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(S)-2-amino-4-cyclohexylbutanoyl-7-amido-4-methylcoumarin + H2O
(S)-2-amino-4-cyclohexylbutanoic acid + 7-amino-4-methylcoumarin
-
-
-
?
Ala-7-amido-4-methylcoumarin + H2O
alanine + 7-amino-4-methylcoumarin
-
-
-
?
Arg-Ala + H2O
L-Arg + L-Ala
-
-
-
-
?
Arg-Pro-Lys-Pro + H2O
Arg + Pro-Lys-Pro
Arg-Pro-Pro-Gly-Phe + H2O
Arg + Pro-Pro-Gly-Phe
-
bradikinin fragment 1-5, no hydrolysis of bradikinin
-
?
Arg-Tyr-Leu-Pro-Thr + H2O
?
-
insect neuropeptide
-
-
?
cholecystokinin octapeptide + H2O
tyrosine sulfate + Asp + Met + Gly + Trp + Met-Asp-Phe-NH2
-
i.e. Asp-tyrosyl sulfate-Met-Gly-Trp-Met-Asp-Phe-NH2
-
-
?
Gly-p-nitroanilide + H2O
Gly + p-nitroaniline
-
58.5% activity compared to L-Pro-p-nitroanilide
-
-
?
His-Ala + H2O
L-His + L-Ala
-
-
-
-
?
homoargininyl-7-amido-4-methylcoumarin + H2O
homoarginine + 7-amino-4-methylcoumarin
-
-
-
?
homophenylalanyl-7-amido-4-methylcoumarin + H2O
homophenylalanine + 7-amino-4-methylcoumarin
-
-
-
?
L-Ala 4-nitroanilide + H2O
L-Ala + 4-nitroaniline
-
-
-
?
L-Ala-p-nitroanilide + H2O
L-Ala + p-nitroaniline
-
55.4% activity compared to L-Pro-p-nitroanilide
-
-
?
L-alanyl-2-naphthylamide + H2O
L-alanine + 2-naphthylamine
-
-
-
?
L-Arg 4-nitroanilide + H2O
L-Arg + 4-nitroaniline
-
-
-
?
L-arginyl-2-naphthylamide + H2O
L-arginine + 2-naphthylamine
-
-
-
?
L-His-2-naphthylamide + H2O
L-His + 2-naphthylamine
-
31.6% activity compared to L-Pro-p-nitroanilide
-
-
?
L-Ile-2-naphthylamide + H2O
L-Ile + 2-naphthylamine
-
4.6% activity compared to L-Pro-p-nitroanilide
-
-
?
L-Leu 4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
-
-
?
L-Leu-4-methylumbelliferyl + H2O
L-leucine + 4-methylumbelliferol
-
-
-
-
?
L-Leu-4-nitroanilide + H2O
L-leucine + 4-nitroaniline
-
-
-
-
?
L-Leu-7-amido-4-methyl-coumarin + H2O
L-leucine + 7-amino-4-methyl-coumarin
-
-
-
?
L-Leu-7-amido-4-methylcoumarin + H2O
L-leucine + 7-amino-4-methylcoumarin
-
-
-
?
L-Leu-p-nitroanilide + H2O
L-Leu + p-nitroaniline
L-leucyl-7-amido-4-methylcoumarin + H2O
L-leucine + 7-amino-4-methylcoumarin
L-Lys 4-nitroanilide + H2O
L-Lys + 4-nitroaniline
-
-
-
?
L-Lys-p-nitroanilide + H2O
L-Lys + p-nitroaniline
-
13% activity compared to L-Pro-p-nitroanilide
-
-
?
L-Met-p-nitroanilide + H2O
L-Met + p-nitroaniline
-
11.5% activity compared to L-Pro-p-nitroanilide
-
-
?
L-methionyl-7-amido-4-methylcoumarin + H2O
L-methionine + 7-amino-4-methylcoumarin
-
-
-
?
L-Phe-p-nitroanilide + H2O
L-Phe + p-nitroaniline
-
1.1% activity compared to L-Pro-p-nitroanilide
-
-
?
L-Pro-2-naphthylamide + H2O
L-Pro + 2-naphthylamine
-
100% activity
-
-
?
L-Pro-p-nitroanilide + H2O
L-Pro + p-nitroaniline
-
100% activity
-
-
?
L-Ser-2-naphthylamide + H2O
L-Ser + 2-naphthylamine
-
64% activity compared to L-Pro-2-naphthylamide
-
-
?
L-Trp-2-naphthylamide + H2O
L-Trp + 2-naphthylamine
-
15.6% activity compared to L-Pro-p-nitroanilide
-
-
?
L-Tyr-2-naphthylamide + H2O
L-Tyr + 2-naphthylamine
-
30.3% activity compared to L-Pro-p-nitroanilide
-
-
?
L-Val-p-nitroanilide + H2O
L-Val + p-nitroaniline
-
5.3% activity compared to L-Pro-p-nitroanilide
-
-
?
Leu 4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
Leu 4-nitroanilide + H2O
?
-
-
-
-
?
Leu-Ala + H2O
L-Leu + L-Ala
-
-
-
-
?
Leu-enkephalin + H2O
?
-
i.e. Tyr-Gly-Gly-Phe-Met, stepwise degradation from the N-terminus
-
-
?
Leu-Gly + H2O
L-Leu + Gly
-
-
-
-
?
Leu-Gly-Gly + H2O
?
-
-
-
-
?
Leu-Gly-Leu + H2O
?
-
-
-
-
?
Leu-Gly-NH2 + H2O
?
-
-
-
-
?
Leu-Gly-Pro + H2O
?
-
-
-
-
?
Leu-Leu + H2O
2 L-Leu
-
-
-
?
