG8]des-Arg9-bradykinin
-
-
0.00023
leuhistin
-
-
4.61
Methicillin
-
-
0.169
morphiceptin
-
-
0.0035
N-hydroxy-2-(naphthalen-2-ylsulfanyl)-acetamide
-
-
0.67
phenylalanine
-
-
0.000019
probestin
-
-
0.0125
puromycin
-
-
0.00044
Substance P
-
-
0.0237
[1-amino-3-(4-hydroxyphenyl)propyl]phosphonic acid
-
-
0.0774
[amino(cyclobutyl)methyl]phosphonic acid
-
-
0.161
[amino(cyclohexyl)methyl]phosphonic acid
-
-
0.178
[amino(cyclopropyl)methyl]phosphonic acid
-
-
0.168
[amino[4-(1-methylethyl)phenyl]methyl]phosphonic acid
-
-
additional information
additional information
-
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00025 - 0.0005
(1-amino-2-methylpropyl)(1-hydroxy-3-phenylpropyl)phosphinic acid
0.00093
(1-amino-2-phenylethyl)(1-hydroxy-3-phenylpropyl)phosphinic acid
Homo sapiens
-
at 37°C in 100 mM Tris-HCl, pH 7.5
0.00042 - 0.001
(1-amino-3-methylbutyl)(1-hydroxy-3-phenylpropyl)phosphinic acid
0.003
(1-amino-3-methylbutyl)(1-hydroxypentyl)phosphinic acid
Homo sapiens
-
-
0.004
(1-amino-3-methylbutyl)[amino(phenyl)methyl]phosphinic acid
Homo sapiens
-
-
0.05
(1-aminobutyl)(1-amino-3-methylbutyl)phosphinic acid
Homo sapiens
-
-
0.002
(1-aminobutyl)(1-hydroxy-2-phenylethyl)phosphinic acid
Homo sapiens
-
at 37°C in 100 mM Tris-HCl, pH 7.5
0.017
(1-aminobutyl)[amino(phenyl)methyl]phosphinic acid
Homo sapiens
-
-
0.155
(1-aminoethyl)(1-amino-3-methylbutyl)phosphinic acid
Homo sapiens
-
-
0.046
(1-aminoethyl)[amino(phenyl)methyl]phosphinic acid
Homo sapiens
-
-
0.00087
(1-aminoethyl)[hydroxy[4-(propan-2-yl)phenyl]methyl]phosphinic acid
Homo sapiens
-
at 37°C in 100 mM Tris-HCl, pH 7.5
0.02
(1-aminohexyl)((2-(methoxycarbonyl)benzyl)carbamothioyl)phosphinic acid
Homo sapiens
-
IC50 above 0.02 mM, at 37°C in 100 mM Tris-HCl, pH 7.5
0.00086
(1-aminopentyl)(1-hydroxy-2-phenylpropyl)phosphinic acid
Homo sapiens
-
at 37°C in 100 mM Tris-HCl, pH 7.5
0.00022
(1-aminopentyl)(1-hydroxy-3-phenylpropyl)phosphinic acid
Homo sapiens
-
at 37°C in 100 mM Tris-HCl, pH 7.5
0.0093
(1-aminopentyl)[hydroxy(4-hydroxyphenyl)methyl]phosphinic acid
Homo sapiens
-
at 37°C in 100 mM Tris-HCl, pH 7.5
0.0006
(1-aminopropyl)(1-hydroxy-3-phenylpropyl)phosphinic acid
Homo sapiens
-
at 37°C in 100 mM Tris-HCl, pH 7.5
0.0297
(1-benzyl-1H-imidazol-4-yl)methyl 6-oxidanyl-6-oxidanylidene-N-[(3,4,5-trimethoxyphenyl)carbonyl]-L-norleucylalaninate
Homo sapiens
-
-
0.00007
(1S)-1-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)ethanaminium acetate
Homo sapiens
-
IC50: 70 nM
0.00005
(1S)-2-phenyl-1-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)ethanaminium acetate
Homo sapiens
-
IC50: 50 nM
0.000074
(1S)-3-methyl-1-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)butan-1-aminium acetate
Homo sapiens
-
IC50: 74 nM
0.3089
(2R)-N-[5-(4-bromophenyl)-1,3,4-thiadiazol-2-yl]-2-[(benzoyl)amino]-propanamide
Homo sapiens
-
in phosphate sodium buffer (pH 7.2, 50 mM), at 37°C
0.2966
(2R)-N-[5-(4-bromophenyl)-1,3,4-thiadiazol-2-yl]-2-[(phenylacetyl)-amino]-propanamide
Homo sapiens
-
in phosphate sodium buffer (pH 7.2, 50 mM), at 37°C
0.1073
(2R)-N-[5-(4-bromophenyl)-1,3,4-thiadiazol-2-yl]-2-[(phenylsulfonyl)-amino]-propanamide
Homo sapiens
-
in phosphate sodium buffer (pH 7.2, 50 mM), at 37°C
0.2875
(2R)-N-[5-(4-chlorophenyl)-1,3,4-thiadiazol-2-yl]-2-[(benzoyl)amino]-propanamide
Homo sapiens
-
in phosphate sodium buffer (pH 7.2, 50 mM), at 37°C
0.2058
(2R)-N-[5-(4-chlorophenyl)-1,3,4-thiadiazol-2-yl]-2-[(phenylacetyl)-amino]-propanamide
Homo sapiens
-
in phosphate sodium buffer (pH 7.2, 50 mM), at 37°C
0.0964
(2R)-N-[5-(4-chlorophenyl)-1,3,4-thiadiazol-2-yl]-2-[(phenylsulfonyl)-amino]-propanamide
Homo sapiens
-
in phosphate sodium buffer (pH 7.2, 50 mM), at 37°C
0.1905
(2R)-N-[5-(4-fluorophenyl)-1,3,4-thiadiazol-2-yl]-2-[(benzoyl)amino]-propanamide
Homo sapiens
-
in phosphate sodium buffer (pH 7.2, 50 mM), at 37°C
0.169
(2R)-N-[5-(4-fluorophenyl)-1,3,4-thiadiazol-2-yl]-2-[(phenylacetyl)-amino]-propanamide
Homo sapiens
-
in phosphate sodium buffer (pH 7.2, 50 mM), at 37°C
0.1153
(2R)-N-[5-(4-fluorophenyl)-1,3,4-thiadiazol-2-yl]-2-[(phenylsulfonyl)amino]-propanamide
Homo sapiens
-
in phosphate sodium buffer (pH 7.2, 50 mM), at 37°C
0.0698
(2R)-N-[5-(4-methoxyphenyl)-1,3,4-thiadiazol-2-yl]-2-[(benzoyl)amino]-propanamide
Homo sapiens
-
in phosphate sodium buffer (pH 7.2, 50 mM), at 37°C
0.0399
(2R)-N-[5-(4-methoxyphenyl)-1,3,4-thiadiazol-2-yl]-2-[(phenylacetyl)-amino]-propanamide
Homo sapiens
-
in phosphate sodium buffer (pH 7.2, 50 mM), at 37°C
0.0488
(2R)-N-[5-(4-methoxyphenyl)-1,3,4-thiadiazol-2-yl]-2-[(phenylsulfonyl)amino]-propanamide
Homo sapiens
-
in phosphate sodium buffer (pH 7.2, 50 mM), at 37°C
0.1178
(2R)-N-[5-(4-methylphenyl)-1,3,4-thiadiazol-2-yl]-2-[(benzoyl)amino]-propanamide
Homo sapiens
-
in phosphate sodium buffer (pH 7.2, 50 mM), at 37°C
0.107
(2R)-N-[5-(4-methylphenyl)-1,3,4-thiadiazol-2-yl]-2-[(phenylacetyl)-amino]-propanamide
Homo sapiens
-
in phosphate sodium buffer (pH 7.2, 50 mM), at 37°C
0.3378
(2R)-N-[5-(4-methylphenyl)-1,3,4-thiadiazol-2-yl]-2-[(phenylsulfonyl)-amino]-propanamide
Homo sapiens
-
in phosphate sodium buffer (pH 7.2, 50 mM), at 37°C
0.3178
(2R)-N-[5-(4-nitrorophenyl)-1,3,4-thiadiazol-2-yl]-2-[(benzoyl)amino]-propanamide
Homo sapiens
-
in phosphate sodium buffer (pH 7.2, 50 mM), at 37°C
0.3091
(2R)-N-[5-(4-nitrorophenyl)-1,3,4-thiadiazol-2-yl]-2-[(phenylacetyl)-amino]-propanamide
Homo sapiens
-
in phosphate sodium buffer (pH 7.2, 50 mM), at 37°C
0.1678
(2R)-N-[5-(4-nitrorophenyl)-1,3,4-thiadiazol-2-yl]-2-[(phenylsulfonyl)-amino]-propanamide
Homo sapiens
-
in phosphate sodium buffer (pH 7.2, 50 mM), at 37°C
0.1701
(2R)-N-[5-phenyl-1,3,4-thiadiazol-2-yl]-2-[(benzoyl)-amino]-propanamide
Homo sapiens
-
in phosphate sodium buffer (pH 7.2, 50 mM), at 37°C
0.1416
(2R)-N-[5-phenyl-1,3,4-thiadiazol-2-yl]-2-[(phenylacetyl)amino]-propanamide
Homo sapiens
-
in phosphate sodium buffer (pH 7.2, 50 mM), at 37°C
0.3732
(2R)-N-[5-phenyl-1,3,4-thiadiazol-2-yl]-2-[(phenylsulfonyl)amino]-propanamide
Homo sapiens
-
in phosphate sodium buffer (pH 7.2, 50 mM), at 37°C
1.88
(2S)-2-amino-N-[(3S)-1-[2-(hydroxyamino)-2-oxoethyl]-2,6-dioxopiperidin-3-yl]-3-phenylpropanamide
Homo sapiens
-
in PBS buffer, at 37°C
0.0578
(3S)-N-hydroxy-2-(phenylsulfonyl)-6,10-dioxa-2-azaspiro[4.5]decane-3-carboxamide
Homo sapiens
-
-
0.0827
(3S)-N-hydroxy-2-(phenylsulfonyl)-6,11-dioxa-2-azaspiro[4.6]undecane-3-carboxamide
