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(S)-2-amino-N-(6-(dimethylamino)pyridin-3-yl)-4-methylpentanamide + H2O
?
-
-
-
-
?
4-[(E)-2-[4-cyano-5-(dicyanomethylidene)-2,2-dimethyl-2,5-dihydrofuran-3-yl]ethenyl]phenyl L-leucinate + H2O
L-leucine + 4-[(E)-2-(4-aminophenyl)ethenyl-3-cyano-5,5-dimethylfuran-2(5H)-ylidene]propanedinitrile
-
-
-
-
?
Ala-4-methylcoumaryl-7-amide + H2O
Ala + 7-amino-4-methylcoumarin
Ala-4-nitroanilide + H2O
Ala + 4-nitroaniline
Ala-4-nitroanilide + H2O
L-alanine + 4-nitroaniline
-
18.7% of activity towards Leu-4-nitroanilide
-
-
?
Ala-Ala-Ala-Ala
?
-
-
-
-
?
alaninehydrazine
?
-
-
-
-
?
alanyl-7-amido-4-methylcoumarin + H2O
alanine + 7-amino-4-methylcoumarin
-
-
-
-
?
amino acid amides + H2O
amino acid + NH3
angiotensin II + H2O
angiotensin IV + ?
-
-
through angiotensin III
?
angiotensin II + H2O
Asp + angiotensin III
-
i.e. Asp-Tyr-Arg-Val-Tyr-Ile-His-Pro-Phe
i.e. Tyr-Arg-Val-Tyr-Ile-His-Pro-Phe
-
?
Arg 4-nitroanilide + H2O
Arg + 4-nitroaniline
Arg-4-nitroanilide + H2O
Arg + 4-nitroaniline
Arg-4-nitroanilide + H2O
L-arginine + 4-nitroaniline
-
52.5% of activity towards Leu-4-nitroanilide
-
-
?
Arg-Ala-Arg + H2O
Arg + Ala-Arg
-
Ala-p-nitroanilide is used as substrate with very low turnover rate
in the assay hydrolysis of Ala-p-nitroanilide is monitored
-
?
Arg-Gly-Arg + H2O
Arg + Gly-Arg
Arg-Gly-Asp + H2O
Arg + Gly-Asp
Arg-Gly-Gly + H2O
Arg + Gly-Gly
Arg-Gly-Leu + H2O
Arg + Gly-Leu
Arg-Gly-Phe + H2O
Arg + Gly-Phe
Arg-Gly-Ser + H2O
Arg + Gly-Ser
Arg-Ser-Arg + H2O
Arg + Ser-Arg
-
Ala-p-nitroanilide is used as substrate with very low turnover rate
in the assay hydrolysis of Ala-p-nitroanilide is monitored
-
?
Asn-Leu + H2O
Asn + Leu
-
-
?
Asp-Gln + H2O
Asp + Gln
-
-
?
Asp-His + H2O
Asp + His
-
-
?
Asp-Ile-Gly-Gly + H2O
Asp + Ile-Gly-Gly
-
-
?
Asp-Leu + H2O
Asp + Leu
-
-
?
Asp-Leu-Gly + H2O
Asp + Leu-Gly
-
-
?
Asp-Leu-Lys + H2O
Asp + Leu-Lys
-
-
?
Asp-Phe + H2O
Asp + Phe
-
-
?
Asp-Tyr + H2O
Asp + Tyr
-
-
?
benzyl-L-cysteinamide + H2O
?
bimane-S-cysteinylglycine + H2O
?
-
-
-
?
Cys-Leu + H2O
Cys + Leu
-
-
?
cysteinyl-bis-glycine + H2O
cysteine + glycine
-
-
-
?
cysteinylglycine + H2O
cysteine + glycine
DL-alpha-amino-acid amide + H2O
D-alpha-amino acid amide + L-alpha-amino acid
-
-
-
-
?
dynorphin A + H2O
?
-
-
-
?
Gln-Leu + H2O
Gln + Leu
-
-
?
Glu-Leu + H2O
Glu + Leu
-
-
?
Gly-7-amido-4-methylcoumarin + H2O
glycine + 7-amino-4-methylcoumarin
enzyme shows only weak activity with this substrate
-
-
?
Gly-Val + H2O
Gly + Val
-
low activity
-
?
glycine-4-methylcoumaryl-7-amide + H2O
glycine + 7-amino-4-methylcoumarin
-
3.9% activity in comparison to L-leucine-4-methyl-coumaryl-7-amide
-
-
?
hArg-7-amido-4-methylcoumarin + H2O
hArg + 7-amino-4-methylcoumarin
-
-
-
-
?
His-Phe-Arg-Trp-Pro-Gly-Pro + H2O
Trp-Pro-Gly-Pro + Arg-Trp-Pro-Gly-Pro
Ile-Leu + H2O
Ile + Leu
-
-
?
kallidin + H2O
?
-
-
-
-
?
kallidin + H2O
Leu + bradykinin
-
i.e. LRPPGFSPFR
i.e. RPPGFSPFR
?