Leu-Leu-Tyr + H2O
Leu + Leu-Tyr
-
-
-
-
?
Leu-NH2 + H2O
L-Leu + NH3
-
-
-
-
?
Leu-Pro-Leu-Arg-Phe-NH2 + H2O
Leu + Pro-Leu-Arg-Phe-NH2
-
a chicken brain pentapeptide
-
-
?
Leu-Pro-Leu-Arg-PheNH2 + H2O
Leu + Pro-Leu-Arg-PheNH2
-
i.e. chicken brain peptide
resistant to the enzyme
?
Lys-Ala + H2O
L-Lys + L-Ala
-
-
-
-
?
Lys-Ala-Met-Cys-Ala + H2O
?
-
-
-
-
?
Lys-Phe-Ile-Gly-Leu-Met-NH2 + H2O
?
-
eledoisin-related peptide, lysine, phenylalanine, isoleucine, glycine and leucine are liberated from the aminoterminus, methionine is not released from Met-NH2 of the final product
-
-
?
Met-Phe + H2O
L-Met + Phe
-
-
-
?
N-Formyl-Met-Leu-Phe + H2O
N-Formyl-Met + Leu-Phe
-
-
-
-
?
norleucyl-7-amido-4-methylcoumarin + H2O
norleucine + 7-amino-4-methylcoumarin
-
-
-
?
norvalinyl-7-amido-4-methylcoumarin + H2O
norvaline + 7-amino-4-methylcoumarin
-
-
-
?
Pro-Phe-Gly-Lys + 2 H2O
Pro + Phe + Gly-Lys
-
-
-
-
?
Pro-Phe-Gly-Lys + H2O
Pro + Phe-Gly-Lys
-
-
-
?
proctolin + H2O
?
-
-
-
-
?
styryl-Ala-7-amido-4-methylcoumarin + H2O
styryl-alanine + 7-amino-4-methylcoumarin
-
-
-
?
tuftsin + H2O
?
-
-
-
-
?
additional information
?
-
Arg-Pro-Lys-Pro + H2O
Arg + Pro-Lys-Pro
-
i.e. , substance P fragment 1-4, hydrolysis of the N-terminal Xaa-bond, no hydrolysis of substance P
-
?
Arg-Pro-Lys-Pro + H2O
Arg + Pro-Lys-Pro
-
substance P fragment 1-4
-
-
?
L-Leu-p-nitroanilide + H2O
L-Leu + p-nitroaniline
-
-
-
-
?
L-Leu-p-nitroanilide + H2O
L-Leu + p-nitroaniline
-
-
-
-
?
L-Leu-p-nitroanilide + H2O
L-Leu + p-nitroaniline
-
8.2% activity compared to L-Pro-p-nitroanilide
-
-
?
L-leucyl-7-amido-4-methylcoumarin + H2O
L-leucine + 7-amino-4-methylcoumarin
-
-
-
-
?
L-leucyl-7-amido-4-methylcoumarin + H2O
L-leucine + 7-amino-4-methylcoumarin
-
-
-
?
additional information
?
-
-
broad specificity for amino acid residues at P1 position, not: Pro-Leu-GlyNH2, schistoFMRF-amide (Pro-Asp-Val-Asp-His-Val-Phe-Leu-Arg-PheNH2), melanocyte-stimulating hormone release-inhibiting factor, Leu-Pro-Thr, Lys-Pro-Arg, Ala-Pro, Gly-Pro, Leu-Pro, Met-Pro, Phe-Pro, alpha-bag cell peptide (Ala-Pro-Arg-Leu-Arg-Phe-Tyr-Ser-Leu)
-
-
?
additional information
?
-
-
the enzyme functiones in regulation of hormone function and thus is involved in diverse biological processes, it offers a biodefense against the infectious microbial product N-formyl-peptide
-
-
?
additional information
?
-
-
the enzyme has a broad specificity for N-terminal amino acids residues at the P1 position of substrates, it degrades hydrophobic, basic, and acidic amino acids including proline, no activity with substance P and melanocyte-stimulating hormone release-inhibiting factor, i.e. Pro-Leu-Gly-NH2
-
-
?
additional information
?
-
-
both S1 and S1' subsite exhibit a preference for basic and hydrophobic side chains over polar and acidic side chains. The relative specificity of the S1 subsite is similar over the pH range 5.5-7.5. Substrate P1 and P1' residues affect both Km and kcat, revealing that side chain-subsite interactions not only drive the formation of the Michaelis complex but also influence the rates of ensuing chemical steps. There is no correlation between S1 and S1' specificities and amino acid abundance in hemoglobin. Interactions between PfA-M1 and the backbone atoms of the P1' and P2' residues as well as the P2' side chain further contribute to the catalytic efficiency of substrate hydrolysis
-
-
?
additional information
?
-
no substrates: Ile-4-nitroanilide, Val-4-nitroanilide, Gly-4-nitroanilide, Pro-4-nitroanilide
-
-
?