Homo sapiens
-
-
0.1067
(3S)-N-hydroxy-2-(phenylsulfonyl)-6,12-dioxa-2-azaspiro[4.7]dodecane-3-carboxamide
Homo sapiens
-
-
0.0485
(3S)-N-hydroxy-2-[(4-methylphenyl)sulfonyl]-6,10-dioxa-2-azaspiro[4.5]decane-3-carboxamide
Homo sapiens
-
-
0.0618
(3S)-N-hydroxy-2-[(4-methylphenyl)sulfonyl]-6,11-dioxa-2-azaspiro[4.6]undecane-3-carboxamide
Homo sapiens
-
-
0.0732
(3S)-N-hydroxy-2-[(4-methylphenyl)sulfonyl]-6,12-dioxa-2-azaspiro[4.7]dodecane-3-carboxamide
Homo sapiens
-
-
0.05
(4R)-4-(ethylamino)-2-(3-methoxypropyl)-1,1-dioxo-1,2,3,4-tetrahydro-1lambda~6~-thieno[3,2-e][1,2]thiazine-6-sulfonamide
Homo sapiens
-
IC50 is 0.05 mM
0.0000077
(4R)-4-(hexanoylamino)-N-hydroxy-1-[(3,4,5-trimethoxyphenyl)carbonyl]-L-prolinamide
0.0000021
(4R)-4-([(2E)-3-(3,4-dimethoxyphenyl)prop-2-enoyl]amino)-N-hydroxy-1-[(3,4,5-trimethoxyphenyl)carbonyl]-L-prolinamide
Homo sapiens
-
IC50: 2.1 nM
0.0000021
(4R)-4-[[(2E)-3-(3,4-dimethoxyphenyl)prop-2-enoyl]amino]-N-hydroxy-1-[(3,4,5-trimethoxyphenyl)carbonyl]-L-prolinamide
Homo sapiens
-
-
0.076
(aminomethyl)(1-amino-3-methylbutyl)phosphinic acid
Homo sapiens
-
-
0.042
(aminomethyl)[amino(phenyl)methyl]phosphinic acid
Homo sapiens
-
-
0.012 - 0.179
1,10-phenanthroline
0.00093
1-amino-2-methylpropyl(benzylcarbamoyl)phosphinic acid
Homo sapiens
-
-
0.00118 - 0.0012
1-amino-2-methylpropyl(hexylcarbamothioyl)phosphinic acid
0.0019 - 0.01535
1-amino-2-methylpropyl(isobutylcarbamothioyl)phosphinic acid
0.0146
1-amino-2-methylpropyl(methylcarbamothioyl)phosphinic acid
Homo sapiens
-
at 37°C in 100 mM Tris-HCl, pH 7.5
0.16
1-amino-2-methylpropyl(phenylcarbamoyl)phosphinic acid
Homo sapiens
-
-
0.02
1-amino-3-methylbutyl(2-(methoxycarbonyl)benzylcarbamothioyl)phosphinic acid
Homo sapiens
-
IC50 above 0.02 mM, at 37°C in 100 mM Tris-HCl, pH 7.5
0.0082
1-amino-3-methylbutyl(benzylcarbamothioyl)phosphinic acid
Homo sapiens
-
at 37°C in 100 mM Tris-HCl, pH 7.5
0.0005 - 0.00096
1-amino-3-methylbutyl(hexylcarbamothioyl)phosphinic acid
0.01056 - 0.02
1-amino-3-methylbutyl(methylcarbamothioyl)phosphinic acid
0.02
1-amino-3-methylbutyl(phenethylcarbamothioyl)phosphinic acid
Homo sapiens
-
IC50 above 0.02 mM, at 37°C in 100 mM Tris-HCl, pH 7.5
0.00047
1-amino-3-phenylpropyl(3-(methylthio)propylcarbamothioyl)phosphinic acid
Homo sapiens
-
at 37°C in 100 mM Tris-HCl, pH 7.5
0.0114
1-amino-3-phenylpropyl(4-(ethoxycarbonyl)benzylcarbamothioyl)phosphinic acid
Homo sapiens
-
at 37°C in 100 mM Tris-HCl, pH 7.5
0.00038 - 0.00064
1-amino-3-phenylpropyl(4-methoxybenzylcarbamothioyl)phosphinic acid
0.0013
1-amino-3-phenylpropyl(benzylcarbamothioyl)phosphinic acid
Homo sapiens
-
at 37°C in 100 mM Tris-HCl, pH 7.5
0.00056
1-amino-3-phenylpropyl(propylcarbamothioyl)phosphinic acid
Homo sapiens
-
at 37°C in 100 mM Tris-HCl, pH 7.5
0.00053
1-amino-4-methylpentyl(benzylcarbamoyl)phosphinic acid
Homo sapiens
-
-
0.035
1-amino-4-methylpentyl(phenylcarbamoyl)phosphinic acid
Homo sapiens
-
-
0.02
1-aminobutyl(2-(methoxycarbonyl)phenethylcarbamothioyl)phosphinic acid
Homo sapiens
-
IC50 above 0.02 mM, at 37°C in 100 mM Tris-HCl, pH 7.5
0.00145
1-aminobutyl(3-(methylthio)propylcarbamothioyl)phosphinic acid
Homo sapiens
-
at 37°C in 100 mM Tris-HCl, pH 7.5
0.02
1-aminobutyl(4-(ethoxycarbonyl)phenethylcarbamothioyl)phosphinic acid
Homo sapiens
-
IC50 above 0.02 mM, at 37°C in 100 mM Tris-HCl, pH 7.5
0.00068
1-aminobutyl(4-methoxybenzylcarbamothioyl)phosphinic acid
Homo sapiens
-
-
0.00215
1-aminobutyl(4-methoxyphenethylcarbamothioyl)phosphinic acid
Homo sapiens
-
at 37°C in 100 mM Tris-HCl, pH 7.5
0.00125
1-aminobutyl(benzylcarbamothioyl)phosphinic acid
Homo sapiens
-
at 37°C in 100 mM Tris-HCl, pH 7.5
0.00228 - 0.0036
1-aminobutyl(phenethylcarbamothioyl)phosphinic acid
0.00252
1-aminoethyl(3-(methylthio)propylcarbamothioyl)phosphinic acid
Homo sapiens
-
at 37°C in 100 mM Tris-HCl, pH 7.5
0.02
1-aminoethyl(4-(ethoxycarbonyl)benzylcarbamothioyl)phosphinic acid
Homo sapiens
-
IC50 above 0.02 mM, at 37°C in 100 mM Tris-HCl, pH 7.5
0.00112 - 0.02
1-aminoethyl(4-methoxybenzylcarbamothioyl)phosphinic acid
0.0022
1-aminoethyl(benzylcarbamothioyl)phosphinic acid
Homo sapiens
-
at 37°C in 100 mM Tris-HCl, pH 7.5
0.0042 - 0.0058
1-aminoethyl(phenethylcarbamothioyl)phosphinic acid
0.02
1-aminopentyl(2-(methoxycarbonyl)benzylcarbamothioyl)phosphinic acid
Homo sapiens
-
IC50 above 0.02 mM, at 37°C in 100 mM Tris-HCl, pH 7.5
0.00077
1-aminopentyl(3-(methylthio)propylcarbamothioyl)phosphinic acid
Homo sapiens
-
at 37°C in 100 mM Tris-HCl, pH 7.5
0.00025 - 0.00064
1-aminopentyl(4-methoxybenzylcarbamothioyl)phosphinic acid
0.0015
1-aminopentyl(benzylcarbamothioyl)phosphinic acid
Homo sapiens
-
at 37°C in 100 mM Tris-HCl, pH 7.5
0.00071 - 0.00073
1-aminopentyl(phenethylcarbamothioyl)phosphinic acid
0.0016
1-aminopropyl(3-(methylthio)propylcarbamothioyl)phosphinic acid
Homo sapiens
-
at 37°C in 100 mM Tris-HCl, pH 7.5
0.0189
2-([[(3S)-2,6-dioxo-3-[[(3,4,5-trimethoxyphenyl)carbonyl]amino]piperidin-1-yl]acetyl]amino)propaneperoxoic acid
Homo sapiens
-
-
0.00002
2-amino-1,4-dihydrophenanthren-3(2H)-one hydrochloride
Homo sapiens
-
-
0.000025
2-amino-2-phenylethanethiol
Homo sapiens
-
IC50: 25 nM
0.000056
2-amino-3-(benzyloxy)propane-1-thiol
Homo sapiens
-
IC50: 56 nM
0.00002
2-amino-3-(methylsulfanyl)propane-1-thiol
Homo sapiens
-
IC50: 20 nM
0.000021
2-amino-3-(methylsulfinyl)propane-1-thiol
Homo sapiens
-
IC50: 21 nM
0.00004
2-amino-3-(tert-butylsulfanyl)propane-1-thiol
Homo sapiens
-
IC50: 40 nM
0.000045
2-amino-3-cyclohexylpropane-1-thiol
Homo sapiens
-
IC50: 45 nM
0.00003
2-amino-3-phenylpropane-1-thiol
Homo sapiens
-
IC50: 30 nM
0.000011
2-amino-4-(methylsulfanyl)butane-1-thiol
Homo sapiens
-
IC50: 11 nM
0.00002
2-amino-4-(methylsulfinyl)butane-1-thiol
Homo sapiens
-
IC50: 20 nM
0.000022
2-amino-4-methylpentane-1-thiol
Homo sapiens
-
IC50: 22 nM
0.00008
3-amino-1-(2-phenylethyl)-3,4-dihydronaphthalen-2(1H)-one hydrochloride
Homo sapiens
-
-
0.02
4-(2-(((1-aminobutyl)(hydroxy)phosphoryl)methanethioamido)ethyl)benzoic acid
Homo sapiens
-
IC50 above 0.02 mM, at 37°C in 100 mM Tris-HCl, pH 7.5
0.000045
4-(2-amino-3-sulfanylpropyl)phenol
Homo sapiens
-
IC50: 45 nM
0.0228
6-hydroxy-6-oxo-N-1,3-thiazol-2-yl-N2-[(3,4,5-trimethoxyphenyl)carbonyl]-L-norleucinamide
Homo sapiens
-
-
0.0532
6-hydroxy-N-(methoxycarbonyl)-6-oxo-N2-[(3,4,5-trimethoxyphenyl)carbonyl]-L-norleucinamide