L-Ala-4-nitroanilide + H2O
L-Ala + 4-nitroaniline
L-Ala-4-nitroanilide + H2O
L-alanine + 4-nitroaniline
L-Ala-7-amido-4-methylcoumarin + H2O
L-Ala + 7-amino-4-methylcoumarin
L-Ala-7-amido-4-trifluoro-methylcoumarin + H2O
L-Ala + 7-amino-4-trifluoromethylcoumarin
-
-
-
-
?
L-Ala-L-Leu + H2O
L-Ala + L-Leu
-
-
-
?
L-alanine 4-nitroanilide + H2O
L-alanine + 4-nitroaniline
L-alanine-4-methylcoumarin-7-amide + H2O
L-alanine + 7-amino-4-methylcoumarin
L-alanine-4-methylcoumaryl-7-amide + H2O
L-alanine + 7-amino-4-methylcoumarin
L-alanine-4-methylcoumaryl-7-amide + H2O
L-alanine + 7-amino-4-methylcoumarine
-
-
-
?
L-alanyl-4-nitroanilide + H2O
L-alanine + 4-nitroaniline
-
-
-
-
?
L-alanyl-7-amido-4-methylcoumarin + H2O
L-alanine + 7-amino-4-methylcoumarin
L-amino acid-peptide + H2O
amino acid + peptide
L-Arg 7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
-
moderate activity
-
-
?
L-Arg-4-nitroanilide + H2O
L-Arg + 4-nitroaniline
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
L-Arg-7-amido-4-trifluoro-methylcoumarin + H2O
L-Arg + 7-amino-4-trifluoromethylcoumarin
-
-
-
-
?
L-arginine-4-methylcoumarin-7-amide + H2O
L-arginine + 7-amino-4-methylcoumarin
L-arginine-4-methylcoumaryl-7-amide + H2O
L-arginine + 7-amino-4-methylcoumarin
L-arginine-4-methylcoumaryl-7-amide + H2O
L-arginine + 7-amino-4-methylcoumarine
L-arginine-4-nitroanilide + H2O
L-arginine + 4-nitroaniline
-
16.5% activity in comparison to L-leucine-4-nitroanilide
-
-
?
L-arginyl-7-amido-4-methylcoumarin + H2O
L-arginine + 7-amino-4-methylcoumarin
L-Cys-7-amido-4-methylcoumarin + H2O
L-Cys + 7-amino-4-methylcoumarin
L-glutamate 4-nitroanilide + H2O
L-glutamate + 4-nitroaniline
L-His-L-Leu + H2O
L-His + L-Leu
-
-
-
?
L-Ile-4-nitroanilide + H2O
L-Ile + 4-nitroaniline
L-Ile-7-amido-4-methylcoumarin + H2O
L-Ile + 7-amino-4-methylcoumarin
L-Ile-7-amido-4-methylcoumarin + H2O
L-isoleucine + 7-amino-4-methylcoumarin
enzyme shows only weak activity with this substrate
-
-
?
L-isoleucine 4-nitroanilide + H2O
L-isoleucine + 4-nitroaniline
L-Leu 7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
L-Leu beta-naphthylamide + H2O
L-Leu + beta-naphthylamine
-
-
-
?
L-Leu methyl ester
?
-
-
-
-
?
L-Leu-2-naphthylamide + H2O
L-Leu + 2-naphthylamine
L-Leu-4-(phenylazo)phenylamide + H2O
L-Leu + 4-(phenylazo)phenylamine
-
-
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
L-Leu-4-nitroanilide + H2O
L-leucine + 4-nitroaniline
L-Leu-7-amido-4-methylcoumarin + H2O
7-amino-4-methylcoumarin + L-Leu
-
-
-
-
?
L-Leu-7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
L-Leu-7-amido-4-trifluoro-methylcoumarin + H2O
L-Leu + 7-amino-4-trifluoromethylcoumarin
-
-
-
-
?
L-Leu-benzyl ester + H2O
L-Leu + benzylalcohol
-
-
-
-
?
L-Leu-Gly + H2O
L-Leu + Gly
L-Leu-hydrazide
?
-
-
-
-
?
L-Leu-L-Arg + H2O
L-Leu + L-Arg
-
-
-
?
L-Leu-L-Asn + H2O
L-Leu + L-Asn
-
-
-
?
L-Leu-L-Asp + H2O
L-Leu + L-Asp
-
low activity
-
?
L-Leu-L-Leu + H2O
L-Leu + L-Leu
-
-
-
?
L-Leu-L-Met + H2O
L-Leu + L-Met
-
-
-
?
L-Leu-L-Phe + H2O
L-Leu + L-Phe
-
-
-
?
L-Leu-L-Ser + H2O
L-Leu + L-Ser
-
-
-
?
L-Leu-L-Tyr + H2O
L-Leu + L-Tyr
-
-
-
?
L-Leu-p-nitroanilide + H2O
L-Leu + p-nitroaniline
L-Leu-p-nitroanilide + H2O
L-leucine + p-nitroaniline
L-Leu-phenylazophenylamide
?
-
-
-
-
?