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(2S,17S,20S,21R)-21-amino-5-(4-benzoylbenzyl)-2-[4-(hex-5-ynoylamino)butyl]-20-hydroxy-17-(naphthalen-2-ylmethyl)-4,7,16,19-tetraoxo-22-phenyl-9,12-dioxa-3,6,15,18-tetraazadocosan-1-amide
-
1-hydroxy-2-oxo-1,2-dihydro-quinoline-3-carboxylic acid (4-phenyl-butyl)-amide
-
-
1-hydroxy-2-oxo-1,2-dihydro-quinoline-3-carboxylic acid 4-fluoro-benzylamide
-
-
2-(4-benzyl-piperidine-1-carbonyl)-4-methyl-pentanoic acid hydroxyamide
-
-
2-benzyl-3-(3,4-dihydro-1H-isoquinolin-2-yl)-N-hydroxy-3-oxo-propionamide
-
-
2-benzyl-3-(4-benzyl-piperazin-1-yl)-N-hydroxy-3-oxo-propionamide
-
-
2-benzyl-3-(4-benzyl-piperidin-1-yl)-N-hydroxy-3-oxo-propionamide
-
-
2-benzyl-N-(2,2-diphenyl-ethyl)-N'-hydroxy-malonamide
-
-
2-benzyl-N-(4-chloro-benzyl)-N'-hydroxy-malonamide
-
-
2-benzyl-N-(4-fluoro-benzyl)-N'-hydroxy-malonamide
-
-
2-benzyl-N-biphenyl-3-ylmethyl-N'-hydroxy-malonamide
-
-
2-benzyl-N-hydroxy-N'-(2-methyl-benzyl)-malonamide
-
-
2-benzyl-N-hydroxy-N'-(3-phenoxy-benzyl)-malonamide
-
-
2-benzyl-N-hydroxy-N'-(3-phenyl-propyl)-malonamide
-
-
2-benzyl-N-hydroxy-N'-(4-phenyl-butyl)-malonamide
-
-
2-benzyl-N-hydroxy-N'-indan-2-yl-malonamide
-
-
2-benzyl-N-hydroxy-N'-naphthalen-1-ylmethyl-malonamide
-
-
2-benzyl-N-hydroxy-N'-phenethyl-malonamide
-
-
2N-dibenzyl-N'-hydroxy-malonamide
-
-
3-(3,4-dihydro-1H-isoquinolin-2-yl)-N-hydroxy-3-oxo-2-(3-phenoxy-benzyl)-propionamide
-
-
3-(4-benzyl-piperidin-1-yl)-N-hydroxy-3-oxo-2-(3-phenoxybenzyl)-propionamide
-
-
betaine
-
complete inhibition at 2 mM
hPhe-PSI[PO2CH2]-Phe
phosphinic dipeptide analog
N-(1-(4-(1H-pyrazol-1-yl)phenyl)-2-(hydroxyamino)-2-oxoethyl)-3-aminobenzamide
highly effective against the malaria parasites, IC50 values of 233 nM; highly effective against the malaria parasites, IC50 values of 233 nM
N-(1-(4-(1H-pyrazol-1-yl)phenyl)-2-(hydroxyamino)-2-oxoethyl)-4-aminobenzamide
highly effective against the malaria parasites, IC50 values of 283 nM; highly effective against the malaria parasites, IC50 values of 283 nM
N-(1-(4-(1H-pyrazol-1-yl)phenyl)-2-(hydroxyamino)-2-oxoethyl)-pivalamide
most effective inhibitor of isoform M1 and one of the more potent inhibitors of isoform M17 tested, the most effective compound against 3D7 malaria parasites, with an IC50 of 227 nM; most effective inhibitor of isoform M1 and one of the more potent inhibitors of isoform M17 tested, the most effective compound against 3D7 malaria parasites, with an IC50 of 227 nM
N-(4-chloro-benzyl)-N'-hydroxy-2-(3-phenoxy-benzyl)-malonamide
-
-
N-(4-chloro-benzyl)-N'-hydroxy-2-isobutyl-malonamide
-
-
N-(4-fluoro-benzyl)-N'-hydroxy-2-isobutyl-malonamide
-
-
N-(4-fluoro-benzyl)-N'-hydroxy-2-[1-phenyl-meth-(E)-ylidene]-malonamide
-
-
N-(4-fluoro-benzyl)-N'-hydroxy-2-[1-phenyl-meth-(Z)-ylidene]-malonamide
-
-
N-benzyl-N'-hydroxy-2-(3-phenoxy-benzyl)-malonamide
-
-
N-benzyl-N'-hydroxy-2-isobutyl-malonamide
-
in Tris-HCl buffer (25 mM, pH 7.4), at 25°C
N-hydroxy-2-(3-phenoxy-benzyl)-N'-(3-phenyl-propyl)-malonamide
-
-
N-hydroxy-2-(3-phenoxy-benzyl)-N'-(4-phenyl-butyl)-malonamide
-
-
N-hydroxy-2-(3-phenoxy-benzyl)-N'-(4-trifluoromethyl-benzyl)-malonamide
-
-
N-hydroxy-2-isobutyl-N'-(1,2,3,4-tetrahydro-naphthalen-1-yl)-malonamide
-
-
N-hydroxy-2-isobutyl-N'-(3-phenoxy-benzyl)-malonamide
-
-
N-hydroxy-2-isobutyl-N'-(3-phenyl-propyl)-malonamide
-
-
N-hydroxy-2-isobutyl-N'-(4-phenyl-butyl)-malonamide
-
-
N-hydroxy-2-isobutyl-N'-naphthalen-1-ylmethyl-malonamide
-
-
N-hydroxy-2-isobutyl-N'-phenethyl-malonamide
-
-
N-hydroxy-N'-(4-phenyl-butyl)-2-[1-phenyl-meth-(Z)-ylidene]-malonamide
-
-
N-[(2-[2-[(N-[(2S,3R)-3-amino-4-[4-(benzyloxy)phenyl]-2-hydroxybutanoyl]-L-alanyl)amino]ethoxy]ethoxy)acetyl]-4-benzoylphenylalanyl-N6-hex-5-ynoyl-L-lysinamide
-
N-[(2S,3R)-3-amino-2-hydroxy-4-(4-methoxyphenyl)butanoyl]-L-leucine
-
-