Homo sapiens
-
-
0.0414
6-hydroxy-N-(methoxycarbonyl)-N-methyl-6-oxo-N2-[(3,4,5-trimethoxyphenyl)carbonyl]-L-norleucinamide
Homo sapiens
-
-
0.0161
6-oxidanyl-6-oxidanylidene-N-[(3,4,5-trimethoxyphenyl)carbonyl]-L-norleucyl-N-hydroxyglycinamide
Homo sapiens
-
-
0.000075 - 0.0031
actinonin
0.00006
alpha1-amino-3-phenylpropyl(alpha2-hydroxy-3-phenylpropyl)phosphinic acid
Homo sapiens
-
at 37°C in 100 mM Tris-HCl, pH 7.5
0.0004 - 0.0169
bestatin
0.0012 - 0.0056
beta-amino-alpha-hydroxyphenylbutanoic acid
Homo sapiens
-
i.e. AHPA, or AHPA-VAl, natural inhibitor isolated from Streptomyces neyagawaensis strain SL-387, IC50: 0.0012-0.0056 mM
0.0073
betulinic acid
Homo sapiens
-
natural inhibitor isolated from birch tree, IC50: 0.0073 mM, a selectively apoptosis-inducing agent, overview
0.05
bis(1-amino-3-methylbutyl)phosphinic acid
Homo sapiens
-
-
0.00083
bis(1-amino-3-phenylpropyl)phosphinic acid
Homo sapiens
-
-
0.0006
bis[amino(phenyl)methyl]phosphinic acid
Homo sapiens
-
-
0.00035
ethyl D-cysteinate
Homo sapiens
-
strong, competitive inhibition, IC50: 350 nM
0.1737
glycyl-N1-[(2R)-2-amino-3-phenylpropyl]-L-cysteinamide hydrochloride
Homo sapiens
-
-
3.244
glycyl-N1-[(2R)-2-amino-3-phenylpropyl]-L-leucinamide hydrochloride
Homo sapiens
-
-
0.098
iodoacetamide
Homo sapiens
-
IC50: 0.098 mM, kidney enzyme
0.5215
L-alanyl-N1-[(2R)-2-amino-3-phenylpropyl]-L-leucinamide hydrochloride
Homo sapiens
-
-
0.0492
L-cysteinyl-N-[(2R)-2-amino-3-phenylpropyl]-L-phenylalaninamide hydrochloride
Homo sapiens
-
-
0.0103
L-cysteinyl-N1-[(2R)-2-amino-3-phenylpropyl]-L-cysteinamide hydrochloride
Homo sapiens
-
-
0.016 - 0.053
L-iso-glutamine inhibitors
Homo sapiens
-
diverse derivatives, IC50 of 0.016-0.053 mM
-
0.0148
L-isoleucyl-N1-[(2R)-2-amino-3-phenylpropyl]-L-cysteinamide hydrochloride
Homo sapiens
-
-
0.1476
L-isoleucyl-N1-[(2R)-2-amino-3-phenylpropyl]-L-leucinamide hydrochloride
Homo sapiens
-
-
0.1579
L-isoleucyl-N1-[(2R)-2-amino-3-phenylpropyl]-L-phenylalaninamide hydrochloride
Homo sapiens
-
-
0.1421
L-leucyl-N1-[(2R)-2-amino-3-phenylpropyl]-L-leucinamide hydrochloride
Homo sapiens
-
-
0.1809
L-leucyl-N1-[(2R)-2-amino-3-phenylpropyl]-L-phenylalaninamide hydrochloride
Homo sapiens
-
-
0.045
L-leucyl-N1-[(2R)-2-amino-3-phenylpropyl]-Lcysteinamide hydrochloride
Homo sapiens
-
-
0.0086
L-lysyl-N1-[(2R)-2-amino-3-phenylpropyl]-L-cysteinamide hydrochloride
Homo sapiens
-
-
0.0895
L-lysyl-N1-[(2R)-2-amino-3-phenylpropyl]-L-phenylalaninamide hydrochloride
Homo sapiens
-
-
0.0088
L-methionyl-N-[(2R)-2-amino-3-phenylpropyl]-L-phenylalaninamide hydrochloride
Homo sapiens
-
-
0.0165
L-methionyl-N1-[(2R)-2-amino-3-phenylpropyl]-L-cysteinamide hydrochloride
Homo sapiens
-
-
0.0304
L-methionyl-N1-[(2R)-2-amino-3-phenylpropyl]-L-leucinamide hydrochloride
Homo sapiens
-
-
0.0332
L-ornithyl-N1-[(2R)-2-amino-3-phenylpropyl]-L-cysteinamide hydrochloride
Homo sapiens
-
-
0.0155
L-phenylalanyl-N-[(2R)-2-amino-3-phenylpropyl]-L-phenylalaninamide
Homo sapiens
-
-
0.0098
L-phenylalanyl-N1-[(2R)-2-amino-3-phenylpropyl]-L-cysteinamide hydrochloride
Homo sapiens
-
-
0.1969
L-tyrosyl-N1-[(2R)-2-amino-3-phenylpropyl]-L-leucinamide hydrochloride
Homo sapiens
-
-
0.0585
L-valyl-N-[(2R)-2-amino-3-phenylpropyl]-L-phenylalaninamide hydrochloride
Homo sapiens
-
-
0.0588
L-valyl-N1-[(2R)-2-amino-3-phenylpropyl]-L-cysteinamide hydrochloride
Homo sapiens
-
-
0.0005
lapstatin
Homo sapiens
-
natural competitive inhibitor from Streptomyces sp., IC50: 0.0005 mM
0.0926
methyl (2S)-1-(methylsulfonyl)-4-oxopyrrolidine-2-carboxylate
Homo sapiens
-
-
0.0549
methyl (2S)-1-[(4-methylphenyl)sulfonyl]-4-oxopyrrolidine-2-carboxylate
Homo sapiens
-
-
0.0758
methyl (2S)-4-oxo-1-(phenylsulfonyl)pyrrolidine-2-carboxylate
Homo sapiens
-
-
0.0416
methyl (2S,4R)-4-hydroxy-1-(methylsulfonyl)pyrrolidine-2-carboxylate
Homo sapiens
-
-
0.0538
methyl (2S,4R)-4-hydroxy-1-(phenylsulfonyl)pyrrolidine-2-carboxylate
Homo sapiens
-
-
0.0384
methyl (2S,4R)-4-hydroxy-1-[(4-methylphenyl)sulfonyl]pyrrolidine-2-carboxylate
Homo sapiens
-
-
0.0000009
methyl (4R)-4-([(2E)-3-(3,4-dihydroxyphenyl)prop-2-enoyl]amino)-1-[(3,4,5-trimethoxyphenyl)carbonyl]-L-prolinate
Homo sapiens
-
IC50: 0.9 nM
0.0000009
methyl (4R)-4-[[(2E)-3-(3,4-dihydroxyphenyl)prop-2-enoyl]amino]-1-[(3,4,5-trimethoxyphenyl)carbonyl]-L-prolinate
Homo sapiens
-
-
0.0217
methyl 2-([[(3S)-2,6-dioxo-3-[[(3,4,5-trimethoxyphenyl)carbonyl]amino]piperidin-1-yl]acetyl]amino)-4-(methylperoxy)-4-oxobutanoate
Homo sapiens
-
-
0.05
methyl 2-chloro-N-[[(3S)-2,6-dioxo-3-[[(3,4,5-trimethoxyphenyl)carbonyl]amino]piperidin-1-yl]acetyl]alaninate
Homo sapiens
-
-
0.0302
methyl 6-oxidanyl-6-oxidanylidene-N-[(3,4,5-trimethoxyphenyl)carbonyl]-L-norleucyl-(4R)-4-(benzyloxy)prolinate
Homo sapiens
-
-
0.0507
methyl 6-oxidanyl-6-oxidanylidene-N-[(3,4,5-trimethoxyphenyl)carbonyl]-L-norleucyl-L-methioninate
Homo sapiens
-
-
0.0368
methyl 6-oxidanyl-6-oxidanylidene-N-[(3,4,5-trimethoxyphenyl)carbonyl]-L-norleucylserinate
Homo sapiens
-
-
0.011
methyl N-[[(3S)-2,6-dioxo-3-[[(3,4,5-trimethoxyphenyl)carbonyl]amino]piperidin-1-yl]acetyl]-D-phenylalaninate
Homo sapiens
-
-
0.0462
methyl N-[[(3S)-2,6-dioxo-3-[[(3,4,5-trimethoxyphenyl)carbonyl]amino]piperidin-1-yl]acetyl]-L-phenylalaninate
Homo sapiens
-
-
0.0503
methyl N-[[(3S)-2,6-dioxo-3-[[(3,4,5-trimethoxyphenyl)carbonyl]amino]piperidin-1-yl]acetyl]cysteinate
Homo sapiens
-
-
0.0554
methyl N-[[(3S)-2,6-dioxo-3-[[(3,4,5-trimethoxyphenyl)carbonyl]amino]piperidin-1-yl]acetyl]glycinate
Homo sapiens
-
-
0.0052
methyl N-[[(3S)-2,6-dioxo-3-[[(3,4,5-trimethoxyphenyl)carbonyl]amino]piperidin-1-yl]acetyl]histidinate
Homo sapiens
-
-
0.0493
methyl N-[[(3S)-2,6-dioxo-3-[[(3,4,5-trimethoxyphenyl)carbonyl]amino]piperidin-1-yl]acetyl]isoleucinate
Homo sapiens
-
-
0.0462
methyl N-[[(3S)-2,6-dioxo-3-[[(3,4,5-trimethoxyphenyl)carbonyl]amino]piperidin-1-yl]acetyl]leucinate
Homo sapiens
-
-
0.0207
methyl N-[[(3S)-2,6-dioxo-3-[[(3,4,5-trimethoxyphenyl)carbonyl]amino]piperidin-1-yl]acetyl]methioninate
Homo sapiens
-
-
0.0519
methyl N-[[(3S)-2,6-dioxo-3-[[(3,4,5-trimethoxyphenyl)carbonyl]amino]piperidin-1-yl]acetyl]threoninate
Homo sapiens
-
-
0.0431
methyl N-[[(3S)-2,6-dioxo-3-[[(3,4,5-trimethoxyphenyl)carbonyl]amino]piperidin-1-yl]acetyl]tryptophanate
Homo sapiens
-
-
0.0448
methyl N-[[(3S)-2,6-dioxo-3-[[(3,4,5-trimethoxyphenyl)carbonyl]amino]piperidin-1-yl]acetyl]tyrosinate