N-[(2S,3R)-3-amino-2-hydroxy-4-(naphthalen-2-yl)butanoyl]-L-leucine
-
-
N-[(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl]-L-norleucine
-
-
N-[(2S,3R)-3-amino-2-hydroxyheptanoyl]-L-leucine
-
-
N-[(2S,3R)-3-amino-4-[4-(benzyloxy)phenyl]-2-hydroxybutanoyl]-L-leucine
-
-
N2-[(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl]-N6-[(benzyloxy)carbonyl]-L-lysine
-
-
tert-butyl (1-(4-(1H-Pyrazol-1-yl)phenyl)-2-(hydroxyamino)-2-oxoethyl)carbamate
compound shows good in vitro inhibitory properties, but IC50 for parasite growth is only 783 nM, suggesting that compounds substituted with the N-Boc group are either less capable of cellular penetration or less stable than the corresponding N-acyl derivatives; compound shows good in vitro inhibitory properties, but IC50 for parasite growth is only 783 nM, suggesting that compounds substituted with the N-Boc group are either less capable of cellular penetration or less stable than the corresponding N-acyl derivatives
tosedostat
i.e. (2S)-([(2R)-2-[(1S)-1-hydroxy-2-(hydroxyamino)-2-oxoethyl]-4-methylpentanoyl]amino)(phenyl)ethanoic acid, crystal structure; i.e. (2S)-({(2R)-2-[(1S)-1-hydroxy-2-(hydroxyamino)-2-oxoethyl]-4-methylpentanoyl}amino)(phenyl)ethanoic acid, crystal structure
Zn2+
0.1 mM, 80% inhibition
1,10-phenanthroline
treatment with 1,10-ortho-phenanthroline in order to deplete metal ions, results in a residual activity of about 8% compared to the initial activity. Activity is partially restored by the addition of divalent metal cations with Zn2+ being the most potent
1,10-phenanthroline
-
complete inhibition at 2 mM
1,10-phenanthroline
1 mM, 80% inhibition
bestatin
-
-
EDTA
-
complete inhibition after dialysis for 24 h and 4°C against 1 mM EDTA
OF 4949-II
-
complete inhibition at 0.1 mM
OF 4949-II
-
substance produced by Penicillium rugulosum, CAS: [93375-50-9]
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Anemia
IgG antibody response against Plasmodium falciparum aminopeptidase 1 antigen in Gabonese children living in Makokou and Franceville.
Infections
IgG antibody response against Plasmodium falciparum aminopeptidase 1 antigen in Gabonese children living in Makokou and Franceville.
Infections
Two-pronged attack: dual inhibition of Plasmodium falciparum M1 and M17 metalloaminopeptidases by a novel series of hydroxamic acid-based inhibitors.
Malaria
Distribution and Biochemical Properties of an M1-family Aminopeptidase in Plasmodium falciparum Indicate a Role in Vacuolar Hemoglobin Catabolism.
Malaria
KBE009: An antimalarial bestatin-like inhibitor of the Plasmodium falciparum M1 aminopeptidase discovered in an Ugi multicomponent reaction-derived peptidomimetic library.
Malaria
Selective inhibition of PfA-M1, over PfA-M17, by an amino-benzosuberone derivative blocks malaria parasites development in vitro and in vivo.
Malaria
Structure of the Plasmodium falciparum M17 aminopeptidase and significance for the design of drugs targeting the neutral exopeptidases.
Malaria
Synthesis and structure-activity relationships of phosphonic arginine mimetics as inhibitors of the M1 and M17 aminopeptidases from Plasmodium falciparum.
Malaria
Synthesis of new (-)-bestatin-based inhibitor libraries reveals a novel binding mode in the s1 pocket of the essential malaria m1 metalloaminopeptidase.
Malaria
Two cap residues in the S1 subsite of a Plasmodium falciparum M1-family aminopeptidase promote broad specificity and enhance catalysis.
Malaria
X-ray crystal structures of an orally available aminopeptidase inhibitor, Tosedostat, bound to anti-malarial drug targets PfA-M1 and PfA-M17.
Malaria, Falciparum
X-ray crystal structures of an orally available aminopeptidase inhibitor, Tosedostat, bound to anti-malarial drug targets PfA-M1 and PfA-M17.
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0.0236
(S)-2-amino-4-cyclohexylbutanoyl-7-amido-4-methylcoumarin
pH 7.4, 37°C
0.0598
Ala-7-amido-4-methylcoumarin
pH 7.4, 37°C
0.0277
homoargininyl-7-amido-4-methylcoumarin
pH 7.4, 37°C
0.0262
homophenylalanyl-7-amido-4-methylcoumarin
pH 7.4, 37°C
0.304
L-Ala 4-nitroanilide
pH 7.2, 37°C
0.21 - 4.4
L-alanyl-2-naphthylamide
0.27
L-Arg 4-nitroanilide
pH 7.2, 37°C
0.086 - 1.1
L-arginyl-2-naphthylamide
0.248
L-Lys 4-nitroanilide
pH 7.2, 37°C
0.0314
L-methionyl-7-amido-4-methylcoumarin
pH 7.4, 37°C
0.01 - 0.8
Leu 4-methylcoumarin 7-amide
0.95
Leu-Gly
-
pH 7.5, 30°C
0.7
Leu-Gly-Gly
-
pH 7.5, 30°C
0.015
Leu-Gly-Leu
-
pH 7.5, 30°C
0.42
Leu-Gly-NH2
-
pH 7.5, 30°C
0.2
Leu-Gly-Pro
-
pH 7.5, 30°C
4.9
Leu-NH2
-
pH 7.5, 30°C
0.58
Leu-Pro-Leu-Arg-PheNH2
-
-
0.0165
norleucyl-7-amido-4-methylcoumarin
pH 7.4, 37°C
0.0354
norvalinyl-7-amido-4-methylcoumarin
pH 7.4, 37°C
0.0302
styryl-Ala-7-amido-4-methylcoumarin
pH 7.4, 37°C
0.4
Arg-Ala
-
pH 7.5, 30°C
4.2
His-Ala
-
pH 7.5, 30°C
35
His-Ala
-
pH 5.5, 30°C
0.21
L-alanyl-2-naphthylamide
recombinant protein, pH 7.5, 37°C
4.4
L-alanyl-2-naphthylamide
recombinant protein, pH 5.5, 37°C
0.086
L-arginyl-2-naphthylamide
p68/p35 complex, pH 7.5, 37°C
0.11
L-arginyl-2-naphthylamide
p120, pH 7.5, 37°C
0.17
L-arginyl-2-naphthylamide
recombinant protein, pH 7.5, 37°C
1.1
L-arginyl-2-naphthylamide
recombinant protein, pH 5.5, 37°C
0.01
Leu 4-methylcoumarin 7-amide
-
plasma enzyme
0.8
Leu 4-methylcoumarin 7-amide
-
granule enzyme
0.64
Leu-Ala
-
pH 7.5, 30°C
10
Leu-Ala
-
pH 5.5, 30°C
0.13
Leu-Leu
recombinant protein, pH 7.5, 37°C
0.41
Leu-Leu
recombinant protein, pH 5.5, 37°C
1.2
Leu-Leu
recombinant protein, pH 5.0, 37°C
0.43
Lys-Ala
-
pH 7.5, 30°C
8.9
Lys-Ala
-
pH 5.5, 30°C
0.022
Met-Phe
recombinant protein, pH 7.5, 37°C
0.065
Met-Phe
recombinant protein, pH 5.5, 37°C
0.38
Met-Phe
recombinant protein, pH 5.0, 37°C
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0.000029 - 0.00033
(2S,17S,20S,21R)-21-amino-5-(4-benzoylbenzyl)-2-[4-(hex-5-ynoylamino)butyl]-20-hydroxy-17-(naphthalen-2-ylmethyl)-4,7,16,19-tetraoxo-22-phenyl-9,12-dioxa-3,6,15,18-tetraazadocosan-1-amide
0.000025 - 0.0038
bestatin
0.00048
bestatin methyl ester
0.000013
hPhe-PSI[PO2CH2]-Phe
pH and temperature not specified in the publication
0.000014 - 0.0055
N-(1-(4-(1H-pyrazol-1-yl)phenyl)-2-(hydroxyamino)-2-oxoethyl)-3-aminobenzamide
0.000011 - 0.0074
N-(1-(4-(1H-pyrazol-1-yl)phenyl)-2-(hydroxyamino)-2-oxoethyl)-4-aminobenzamide
0.000028 - 0.0007
N-(1-(4-(1H-pyrazol-1-yl)phenyl)-2-(hydroxyamino)-2-oxoethyl)-pivalamide
0.00026 - 0.004
N-[(2-[2-[(N-[(2S,3R)-3-amino-4-[4-(benzyloxy)phenyl]-2-hydroxybutanoyl]-L-alanyl)amino]ethoxy]ethoxy)acetyl]-4-benzoylphenylalanyl-N6-hex-5-ynoyl-L-lysinamide
0.000043
N-[(2S,3R)-3-amino-2-hydroxy-4-(4-methoxyphenyl)butanoyl]-L-leucine
-
pH 7.5, temperature not specified in the publication
0.003
N-[(2S,3R)-3-amino-2-hydroxy-4-(naphthalen-2-yl)butanoyl]-L-leucine
-
pH 7.5, temperature not specified in the publication
0.0009
N-[(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl]-L-norleucine
-
pH 7.5, temperature not specified in the publication
0.0053
N-[(2S,3R)-3-amino-2-hydroxyheptanoyl]-L-leucine
-
pH 7.5, temperature not specified in the publication
0.00049
N-[(2S,3R)-3-amino-4-[4-(benzyloxy)phenyl]-2-hydroxybutanoyl]-L-leucine
-
pH 7.5, temperature not specified in the publication
0.00145
N2-[(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl]-N6-[(benzyloxy)carbonyl]-L-lysine
-
pH 7.5, temperature not specified in the publication
0.00003 - 0.0008
tert-butyl (1-(4-(1H-Pyrazol-1-yl)phenyl)-2-(hydroxyamino)-2-oxoethyl)carbamate
0.000029
(2S,17S,20S,21R)-21-amino-5-(4-benzoylbenzyl)-2-[4-(hex-5-ynoylamino)butyl]-20-hydroxy-17-(naphthalen-2-ylmethyl)-4,7,16,19-tetraoxo-22-phenyl-9,12-dioxa-3,6,15,18-tetraazadocosan-1-amide
pH 7.5, temperature not specified in the publication