Homo sapiens
-
-
0.0214
methyl N-[[(3S)-2,6-dioxo-3-[[(3,4,5-trimethoxyphenyl)carbonyl]amino]piperidin-1-yl]acetyl]valinate
Homo sapiens
-
-
0.042
methyl N2-[[(3S)-2,6-dioxo-3-[[(3,4,5-trimethoxyphenyl)carbonyl]amino]piperidin-1-yl]acetyl]-N5-(nitrocarbamimidoyl)ornithinate
Homo sapiens
-
-
0.0381
methyl N2-[[(3S)-2,6-dioxo-3-[[(3,4,5-trimethoxyphenyl)carbonyl]amino]piperidin-1-yl]acetyl]lysinate
Homo sapiens
-
-
0.0634
methyl [(3S)-2,6-dioxo-3-[[(3,4,5-trimethoxyphenyl)carbonyl]amino]piperidin-1-yl]acetate
Homo sapiens
-
-
0.0234
N-(4-aminophenyl)-6-hydroxy-6-oxo-N2-[(3,4,5-trimethoxyphenyl)carbonyl]-L-norleucinamide
Homo sapiens
-
-
0.0243
N-(4-chlorophenyl)-6-hydroxy-6-oxo-N2-[(3,4,5-trimethoxyphenyl)carbonyl]-L-norleucinamide
Homo sapiens
-
-
0.0000023
N-[(2S)-2-(([(1R)-1-amino-2-phenylethyl](hydroxy)phosphoryl)methyl)-4-methylpentanoyl]-L-phenylalanine
Homo sapiens
-
IC50: 2.3 nM
0.0000053
N-[(2S)-3-([(1R)-1-amino-2-phenylethyl](hydroxy)phosphoryl)-2-(biphenyl-4-ylmethyl)propanoyl]-L-alanine
Homo sapiens
-
IC50: 5.3 nM
0.0000015
N-[(2S)-3-([(1R)-1-amino-2-phenylethyl](hydroxy)phosphoryl)-2-benzylpropanoyl]phenylalanine
Homo sapiens
-
IC50: 1.5 nM
0.0000019
N-[(2S)-3-([(1R)-1-aminoethyl](hydroxy)phosphoryl)-2-(4-bromobenzyl)propanoyl]-L-alanine
Homo sapiens
-
IC50: 1.9 nM
0.0000029
N-[(2S)-3-([(1R)-1-aminoethyl](hydroxy)phosphoryl)-2-(biphenyl-4-ylmethyl)propanoyl]alanine
Homo sapiens
-
IC50: 2.9 nM
0.0000048
N-[(2S)-3-([(R)-amino(phenyl)methyl](hydroxy)phosphoryl)-2-(biphenyl-4-ylmethyl)propanoyl]-L-alanine
Homo sapiens
-
IC50: 4.8 nM
0.0000049
N-[(2S)-3-([(R)-amino(phenyl)methyl](hydroxy)phosphoryl)-2-(biphenyl-4-ylmethyl)propanoyl]-L-serine
Homo sapiens
-
IC50: 4.9 nM
0.0000102
N-[(2S)-3-([(R)-amino(phenyl)methyl](hydroxy)phosphoryl)-2-(biphenyl-4-ylmethyl)propanoyl]-L-threonine
Homo sapiens
-
IC50: 10.2 nM
0.0000328
N-[(2S)-3-([(R)-amino(phenyl)methyl](hydroxy)phosphoryl)-2-(biphenyl-4-ylmethyl)propanoyl]glycine
Homo sapiens
-
IC50: 32.8 nM
0.0000042
N-[(2S)-3-([(R)-amino(phenyl)methyl](hydroxy)phosphoryl)-2-benzylpropanoyl]-L-phenylalanine
Homo sapiens
-
IC50: 4.2 nM
0.0031
N-[(3S)-1-[2-(hydroxyamino)-2-oxoethyl]-2,6-dioxopiperidin-3-yl]-3,4,5-trimethoxybenzamide
Homo sapiens
-
-
1.049
N1-[(2R)-2-amino-3-phenylpropyl]-N-(2,4-dichlorobenzoyl)-L-cysteinamide hydrochloride
Homo sapiens
-
-
2.263
N1-[(2R)-2-amino-3-phenylpropyl]-N-(2,4-dichlorobenzoyl)-L-phenylalaninamide hydrochloride
Homo sapiens
-
-
0.2772
N1-[(2R)-2-amino-3-phenylpropyl]-N-(3,5-dinitrobenzoyl)-L-phenylalaninamide hydrochloride
Homo sapiens
-
-
0.366
N1-[(2R)-2-amino-3-phenylpropyl]-N-(3-phenylpropanoyl)-L-phenylalaninamide hydrochloride
Homo sapiens
-
-
0.6928
N1-[(2R)-2-amino-3-phenylpropyl]-N-(4-chlorobutanoyl)-L-phenylalaninamide hydrochloride
Homo sapiens
-
-
0.1736
N1-[(2R)-2-amino-3-phenylpropyl]-N-(4-methoxybenzoyl)-L-phenylalaninamide hydrochloride
Homo sapiens
-
-
1.39
N1-[(2R)-2-amino-3-phenylpropyl]-N-(4-nitrobenzoyl)-Lphenylalaninamide hydrochloride
Homo sapiens
-
-
0.2024
N1-[(2R)-2-amino-3-phenylpropyl]-N-(6-aminohexanoyl)-L-cysteinamide hydrochloride
Homo sapiens
-
-
1.457
N1-[(2R)-2-amino-3-phenylpropyl]-N-(6-aminohexanoyl)-L-leucinamide hydrochloride
Homo sapiens
-
-
1.539
N1-[(2R)-2-amino-3-phenylpropyl]-N-(6-aminohexanoyl)-L-phenylalaninamide hydrochloride
Homo sapiens
-
-
0.097
N6-[(benzyloxy)carbonyl]-N-hydroxy-N2-(pyrazin-2-ylcarbonyl)-L-lysinamide
Homo sapiens
-
-
0.0912 - 0.0943
N6-[(benzyloxy)carbonyl]-N-hydroxy-N2-(pyridin-3-ylcarbonyl)-L-lysinamide
0.5696
N6-[(benzyloxy)carbonyl]-N-hydroxy-N2-[(2E)-3-phenylprop-2-enoyl]-L-lysinamide
Homo sapiens
-
-
0.0958
N6-[(benzyloxy)carbonyl]-N-hydroxy-N2-[(3-nitrophenyl)carbonyl]-L-lysinamide
Homo sapiens
-
-
0.1974
N6-[(benzyloxy)carbonyl]-N2-(pyrazin-2-ylcarbonyl)-L-lysine
Homo sapiens
-
-
0.1668 - 0.2196
N6-[(benzyloxy)carbonyl]-N2-(pyridin-3-ylcarbonyl)-L-lysine
0.1272
N6-[(benzyloxy)carbonyl]-N2-[(2,4-dichlorophenyl)carbonyl]-L-lysine
Homo sapiens
-
-
0.0132
N6-[(benzyloxy)carbonyl]-N2-[(2,4-dichlorophenyl)carbonyl]-N-hydroxy-L-lysinamide
Homo sapiens
-
-
0.2151
N6-[(benzyloxy)carbonyl]-N2-[(2E)-3-phenylprop-2-enoyl]-L-lysine
Homo sapiens
-
-
0.1108
N6-[(benzyloxy)carbonyl]-N2-[(3-nitrophenyl)carbonyl]-L-lysine
Homo sapiens
-
-
0.188
N6-[(benzyloxy)carbonyl]-N2-[(4-bromophenyl)carbonyl]-L-lysine
Homo sapiens
-
-
0.1119
N6-[(benzyloxy)carbonyl]-N2-[(4-bromophenyl)carbonyl]-N-hydroxy-L-lysinamide
Homo sapiens
-
-
0.00029
PAQ-22
Homo sapiens
-
IC50: 0.00029 mM, kidney enzyme
0.000015
phebestin
Homo sapiens
-
IC50: 0.000015 mM, kidney enzyme
0.000016 - 0.00005
probestin
0.007 - 0.018
psammaplin A
Homo sapiens
-
natural inhibitor isolated from a marine sponge, non-competitive, highly cytotoxic, IC50: 0.007-0.018 mM, overview
0.0031
puromycin
Homo sapiens
-
IC50: 0.0031 mM, kidney enzyme
0.000025
RB3014
Homo sapiens
-
IC50: 0.000025 mM, kidney enzyme
0.0498
[(3S)-2,6-dioxo-3-[[(3,4,5-trimethoxyphenyl)carbonyl]amino]piperidin-1-yl]acetic acid
Homo sapiens
-
-
0.025
[3-nitro-2-(2-nitrophenyl)-4-oxo-4H-chromen-8-yl]acetic acid
Homo sapiens
-
IC50: 0.025 mM
0.00071
[amino(phenyl)methyl](1-amino-3-phenylpropyl)phosphinic acid
Homo sapiens
-
-
0.0044 - 0.012
[amino(phenyl)methyl](1-hydroxy-3-methylbutyl)phosphinic acid
0.00024 - 0.00073
[amino(phenyl)methyl](1-hydroxy-3-phenylpropyl)phosphinic acid
0.0182 - 0.048
[amino(phenyl)methyl](1-hydroxyethyl)phosphinic acid
0.028
[amino(phenyl)methyl](1-hydroxypentyl)phosphinic acid
Homo sapiens
-
-
0.00055 - 0.0015
[amino(phenyl)methyl][hydroxy(phenyl)methyl]phosphinic acid
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.38
-
cell extract
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7.6
-
assay at, dependent on substrate used
6.75 - 7
-
substrate Ala-2-naphtylamide
7 - 7.5
7.2
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
assay at
32 - 37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
endothelial cell
Manually annotated by BRENDA team
in women with active exposure to tobacco smoke, a higher activity level of alanine aminopeptidase and gamma-glutamyltransferase in the plasma is found
Manually annotated by BRENDA team
fibroblast
Manually annotated by BRENDA team
endothelial cell
Manually annotated by BRENDA team
selective expression of APN/CD13
Manually annotated by BRENDA team
-
melanoma cell line
Manually annotated by BRENDA team
-
arterial smooth muscle
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
surrounding a lung tumor nest
Manually annotated by BRENDA team
-
highly invasive lung adenocarcinoma cell line, high expression level
Manually annotated by BRENDA team
-
has high levels of APN/CD13
Manually annotated by BRENDA team
-
keratinocyte cell line, high activity
Manually annotated by BRENDA team
-
neoplastic lievre tissue, canalicular pattern of the enzyme, overview
Manually annotated by BRENDA team
-
had low levels of APN/CD13
Manually annotated by BRENDA team
-
lung adenocarcinoma cell line
Manually annotated by BRENDA team
-
Kaposi sarkoma-derived endothelial cell
Manually annotated by BRENDA team
-
CD13 expression analysis, interstitial tissue, blood vessels, and fibroblasts surrounding the tumor nest
Manually annotated by BRENDA team
-
negative for expression of enzyme
Manually annotated by BRENDA team
-
prostate adenocarcinoma cell line
Manually annotated by BRENDA team
-
APN mRNA expression in hormone-refractory prostate cancer tissue is significantly lower than that in normal prostate tissue
Manually annotated by BRENDA team
-
retinal pericyte
Manually annotated by BRENDA team
-
arterial smooth muscle
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
memebrane-bound
Manually annotated by BRENDA team
-
mannose-rich precursor enzyme form
Manually annotated by BRENDA team
-
wild-type mature enzyme
Manually annotated by BRENDA team
additional information
-
intracellular distribution pattern
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
inhibiting the expression of LAP with siRNA decreases cell viability
physiological function
intracellular LAP plays a role in the intrinsic drug resistance to cisplatin in cancer cells
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
AMPN_HUMAN
967
1
109540
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
108000
-
2 * 108000, SDS-PAGE
110000
-
deduced from cDNA sequence
132000
-
2 * 132000
137000 - 153000
-
light scattering, native PAGE, SDS-PAGE
143000
-
SDS-PAGE
150000
160000
166000
-
1 * 170000, mannose-rich precursor, SDS-PAGE, 1 * 166000, complex glycosylated mature enzyme, SDS-PAGE, 1 * 190000, about, recombinant GFP-tagged complex glycosylated mature enzyme, SDS-PAGE
170000
-
1 * 170000, mannose-rich precursor, SDS-PAGE, 1 * 166000, complex glycosylated mature enzyme, SDS-PAGE, 1 * 190000, about, recombinant GFP-tagged complex glycosylated mature enzyme, SDS-PAGE
190000
-
1 * 170000, mannose-rich precursor, SDS-PAGE, 1 * 166000, complex glycosylated mature enzyme, SDS-PAGE, 1 * 190000, about, recombinant GFP-tagged complex glycosylated mature enzyme, SDS-PAGE
206000
-
gel filtration
210800
-
equilibrium centrifugation
240000
-
gel filtration
260000
-
the protein present in sera of patients with cholestatic diseases is later found to be a high molecular isoform of CD13 (260 kDa)
75000
-
2 * 75000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
homodimer
-
2 * 75000
monomer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
proteolytic modification
-
the enzyme is processed in the Golgi apparatus to form a homodimer and then exported by the endoplasmic reticulum
side-chain modification
-
glycoprotein, 11.6% carbohydrate
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E354G
-
almost complete loss of activity
E354I
-
almost complete loss of activity
E354Q
-
almost complete loss of activity
E388G
-
almost complete loss of activity
E410G
-
almost complete loss of activity
H387C/H391C
-
almost complete loss of activity
H387I/H391I
-
almost complete loss of activity
L243P
-
a natural mutation in the enzyme isolated from a patient suffering from leukemia leads to an arrest in the endoplasmic reticulum, the mutant is inactive at physiological temperatures of 32-37°C, persists as a mannose-rich proteinin the endoplasmic reticulum, and is degraded by a ER-associated degradation pathway, overview
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 10
-
stable
35875
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
-
stable for at least 30 min
55
-
stable for at least 30 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
resistant against several cycles of freezing and thawing
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-30óC, at least four months, stable
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, identification of six polymorphisms e.g. C956T, G978T, G987A, and C398T, allele frequency and haplotype identification, overview
expression in LLC-PK1 cell
expression of the enzyme in murine CMT93 cells and in transgenic mice
DNA and amino acid sequence determination and analysis, quantitativ expression analysis in monocytes and macrophages of percardial fluid
-
expressed in Escherichia coli
-
expression analysis
-
expression in HEK-293 cell
-
expression in HT-1080 cell
-
expression in human embryonic kidney cell
-
from an intestinal cDNA library, the gene is localized on chromosome 15, intestinal and myeloid epithelial cells use different promoters
-
gene mapping on chromosome 15q25-26, DNA and amino acid sequence analysis
-
overexpression in tumour cells
-
transient expression of wild-type and mutant enzymes in COS-1 cells, as GFP-tagged proteins, and in renal carcinoma N109 cells
-
transient expression of wild-type and mutant enzymes in murine BALB/3T3 fibroblasts, and stable expression in CL1-0 cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the rates of inhibition of APN expression by 0.004, 0.02, and 0.1 mM (S)-2-amino-N-((S)-1-(2-(hydroxyamino)-2-oxoethyl)-2,6-dioxopiperidin-3-yl)-3-phenylpropanamide are 26%, 59.1%, and 87.7%, respectively. Bestatin (0.1 mM) decreases the expression of APN in ES-2 cells by 62.4%
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
treatment of cell with aminopeptidase N siRNA increases total cellular Na+K+-ATPase activity and basolateral Na+K+-ATPase abundance about twofold. Overexpression of the enzyme reduces Na+K+-ATPase activity and basolateral abundance by 50%. The effect is mediated via angiotensin IV and angiotensin IV receptor signaling
diagnostics
drug development
medicine
pharmacology
-
the enzyme is a target for design of inhibitors acting as anti-hypertensive drugs
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Luciani, N.; Marie-Claire, C.; Ruffet, E.; Beaumont, A.; Roques, B.P.; Fournie-Zaluski, M.C.