0.00033
(2S,17S,20S,21R)-21-amino-5-(4-benzoylbenzyl)-2-[4-(hex-5-ynoylamino)butyl]-20-hydroxy-17-(naphthalen-2-ylmethyl)-4,7,16,19-tetraoxo-22-phenyl-9,12-dioxa-3,6,15,18-tetraazadocosan-1-amide
pH 7.5, temperature not specified in the publication
0.000025
bestatin
pH and temperature not specified in the publication
0.00012
bestatin
pH 7.5, 37°C
0.00019
bestatin
-
pH 7.5, temperature not specified in the publication
0.0038
bestatin
pH 5.5, 37°C
0.00048
bestatin methyl ester
pH 7.5, 37°C
0.00048
bestatin methyl ester
pH 5.5, 37°C
0.000014
N-(1-(4-(1H-pyrazol-1-yl)phenyl)-2-(hydroxyamino)-2-oxoethyl)-3-aminobenzamide
pH 8.0, 37°C
0.0055
N-(1-(4-(1H-pyrazol-1-yl)phenyl)-2-(hydroxyamino)-2-oxoethyl)-3-aminobenzamide
pH 8.0, 37°C
0.000011
N-(1-(4-(1H-pyrazol-1-yl)phenyl)-2-(hydroxyamino)-2-oxoethyl)-4-aminobenzamide
pH 8.0, 37°C
0.0074
N-(1-(4-(1H-pyrazol-1-yl)phenyl)-2-(hydroxyamino)-2-oxoethyl)-4-aminobenzamide
pH 8.0, 37°C
0.000028
N-(1-(4-(1H-pyrazol-1-yl)phenyl)-2-(hydroxyamino)-2-oxoethyl)-pivalamide
pH 8.0, 37°C
0.0007
N-(1-(4-(1H-pyrazol-1-yl)phenyl)-2-(hydroxyamino)-2-oxoethyl)-pivalamide
pH 8.0, 37°C
0.00026
N-[(2-[2-[(N-[(2S,3R)-3-amino-4-[4-(benzyloxy)phenyl]-2-hydroxybutanoyl]-L-alanyl)amino]ethoxy]ethoxy)acetyl]-4-benzoylphenylalanyl-N6-hex-5-ynoyl-L-lysinamide
pH 7.5, temperature not specified in the publication
0.004
N-[(2-[2-[(N-[(2S,3R)-3-amino-4-[4-(benzyloxy)phenyl]-2-hydroxybutanoyl]-L-alanyl)amino]ethoxy]ethoxy)acetyl]-4-benzoylphenylalanyl-N6-hex-5-ynoyl-L-lysinamide
pH 7.5, temperature not specified in the publication
0.00003
tert-butyl (1-(4-(1H-Pyrazol-1-yl)phenyl)-2-(hydroxyamino)-2-oxoethyl)carbamate
pH 8.0, 37°C
0.0008
tert-butyl (1-(4-(1H-Pyrazol-1-yl)phenyl)-2-(hydroxyamino)-2-oxoethyl)carbamate
pH 8.0, 37°C
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0.01
1-hydroxy-2-oxo-1,2-dihydro-quinoline-3-carboxylic acid (4-phenyl-butyl)-amide
Plasmodium falciparum
-
IC50 above 0.01 mM, in Tris-HCl buffer (25 mM, pH 7.4), at 25°C
0.01
1-hydroxy-2-oxo-1,2-dihydro-quinoline-3-carboxylic acid 4-fluoro-benzylamide
Plasmodium falciparum
-
IC50 above 0.01 mM, in Tris-HCl buffer (25 mM, pH 7.4), at 25°C
0.000406
2-(4-benzyl-piperidine-1-carbonyl)-4-methyl-pentanoic acid hydroxyamide
Plasmodium falciparum
-
in Tris-HCl buffer (25 mM, pH 7.4), at 25°C
0.000253
2-benzyl-3-(3,4-dihydro-1H-isoquinolin-2-yl)-N-hydroxy-3-oxo-propionamide
Plasmodium falciparum
-
in Tris-HCl buffer (25 mM, pH 7.4), at 25°C
0.00176
2-benzyl-3-(4-benzyl-piperazin-1-yl)-N-hydroxy-3-oxo-propionamide
Plasmodium falciparum
-
in Tris-HCl buffer (25 mM, pH 7.4), at 25°C
0.000206
2-benzyl-3-(4-benzyl-piperidin-1-yl)-N-hydroxy-3-oxo-propionamide
Plasmodium falciparum
-
in Tris-HCl buffer (25 mM, pH 7.4), at 25°C
0.005363
2-benzyl-N-(2,2-diphenyl-ethyl)-N'-hydroxy-malonamide
Plasmodium falciparum
-
in Tris-HCl buffer (25 mM, pH 7.4), at 25°C
0.00017
2-benzyl-N-(4-chloro-benzyl)-N'-hydroxy-malonamide
Plasmodium falciparum
-
in Tris-HCl buffer (25 mM, pH 7.4), at 25°C
0.000027
2-benzyl-N-(4-fluoro-benzyl)-N'-hydroxy-malonamide
Plasmodium falciparum
-
in Tris-HCl buffer (25 mM, pH 7.4), at 25°C
0.001168
2-benzyl-N-biphenyl-3-ylmethyl-N'-hydroxy-malonamide
Plasmodium falciparum
-
in Tris-HCl buffer (25 mM, pH 7.4), at 25°C
0.000041
2-benzyl-N-hydroxy-N'-(2-methyl-benzyl)-malonamide
Plasmodium falciparum
-
in Tris-HCl buffer (25 mM, pH 7.4), at 25°C
0.002515
2-benzyl-N-hydroxy-N'-(3-phenoxy-benzyl)-malonamide
Plasmodium falciparum
-
in Tris-HCl buffer (25 mM, pH 7.4), at 25°C
0.000125
2-benzyl-N-hydroxy-N'-(3-phenyl-propyl)-malonamide
Plasmodium falciparum
-
in Tris-HCl buffer (25 mM, pH 7.4), at 25°C
0.000046
2-benzyl-N-hydroxy-N'-(4-phenyl-butyl)-malonamide
Plasmodium falciparum
-
in Tris-HCl buffer (25 mM, pH 7.4), at 25°C
0.001931
2-benzyl-N-hydroxy-N'-indan-2-yl-malonamide
Plasmodium falciparum