Characterization of Glu350 as a critical residue involved in the N-terminal amine binding site of aminopeptidase N (EC 3.4.11.2): insights into its mechanism of action
Biochemistry
37
686-692
1998
Homo sapiens, Sus scrofa
Manually annotated by BRENDA team
Menrad, A.; Speicher, D.; Wacker, J.; Herlyn, M.
Biochemical and functional characterization of aminopeptidase N expressed by human melanoma cells
Cancer Res.
53
1450-1455
1993
Homo sapiens
Manually annotated by BRENDA team
Lalu, K.; Lampelo, S.; Vanha-Perttula, T.
Characterization of three aminopeptidases purified from maternal serum
Biochim. Biophys. Acta
873
190-197
1986
Homo sapiens
Manually annotated by BRENDA team
Huang, K.; Takahara, S.; Kinouchi, T.; Takeyama, M.; Ishida, T.; Ueyama, H.; Nishi, K.; Ohkubo, I.
Alanyl aminopeptidase from human seminal plasma: purification, characterization, and immunohistochemical localization in the male genital tract
J. Biochem.
122
779-787
1997
Homo sapiens
Manually annotated by BRENDA team
McClellan, J.B.; Garner, C.W.
Purification and properties of human intestine alanine aminopeptidase
Biochim. Biophys. Acta
613
160-167
1980
Homo sapiens
Manually annotated by BRENDA team
Olsen, J.; Cowell, G.M.; Konigshofer, E.; Danielsen, E.M.; Moller, J.; Laustsen, L.; Hansen, O.C.; Welinder, K.G.; Engberg, J.; Hunziker, W.; Spiess, M.; Sjstrm, H.; Noren, O.
Complete amino acid sequence of human intestinal aminopeptidase N as deduced from cloned cDNA
FEBS Lett.
238
307-314
1988
Homo sapiens
Manually annotated by BRENDA team
Tokioka-Terao, M.; Hiwada, K.; Kokubu, T.
Purification and characterization of aminopeptidase N from human plasma
Enzyme
32
65-75
1984
Homo sapiens
Manually annotated by BRENDA team
Bauvois, B.; Puiffe, M.L.; Bongui, J.B.; Paillat, S.; Monneret, C.; Dauzonne, D.
Synthesis and biological evaluation of novel flavone-8-acetic acid derivatives as reversible inhibitors of aminopeptidase N/CD13
J. Med. Chem.
46
3900-3913
2003
Homo sapiens
Manually annotated by BRENDA team
Acartuerk, F.; Parlatan, Z.I.; Saracoglu, O.F.
Comparison of vaginal aminopeptidase enzymatic activities in various animals and in humans
J. Pharm. Pharmacol.
53
1499-1504
2001
Cavia porcellus, Oryctolagus cuniculus, Ovis aries, Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Taracha, E.; Habrat, B.; Lehner, M.; Wislowska, A.; Woronowicz, B.T.; Bogulas, M.; Charewicz, J.; Markuszewski, C.; Plaznik, A.
Alanine aminopeptidase activity in urine: a new marker of chronic alcohol abuse?
Alcohol. Clin. Exp. Res.
28
729-735
2004
Homo sapiens
Manually annotated by BRENDA team
Lendeckel, U.; Bukowska, A.; Laettig, J.H.; Brandt, W.
Alanyl-aminopeptidases in human T cells. Structures and functions
Aminopeptidases in Biology and Disease (Hooper, N. M. ; Lendechel, U. , eds. )
2
201-227
2004
Homo sapiens
-
Manually annotated by BRENDA team
Iturrioz, X.; Reaux-Le Goazigo, A.; Llorens-Cortes, C.
Aminopeptidase inhibitors as anti-hypertensive drugs
Aminopeptidases in Biology and Disease (Hooper, N. M. ; Lendechel, U. , eds. )
2
229-250
2004
Homo sapiens
-
Manually annotated by BRENDA team
Thielitz, A.; Bukowska, A.; Wolke, C.; Vetter, R.; Lendeckel, U.; Wrenger, S.; Hashimoto, Y.; Ansorge, S.; Gollnick, H.; Reinhold, D.
Identification of extra- and intracellular alanyl aminopeptidases as new targets to modulate keratinocyte growth and differentiation
Biochem. Biophys. Res. Commun.
321
795-801
2004
Homo sapiens
Manually annotated by BRENDA team
Riemann, D.; Tcherkes, A.; Hansen, G.H.; Wulfaenger, J.; Blosz, T.; Danielsen, E.M.
Functional co-localization of monocytic aminopeptidase N/CD13 with the Fc gamma receptors CD32 and CD64
Biochem. Biophys. Res. Commun.
331
1408-1412
2005
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Fontijn, D.; Duyndam, M.C.; van Berkel, M.P.; Yuana, Y.; Shapiro, L.H.; Pinedo, H.M.; Broxterman, H.J.; Boven, E.
CD13/Aminopeptidase N overexpression by basic fibroblast growth factor mediates enhanced invasiveness of 1F6 human melanoma cells
Br. J. Cancer
94
1627-1636
2006
Homo sapiens
Manually annotated by BRENDA team
Fukasawa, K.; Fujii, H.; Saitoh, Y.; Koizumi, K.; Aozuka, Y.; Sekine, K.; Yamada, M.; Saiki, I.; Nishikawa, K.
Aminopeptidase N (APN/CD13) is selectively expressed in vascular endothelial cells and plays multiple roles in angiogenesis
Cancer Lett.
243
135-143
2006
Homo sapiens (P15144), Homo sapiens
Manually annotated by BRENDA team
Xu, W.; Li, Q.
Progress in the development of aminopeptidase N (APN/CD13) inhibitors
Curr. Med. Chem.
5
281-301
2005
Homo sapiens
Manually annotated by BRENDA team
Turner, A.J.
Membrane alanyl aminopeptidase
Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds. )
1
289-294
2004
Oryctolagus cuniculus, Homo sapiens, Lactococcus lactis, Lymantria dispar, Rattus norvegicus, Sus scrofa
-
Manually annotated by BRENDA team
Gabrilovac, J.; Cupic, B.; Breljak, D.; Zekusic, M.; Boranic, M.
Expression of CD13/aminopeptidase N and CD10/neutral endopeptidase on cultured human keratinocytes
Immunol. Lett.
91
39-47
2004
Homo sapiens
Manually annotated by BRENDA team
Chang, Y.W.; Chen, S.C.; Cheng, E.C.; Ko, Y.P.; Lin, Y.C.; Kao, Y.R.; Tsay, Y.G.; Yang, P.C.; Wu, C.W.; Roffler, S.R.
CD13 (aminopeptidase N) can associate with tumor-associated antigen L6 and enhance the motility of human lung cancer cells
Int. J. Cancer
116
243-252
2005
Homo sapiens
Manually annotated by BRENDA team
Vijgen, L.; Keyaerts, E.; Zlateva, K.; Van Ranst, M.
Identification of six new polymorphisms in the human coronavirus 229E receptor gene (aminopeptidase N/CD13)
Int. J. Infect. Dis.
8
217-222
2004
Homo sapiens (P15144), Homo sapiens
Manually annotated by BRENDA team
Kehlen, A.; Geisler, M.; Olsen, J.; Sablotzki, A.; Langner, J.; Riemann, D.
IL-10 and TGF-beta differ in their regulation of aminopeptidase N/CD13 expression in monocytes
Int. J. Mol. Med.
13
877-882
2004
Homo sapiens
Manually annotated by BRENDA team
Alfalah, M.; Krahn, M.P.; Wetzel, G.; von Horsten, S.; Wolke, C.; Hooper, N.; Kalinski, T.; Krueger, S.; Naim, H.Y.; Lendeckel, U.
A mutation in aminopeptidase N (CD13) isolated from a patient suffering from leukemia leads to an arrest in the endoplasmic reticulum
J. Biol. Chem.
281
11894-11900
2006
Homo sapiens
Manually annotated by BRENDA team
Cowburn, A.S.; Sobolewski, A.; Reed, B.J.; Deighton, J.; Murray, J.; Cadwallader, K.A.; Bradley, J.R.; Chilvers, E.R.
Aminopeptidase N (CD13) regulates tumor necrosis factor-alpha-induced apoptosis in human neutrophils
J. Biol. Chem.
281
12458-12467
2006
Homo sapiens
Manually annotated by BRENDA team
Roecken, C.; Licht, J.; Roessner, A.; Carl-McGrath, S.
Canalicular immunostaining of aminopeptidase N (CD13) as a diagnostic marker for hepatocellular carcinoma
J. Clin. Pathol.
58
1069-1075
2005
Homo sapiens
Manually annotated by BRENDA team
Mina-Osorio, P.; Ortega, E.
Aminopeptidase N (CD13) functionally interacts with FcgammaRs in human monocytes
J. Leukocyte Biol.
77
1008-1017
2005
Homo sapiens
Manually annotated by BRENDA team
Mina-Osorio, P.; Shapiro, L.H.; Ortega, E.
CD13 in cell adhesion: aminopeptidase N (CD13) mediates homotypic aggregation of monocytic cells
J. Leukocyte Biol.
79
719-730
2006
Homo sapiens
Manually annotated by BRENDA team
Kunii, R.; Nemoto, E.; Kanaya, S.; Tsubahara, T.; Shimauchi, H.
Expression of CD13/aminopeptidase N on human gingival fibroblasts and up-regulation upon stimulation with interleukin-4 and interleukin-13
J. Periodontal Res.
40
138-146
2005
Homo sapiens
Manually annotated by BRENDA team
Bauvois, B.; Dauzonne, D.
Aminopeptidase-N/CD13 (EC 3.4.11.2) inhibitors: chemistry, biological evaluations, and therapeutic prospects
Med. Res. Rev.
26
88-130
2006
Homo sapiens
Manually annotated by BRENDA team
Ichimura, E.; Yamada, M.; Nishikawa, K.; Abe, F.; Nakajima, T.
Immunohistochemical expression of aminopeptidase N (CD13) in human lung squamous cell carcinomas, with special reference to bestatin adjuvant therapy
Pathol. Int.
56
296-300
2006
Homo sapiens
Manually annotated by BRENDA team
Kasman, L.M.
CD13/aminopeptidase N and murine cytomegalovirus infection
Virology
334
1-9
2005
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Wentworth, D.E.; Tresnan, D.B.; Turner, B.C.; Lerman, I.R.; Bullis, B.; Hemmila, E.M.; Levis, R.; Shapiro, L.H.; Holmes, K.V.
Cells of human aminopeptidase N (CD13) transgenic mice are infected by human coronavirus-229E in vitro, but not in vivo
Virology
335
185-197
2005
Homo sapiens (P15144), Homo sapiens
Manually annotated by BRENDA team
Reinhold, D.; Biton, A.; Goihl, A.; Pieper, S.; Lendeckel, U.; Faust, J.; Neubert, K.; Bank, U.; Taeger, M.; Ansorge, S.; Brocke, S.
Dual inhibition of dipeptidyl peptidase IV and aminopeptidase N suppresses inflammatory immune responses
Ann. N. Y. Acad. Sci.
1110
402-409
2007
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Thielitz, A.; Reinhold, D.; Vetter, R.; Bank, U.; Helmuth, M.; Hartig, R.; Wrenger, S.; Wiswedel, I.; Lendeckel, U.; Kaehne, T.; Neubert, K.; Faust, J.; Zouboulis, C.C.; Ansorge, S.; Gollnick, H.
Inhibitors of dipeptidyl peptidase IV and aminopeptidase N target major pathogenetic steps in acne initiation
J. Invest. Dermatol.
127
1042-1051
2007
Homo sapiens
Manually annotated by BRENDA team
Kotlo, K.; Shukla, S.; Tawar, U.; Skidgel, R.A.; Danziger, R.S.
Aminopeptidase N reduces basolateral Na+ -K+ -ATPase in proximal tubule cells
Am. J. Physiol. Renal Physiol.
293
F1047-F1053
2007
Homo sapiens (P15144)
Manually annotated by BRENDA team
Garde, S.V.; Forte, A.J.; Ge, M.; Lepekhin, E.A.; Panchal, C.J.; Rabbani, S.A.; Wu, J.J.
Binding and internalization of NGR-peptide-targeted liposomal doxorubicin (TVT-DOX) in CD13-expressing cells and its antitumor effects
Anticancer Drugs
18
1189-1200
2007
Homo sapiens
Manually annotated by BRENDA team
Mina-Osorio, P.; Soto-Cruz, I.; Ortega, E.
A role for galectin-3 in CD13-mediated homotypic aggregation of monocytes
Biochem. Biophys. Res. Commun.
353
605-610
2007
Homo sapiens
Manually annotated by BRENDA team
Yang, E.; Shim, J.S.; Woo, H.J.; Kim, K.W.; Kwon, H.J.
Aminopeptidase N/CD13 induces angiogenesis through interaction with a pro-angiogenic protein, galectin-3
Biochem. Biophys. Res. Commun.
363
336-341
2007
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Petrovic, N.; Schacke, W.; Gahagan, J.R.; OConor, C.A.; Winnicka, B.; Conway, R.E.; Mina-Osorio, P.; Shapiro, L.H.
CD13/APN regulates endothelial invasion and filopodia formation
Blood
110
142-150
2007
Homo sapiens
Manually annotated by BRENDA team
Terauchi, M.; Kajiyama, H.; Shibata, K.; Ino, K.; Nawa, A.; Mizutani, S.; Kikkawa, F.
Inhibition of APN/CD13 leads to suppressed progressive potential in ovarian carcinoma cells
BMC Cancer
7
140
2007
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Tsukamoto, H.; Shibata, K.; Kajiyama, H.; Terauchi, M.; Nawa, A.; Kikkawa, F.
Aminopeptidase N (APN)/CD13 inhibitor, Ubenimex, enhances radiation sensitivity in human cervical cancer
BMC Cancer
8
74
2008
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Tokuhara, T.; Hattori, N.; Ishida, H.; Hirai, T.; Higashiyama, M.; Kodama, K.; Miyake, M.
Clinical significance of aminopeptidase N in non-small cell lung cancer
Clin. Cancer Res.
12
3971-3978
2006
Homo sapiens
Manually annotated by BRENDA team
Demaegdt, H.; Lenaerts, P.J.; Swales, J.; De Backer, J.P.; Laeremans, H.; Le, M.T.; Kersemans, K.; Vogel, L.K.; Michotte, Y.; Vanderheyden, P.; Vauquelin, G.
Angiotensin AT4 receptor ligand interaction with cystinyl aminopeptidase and aminopeptidase N: [125I]angiotensin IV only binds to the cystinyl aminopeptidase apo-enzyme
Eur. J. Pharmacol.
546
19-27
2006
Homo sapiens
Manually annotated by BRENDA team
Vanderheyden, P.M.; Demaegdt, H.; Swales, J.; Lenaerts, P.J.; De Backer, J.P.; Vogel, L.K.; Vauquelin, G.
Synergistic inhibition of the enzymatic activity of aminopeptidase N by divalent metal ion chelators
Fundam. Clin. Pharmacol.
20
613-619
2006
Homo sapiens, Sus scrofa
Manually annotated by BRENDA team
Kawamura, J.; Shimada, Y.; Kitaichi, H.; Komoto, I.; Hashimoto, Y.; Kaganoi, J.; Miyake, M.; Yamasaki, S.; Kondo, K.; Imamura, M.
Clinicopathological significance of aminopeptidase N/CD13 expression in human gastric carcinoma
Hepatogastroenterology
54
36-40
2007
Homo sapiens
Manually annotated by BRENDA team
Yamashita, M.; Kajiyama, H.; Terauchi, M.; Shibata, K.; Ino, K.; Nawa, A.; Mizutani, S.; Kikkawa, F.
Involvement of aminopeptidase N in enhanced chemosensitivity to paclitaxel in ovarian carcinoma in vitro and in vivo
Int. J. Cancer
120
2243-2250
2007
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Surowiak, P.; Drag, M.; Materna, V.; Suchocki, S.; Grzywa, R.; Spaczy?ski, M.; Dietel, M.; Oleksyszyn, J.; Zabel, M.; Lage, H.
Expression of aminopeptidase N/CD13 in human ovarian cancers
Int. J. Gynecol. Cancer
16
1783-1788
2006
Homo sapiens
Manually annotated by BRENDA team
Sonneck, K.; Baumgartner, C.; Rebuzzi, L.; Marth, K.; Chen, K.W.; Hauswirth, A.W.; Florian, S.; Vrtala, S.; Buehring, H.J.; Valenta, R.; Valent, P.
Recombinant allergens promote expression of aminopeptidase-N (CD13) on basophils in allergic patients
Int. J. Immunopathol. Pharmacol.
21
11-21
2008
Homo sapiens
Manually annotated by BRENDA team
Miki, T.; Takegami, Y.; Okawa, K.; Muraguchi, T.; Noda, M.; Takahashi, C.
The reversion-inducing cysteine-rich protein with Kazal motifs (RECK) interacts with membrane type 1 matrix metalloproteinase and CD13/aminopeptidase N and modulates their endocytic pathways
J. Biol. Chem.
282
12341-12352
2007
Homo sapiens
Manually annotated by BRENDA team
von Wallbrunn, A.; Waldeck, J.; Hoeltke, C.; Zuehlsdorf, M.; Mesters, R.; Heindel, W.; Schaefers, M.; Bremer, C.
In vivo optical imaging of CD13/APN-expression in tumor xenografts
J. Biomed. Opt.
13
011007
2008
Homo sapiens
Manually annotated by BRENDA team
Mina-Osorio, P.; Shapiro, L.H.; Ortega, E.
CD13 in cell adhesion: aminopeptidase N (CD13) mediates homotypic aggregation of monocytic cells
J. Leukoc. Biol.
79
719-730
2006
Homo sapiens
Manually annotated by BRENDA team
Axen, A.; Andersson, H.; Lindeberg, G.; Roennholm, H.; Kortesmaa, J.; Demaegdt, H.; Vauquelin, G.; Karlen, A.; Hallberg, M.
Small potent ligands to the insulin-regulated aminopeptidase (IRAP)/AT(4) receptor
J. Pept. Sci.
13
434-444
2007
Homo sapiens
Manually annotated by BRENDA team
Gera, L.; Fortin, J.; Adam, A.; Stewart, J.M.; Marceau, F.
Discovery of a dual-function peptide that combines aminopeptidase N inhibition and kinin B1 receptor antagonism
J. Pharmacol. Exp. Ther.
317
300-308
2006
Oryctolagus cuniculus, Homo sapiens
Manually annotated by BRENDA team
Wulfaenger, J.; Niedling, S.; Riemann, D.; Seliger, B.
Aminopeptidase N (APN)/CD13-dependent CXCR4 downregulation is associated with diminished cell migration, proliferation and invasion
Mol. Membr. Biol.