-
in Tris-HCl buffer (25 mM, pH 7.4), at 25°C
0.000107
2-benzyl-N-hydroxy-N'-naphthalen-1-ylmethyl-malonamide
Plasmodium falciparum
-
in Tris-HCl buffer (25 mM, pH 7.4), at 25°C
0.001011
2-benzyl-N-hydroxy-N'-phenethyl-malonamide
Plasmodium falciparum
-
in Tris-HCl buffer (25 mM, pH 7.4), at 25°C
0.000125
2N-dibenzyl-N'-hydroxy-malonamide
Plasmodium falciparum
-
in Tris-HCl buffer (25 mM, pH 7.4), at 25°C
0.000966
3-(3,4-dihydro-1H-isoquinolin-2-yl)-N-hydroxy-3-oxo-2-(3-phenoxy-benzyl)-propionamide
Plasmodium falciparum
-
in Tris-HCl buffer (25 mM, pH 7.4), at 25°C
0.000248
3-(4-benzyl-piperidin-1-yl)-N-hydroxy-3-oxo-2-(3-phenoxybenzyl)-propionamide
Plasmodium falciparum
-
in Tris-HCl buffer (25 mM, pH 7.4), at 25°C
0.00013
N-(4-chloro-benzyl)-N'-hydroxy-2-(3-phenoxy-benzyl)-malonamide
Plasmodium falciparum
-
in Tris-HCl buffer (25 mM, pH 7.4), at 25°C
0.000904
N-(4-chloro-benzyl)-N'-hydroxy-2-isobutyl-malonamide
Plasmodium falciparum
-
in Tris-HCl buffer (25 mM, pH 7.4), at 25°C
0.003896
N-(4-fluoro-benzyl)-N'-hydroxy-2-isobutyl-malonamide
Plasmodium falciparum
-
in Tris-HCl buffer (25 mM, pH 7.4), at 25°C
0.00033
N-(4-fluoro-benzyl)-N'-hydroxy-2-[1-phenyl-meth-(E)-ylidene]-malonamide
Plasmodium falciparum
-
in Tris-HCl buffer (25 mM, pH 7.4), at 25°C
0.000006
N-(4-fluoro-benzyl)-N'-hydroxy-2-[1-phenyl-meth-(Z)-ylidene]-malonamide
Plasmodium falciparum
-
in Tris-HCl buffer (25 mM, pH 7.4), at 25°C
0.000164
N-benzyl-N'-hydroxy-2-(3-phenoxy-benzyl)-malonamide
Plasmodium falciparum
-
in Tris-HCl buffer (25 mM, pH 7.4), at 25°C
0.000495
N-benzyl-N'-hydroxy-2-isobutyl-malonamide
Plasmodium falciparum
-
in Tris-HCl buffer (25 mM, pH 7.4), at 25°C
0.000527
N-hydroxy-2-(3-phenoxy-benzyl)-N'-(3-phenyl-propyl)-malonamide
Plasmodium falciparum
-
in Tris-HCl buffer (25 mM, pH 7.4), at 25°C
0.000225
N-hydroxy-2-(3-phenoxy-benzyl)-N'-(4-phenyl-butyl)-malonamide
Plasmodium falciparum
-
in Tris-HCl buffer (25 mM, pH 7.4), at 25°C
0.000231
N-hydroxy-2-(3-phenoxy-benzyl)-N'-(4-trifluoromethyl-benzyl)-malonamide
Plasmodium falciparum
-
in Tris-HCl buffer (25 mM, pH 7.4), at 25°C
0.000109
N-hydroxy-2-isobutyl-N'-(1,2,3,4-tetrahydro-naphthalen-1-yl)-malonamide
Plasmodium falciparum
-
in Tris-HCl buffer (25 mM, pH 7.4), at 25°C
0.000045
N-hydroxy-2-isobutyl-N'-(3-phenoxy-benzyl)-malonamide
Plasmodium falciparum
-
in Tris-HCl buffer (25 mM, pH 7.4), at 25°C
0.00079
N-hydroxy-2-isobutyl-N'-(3-phenyl-propyl)-malonamide
Plasmodium falciparum
-
in Tris-HCl buffer (25 mM, pH 7.4), at 25°C
0.001149
N-hydroxy-2-isobutyl-N'-(4-phenyl-butyl)-malonamide
Plasmodium falciparum
-
in Tris-HCl buffer (25 mM, pH 7.4), at 25°C
0.000091
N-hydroxy-2-isobutyl-N'-naphthalen-1-ylmethyl-malonamide
Plasmodium falciparum
-
in Tris-HCl buffer (25 mM, pH 7.4), at 25°C
0.000885
N-hydroxy-2-isobutyl-N'-phenethyl-malonamide
Plasmodium falciparum
-
in Tris-HCl buffer (25 mM, pH 7.4), at 25°C
0.000013
N-hydroxy-N'-(4-phenyl-butyl)-2-[1-phenyl-meth-(Z)-ylidene]-malonamide
Plasmodium falciparum
-
in Tris-HCl buffer (25 mM, pH 7.4), at 25°C
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Ichishima, E.; Yamagata, Y.; Chiba, H.; Sawaguchi, K.; Tanaka, T.
Soluble and bound forms of aminopeptidase in hen's egg yolk
Agric. Biol. Chem.
53
1867-1872
1989
Gallus gallus
-
brenda
Tanaka, T.; Ichishima, E.
Substrate specificity of aminopeptidase Ey from hens (Gallus domesticus) egg yolk
Comp. Biochem. Physiol. B
105
105-110
1993
Gallus gallus
brenda
Tanaka, T.; Ichishima, E.
Molecular properties of aminopeptidase Ey as a zinc-metalloenzyme
Int. J. Biochem.
25
1681-1688
1993
Gallus gallus
brenda
Midorikawa, T.; Abe, R.; Yamagata, Y.; Nakajima, T.; Ichishima, E.
Isolation and characterization of cDNA encoding chicken egg yolk aminopeptidase Ey
Comp. Biochem. Physiol. B
119
513-520
1998
Gallus gallus
brenda
Ichishima, E.