25
72-82
2008
Homo sapiens
Manually annotated by BRENDA team
Uehara, N.; Fujita, M.; Shimizu, T.
Colorimetric assay of aminopeptidase N activity based on inhibition of the disassembly of gold nano-composites conjugated with a thermo-responsive copolymer
Anal. Sci.
25
267-273
2009
Homo sapiens
Manually annotated by BRENDA team
Shim, J.S.; Park, H.M.; Lee, J.; Kwon, H.J.
Global and focused transcriptional profiling of small molecule aminopeptidase N inhibitor reveals its mechanism of angiogenesis inhibition
Biochem. Biophys. Res. Commun.
371
99-103
2008
Homo sapiens
Manually annotated by BRENDA team
Shang, L.; Fang, H.; Zhu, H.; Wang, X.; Wang, Q.; Mu, J.; Wang, B.; Kishioka, S.; Xu, W.
Design, synthesis and SAR studies of tripeptide analogs with the scaffold 3-phenylpropane-1,2-diamine as aminopeptidase N/CD13 inhibitors
Bioorg. Med. Chem.
17
2775-2784
2009
Homo sapiens
Manually annotated by BRENDA team
Mawrin, C.; Wolke, C.; Haase, D.; Krueger, S.; Firsching, R.; Keilhoff, G.; Paulus, W.; Gutmann, D.H.; Lal, A.; Lendeckel, U.
Reduced activity of CD13/aminopeptidase N (APN) in aggressive meningiomas is associated with increased levels of SPARC
Brain Pathol.
20
200-210
2009
Homo sapiens
Manually annotated by BRENDA team
Morikawa, T.; Xie, H.; Wang, T.; Matsuda, H.; Yoshikawa, M.
Acylated flavonol bisdesmosides, sinocrassosides A3-A7 and B3, with aminopeptidase N inhibitory activity from Sinocrassula indica
Chem. Biodivers.
6
411-420
2009
Homo sapiens
Manually annotated by BRENDA team
Morikawa, T.; Xie, H.; Wang, T.; Matsuda, H.; Yoshikawa, M.
Bioactive constituents from Chinese natural medicines. XXXII. aminopeptidase N and aldose reductase inhibitors from Sinocrassula indica: structures of sinocrassosides B4, B5, C1, and D1-D3
Chem. Pharm. Bull.
56
1438-1444
2008
Homo sapiens
Manually annotated by BRENDA team
Morikawa, T.; Funakoshi, K.; Ninomiya, K.; Yasuda, D.; Miyagawa, K.; Matsuda, H.; Yoshikawa, M.
Medicinal foodstuffs. XXXIV. Structures of new prenylchalcones and prenylflavanones with TNF-alpha and aminopeptidase N inhibitory activities from Boesenbergia rotunda
Chem. Pharm. Bull.
56
956-962
2008
Homo sapiens
Manually annotated by BRENDA team
Holdt, B.; Peters, E.; Nagel, H.R.; Steiner, M.
An automated assay of urinary alanine aminopeptidase activity
Clin. Chem. Lab. Med.
46
537-540
2008
Homo sapiens
Manually annotated by BRENDA team
Ansorge, S.; Bank, U.; Heimburg, A.; Helmuth, M.; Koch, G.; Tadje, J.; Lendeckel, U.; Wolke, C.; Neubert, K.; Faust, J.; Fuchs, P.; Reinhold, D.; Thielitz, A.; Taeger, M.
Recent insights into the role of dipeptidyl aminopeptidase IV (DPIV) and aminopeptidase N (APN) families in immune functions
Clin. Chem. Lab. Med.
47
253-261
2009
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
Stankovic, M.; Vlahovic, P.; Avramovic, V.; Todorovic, M.
Distribution of dipeptidyl peptidase IV in patients with chronic tonsillitis
Clin. Vaccine Immunol.
15
794-798
2008
Homo sapiens
Manually annotated by BRENDA team
Zhang, X.; Xu, W.
Aminopeptidase N (APN/CD13) as a target for anti-cancer agent design
Curr. Med. Chem.
15
2850-2865
2008
Homo sapiens
Manually annotated by BRENDA team
Gabrilovac, J.; Breljak, D.; Cupic, B.
Regulation of aminopeptidase N (EC 3.4.11.2; APN; CD13) on the HL-60 cell line by TGF-beta1
Int. Immunopharmacol.
8
613-623
2008
Homo sapiens
Manually annotated by BRENDA team
Cai, J.; Kehoe, O.; Smith, G.M.; Hykin, P.; Boulton, M.E.
The angiopoietin/Tie-2 system regulates pericyte survival and recruitment in diabetic retinopathy
Invest. Ophthalmol. Vis. Sci.
49
2163-2171
2008
Homo sapiens
Manually annotated by BRENDA team
Lukaszuk, A.; Demaegdt, H.; Szemenyei, E.; Toth, G.; Tymecka, D.; Misicka, A.; Karoyan, P.; Vanderheyden, P.; Vauquelin, G.; Tourwe, D.
Beta-homo-amino acid scan of angiotensin IV
J. Med. Chem.
51
2291-2296
2008
Homo sapiens
Manually annotated by BRENDA team
Kuehlmann, U.C.; Chwieralski, C.E.; van den Brule, S.; Roecken, C.; Reinhold, D.; Welte, T.; Buehling, F.
Modulation of cytokine production and silica-induced lung fibrosis by inhibitors of aminopeptidase N and of dipeptidyl peptidase-IV-related proteases
Life Sci.
84
1-11
2009
Homo sapiens
Manually annotated by BRENDA team
Li, S.H.; Li, G.; Huang, H.M.; Xiong, F.; Mai, X.; Kuang, B.H.; Liu, C.M.; Tu, G.G.
Synthesis of 1,3,4-thiadiazole derivatives as aminopeptidase N inhibitors
Pharmazie
64
67-70
2009
Homo sapiens
Manually annotated by BRENDA team
Teranishi, J.; Ishiguro, H.; Hoshino, K.; Noguchi, K.; Kubota, Y.; Uemura, H.
Evaluation of role of angiotensin III and aminopeptidases in prostate cancer cells
Prostate
68
1666-1673
2008
Homo sapiens
Manually annotated by BRENDA team
Mina-Osorio, P.
The moonlighting enzyme CD13: old and new functions to target
Trends Mol. Med.
14
361-371
2008
Homo sapiens
Manually annotated by BRENDA team
Grzywa, R.; Oleksyszyn, J.; Salvesen, G.S.; Drag, M.
Identification of very potent inhibitor of human aminopeptidase N (CD13)
Bioorg. Med. Chem. Lett.
20
2497-2499
2010
Homo sapiens, Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Inagaki, Y.; Tang, W.; Zhang, L.; Du, G.; Xu, W.; Kokudo, N.
Novel aminopeptidase N (APN/CD13) inhibitor 24F can suppress invasion of hepatocellular carcinoma cells as well as angiogenesis
Biosci. Trends
4
56-60
2010
Homo sapiens
Manually annotated by BRENDA team
Hausheer, F.H.; Parker, A.R.; Petluru, P.N.; Jair, K.W.; Chen, S.; Huang, Q.; Chen, X.; Ayala, P.Y.; Shanmugarajah, D.; Kochat, H.
Mechanistic study of BNP7787-mediated cisplatin nephroprotection: modulation of human aminopeptidase N
Cancer Chemother. Pharmacol.
67
381-391
2011
Homo sapiens
Manually annotated by BRENDA team
Saxena, A.; Rai, A.; Raina, V.; Seth, T.; Mitra, D.K.
Expression of CD13/aminopeptidase N in precursor B-cell leukemia: role in growth regulation of B cells
Cancer Immunol. Immunother.
59
125-135
2010
Homo sapiens
Manually annotated by BRENDA team
Cui, S.X.; Qu, X.J.; Gao, Z.H.; Zhang, Y.S.; Zhang, X.F.; Zhao, C.R.; Xu, W.F.; Li, Q.B.; Han, J.X.
Targeting aminopeptidase N (APN/CD13) with cyclic-imide peptidomimetics derivative CIP-13F inhibits the growth of human ovarian carcinoma cells
Cancer Lett.
292
153-162
2010
Homo sapiens
Manually annotated by BRENDA team
Gong, Q.; Shi, W.; Li, L.; Ma, H.
Leucine aminopeptidase may contribute to the intrinsic resistance of cancer cells toward cisplatin as revealed by an ultrasensitive fluorescent probe
Chem. Sci.
7
788-792
2016
Homo sapiens (P28838)
Manually annotated by BRENDA team
Bizon, A.; Milnerowicz, H.
The effect of passive and active exposure to tobacco smoke on lipid profile parameters and the activity of certain membrane enzymes in the blood of women in the first trimester of pregnancy
Environ. Toxicol. Pharmacol.
53
74-80
2017
Homo sapiens (P15144), Homo sapiens
Manually annotated by BRENDA team
Weglarz-Tomczak, E.; Berlicki, L.; Pawelczak, M.; Nocek, B.; Joachimiak, A.; Mucha, A.
A structural insight into the P1S1 binding mode of diaminoethylphosphonic and phosphinic acids, selective inhibitors of alanine aminopeptidases
Eur. J. Med. Chem.
117
187-196
2016
Homo sapiens (P15144), Neisseria meningitidis serogroup B (Q9JYV4), Neisseria meningitidis serogroup B MC58 (Q9JYV4)
Manually annotated by BRENDA team