Aminopeptidase Ey
Handbook of Proteolytic Enzymes (2nd Edition)
1
294-296
2004
Gallus gallus
-
brenda
Flipo, M.; Beghyn, T.; Leroux, V.; Florent, I.; Deprez, B.P.; Deprez-Poulain, R.F.
Novel selective inhibitors of the zinc plasmodial aminopeptidase PfA-M1 as potential antimalarial agents
J. Med. Chem.
50
1322-1334
2007
Plasmodium falciparum, Plasmodium falciparum FcB1
brenda
Santos, K.; Medrano, F.J.
Expression, purification, and characterization of an aminopeptidase (Xac2987) with broad specificity from Xanthomonas axonopodis pv. citri
Protein Expr. Purif.
52
117-122
2007
Xanthomonas axonopodis
brenda
Ragheb, D.; Dalal, S.; Bompiani, K.M.; Ray, W.K.; Klemba, M.
Distribution and biochemical properties of an M1-family aminopeptidase in Plasmodium falciparum indicate a role in vacuolar hemoglobin catabolism
J. Biol. Chem.
286
27255-27265
2011
Plasmodium falciparum (Q8IEK1), Plasmodium falciparum
brenda
Velmourougane, G.; Harbut, M.B.; Dalal, S.; McGowan, S.; Oellig, C.A.; Meinhardt, N.; Whisstock, J.C.; Klemba, M.; Greenbaum, D.C.
Synthesis of new (-)-bestatin-based inhibitor libraries reveals a novel binding mode in the S1 pocket of the essential malaria M1 metalloaminopeptidase
J. Med. Chem.
54
1655-1666
2011
Plasmodium falciparum
brenda
Azimzadeh, O.; Sow, C.; Geze, M.; Nyalwidhe, J.; Florent, I.
Plasmodium falciparum PfA-M1 aminopeptidase is trafficked via the parasitophorous vacuole and marginally delivered to the food vacuole
Malar. J.
9
189
2010
Plasmodium falciparum (O96935), Plasmodium falciparum
brenda
McGowan, S.; Oellig, C.A.; Birru, W.A.; Caradoc-Davies, T.T.; Stack, C.M.; Lowther, J.; Skinner-Adams, T.; Mucha, A.; Kafarski, P.; Grembecka, J.; Trenholme, K.R.; Buckle, A.M.; Gardiner, D.L.; Dalton, J.P.; Whisstock, J.C.
Structure of the Plasmodium falciparum M17 aminopeptidase and significance for the design of drugs targeting the neutral exopeptidases
Proc. Natl. Acad. Sci. USA
107
2449-2454
2010
Plasmodium falciparum (Q8IL11), Plasmodium falciparum
brenda
Harbut, M.B.; Velmourougane, G.; Dalal, S.; Reiss, G.; Whisstock, J.C.; Onder, O.; Brisson, D.; McGowan, S.; Klemba, M.; Greenbaum, D.C.
Bestatin-based chemical biology strategy reveals distinct roles for malaria M1- and M17-family aminopeptidases
Proc. Natl. Acad. Sci. USA
108
E526-E534
2011
Plasmodium falciparum, Plasmodium falciparum (Q8IL11)
brenda
Gras, S.; Byzia, A.; Gilbert, F.B.; McGowan, S.; Drag, M.; Silvestre, A.; Niepceron, A.; Lecaille, F.; Lalmanach, G.; Brossier, F.
Aminopeptidase N1 (EtAPN1), an M1 metalloprotease of the apicomplexan parasite Eimeria tenella, participates in parasite development
Eukaryot. Cell
13
884-895
2014
Eimeria tenella (V5T9T8), Eimeria tenella
brenda
Mistry, S.N.; Drinkwater, N.; Ruggeri, C.; Sivaraman, K.K.; Loganathan, S.; Fletcher, S.; Drag, M.; Paiardini, A.; Avery, V.M.; Scammells, P.J.; McGowan, S.
Two-pronged attack: dual inhibition of Plasmodium falciparum M1 and M17 metalloaminopeptidases by a novel series of hydroxamic acid-based inhibitors
J. Med. Chem.
57
9168-9183
2014
Plasmodium falciparum (O96935), Plasmodium falciparum (Q8IL11), Plasmodium falciparum, Plasmodium falciparum isolate FcB1/Columbia (O96935)
brenda
Dalal, S.; Ragheb, D.R.; Klemba, M.
Engagement of the S1, S1' and S2' subsites drives efficient catalysis of peptide bond hydrolysis by the M1-family aminopeptidase from Plasmodium falciparum
Mol. Biochem. Parasitol.
183
70-77
2012
Plasmodium falciparum
brenda
Gonzalez-Bacerio, J.; Osuna, J.; Ponce, A.; Fando, R.; Figarella, K.; Mendez, Y.; Charli, J.L.; Chavez, M.D.
High-level expression in Escherichia coli, purification and kinetic characterization of Plasmodium falciparum M1-aminopeptidase
Protein Expr. Purif.
104C
103-114
2014
Plasmodium falciparum (Q8IEK1)
brenda
Drinkwater, N.; Bamert, R.S.; Kannan Sivaraman, K.; Paiardini, A.; McGowan, S.
X-ray crystal structures of an orally available aminopeptidase inhibitor, tosedostat, bound to anti-malarial drug targets PfA-M1 and PfA-M17
Proteins
83
789-795
2015
Plasmodium falciparum (O96935), Plasmodium falciparum (Q8IL11), Plasmodium falciparum, Plasmodium falciparum isolate FcB1/Columbia (O96935)
brenda
Da Silva, M.; Labas, V.; Nys, Y.; Rhault-Godbert, S.
Investigating proteins and proteases composing amniotic and allantoic fluids during chicken embryonic development
Poult. Sci.
96
2931-2941
2017
Gallus gallus (O57579)
brenda