L-leucine 4-nitroanilide + H2O
L-leucine + 4-nitroaniline
L-leucine 4-nitroanilide + H2O
leucine + 4-nitroaniline
L-leucine amide + H2O
L-leucine + NH3
L-leucine hydrazide + H2O
L-leucine + azide
L-leucine-4-methylcoumarin-7-amide + H2O
L-leucine + 7-amino-4-methylcoumarin
L-leucine-4-methylcoumaryl-7-amide + H2O
L-leucine + 7-amino-4-methylcoumarin
L-leucine-4-methylcoumaryl-7-amide + H2O
L-leucine + 7-amino-4-methylcoumarine
L-leucine-4-nitroanilide + H2O
L-leucine + 4-nitroaniline
L-leucine-7-amido-4-methylcoumarin + H2O
L-leucine + 7-amino-4-methylcoumarin
L-leucine-p-nitroanilide + H2O
L-Leu + p-nitroaniline
-
-
-
-
?
L-leucine-p-nitroanilide + H2O
L-leucine + p-nitroaniline
L-leucinhydrazide + H2O
L-leucine + H2NNH2
-
-
-
-
?
L-leucyl-2-naphthylamide + H2O
L-leucine + 2-naphthylamine
L-leucyl-4-nitroanilide + H2O
L-leucine + 4-nitroaniline
-
-
-
-
?
L-leucyl-7-amido-4-methylcoumarin + H2O
L-leucine + 7-amino-4-methylcoumarin
L-leucylamide + H2O
L-leucine + NH3
-
-
-
-
?
L-leucylglycine + H2O
L-leucine + glycine
L-Lys-4-nitroanilide + H2O
L-Lys + 4-nitroaniline
-
-
-
?
L-Lys-4-nitroanilide + H2O
L-lysine + 4-nitroaniline
L-lysine-4-methylcoumaryl-7-amide + H2O
L-lysine + 7-amino-4-methylcoumarin
L-lysine-4-nitroanilide + H2O
L-lysine + 4-nitroaniline
L-lysyl-4-nitroanilide + H2O
L-lysine + 4-nitroaniline
-
-
-
-
?
L-lysyl-7-amido-4-methylcoumarin + H2O
L-lysine + 7-amino-4-methylcoumarin
ERAP2 preferentially hydrolyzes Arg-aminomethylcoumarin and Lys-aminomethylcoumarin
-
-
?
L-Met 7-amido-4-methylcoumarin + H2O
L-Met + 7-amino-4-methylcoumarin
-
moderate activity
-
-
?
L-Met-4-nitroanilide + H2O
L-Met + 4-nitroaniline
L-Met-7-amido-4-methylcoumarin + H2O
L-Met + 7-amino-4-methylcoumarin
L-Met-Gly + H2O
L-Met + Gly
-
-
-
?
L-Met-L-Leu + H2O
L-Met + L-Leu
-
-
-
?
L-methionine 4-nitroanilide + H2O
L-methionine + 4-nitroaniline
L-methionine-4-methylcoumaryl-7-amide + H2O
L-methionine + 7-amino-4-methylcoumarin
L-methionine-4-nitroanilide + H2O
L-methionine + 4-nitroaniline
L-methionyl-4-nitroanilide + H2O
L-methionine + 4-nitroaniline
-
-
-
-
?
L-methionyl-7-amido-4-methylcoumarin + H2O
L-methionine + 7-amino-4-methylcoumarin
high activity
-
-
?
L-Phe 7-amido-4-methylcoumarin + H2O
L-Phe + 7-amino-4-methylcoumarin
-
low activity
-
-
?
L-Phe-4-nitroanilide + H2O
L-Phe + 4-nitroaniline
-
-
-
?
L-Phe-7-amido-4-methylcoumarin + H2O
L-Phe + 7-amino-4-methylcoumarin
L-Phe-L-Leu + H2O
L-Phe + L-Leu
-
-
-
?
L-phenylalanine-4-methylcoumarin-7-amide + H2O
L-phenylalanine + 7-amino-4-methylcoumarin
L-phenylalanine-4-methylcoumaryl-7-amide + H2O
L-phenylalanine + 7-amino-4-methylcoumarin
L-phenylalanine-4-methylcoumaryl-7-amide + H2O
L-phenylalanine + 7-amino-4-methylcoumarine
-
-
-
?
L-phenylalanine-4-nitroanilide + H2O
L-phenylalanine + 4-nitroaniline
L-Pro-4-nitroanilide + H2O
L-Pro + 4-nitroaniline
-
-
-
?
L-Pro-4-nitroanilide + H2O
L-proline + 4-nitroaniline
L-Pro-L-Leu + H2O
L-Pro + L-Leu
-
-
-
?
L-proline-4-methylcoumarin-7-amide + H2O
L-proline + 7-amino-4-methylcoumarin
L-proline-4-methylcoumaryl-7-amide + H2O
L-proline + 7-amino-4-methylcoumarin
-
1.3% activity in comparison to L-leucine-4-methyl-coumaryl-7-amide
-
-
?
L-proline-4-methylcoumaryl-7-amide + H2O
L-proline + 7-amino-4-methylcoumarine
-
-
-
?
L-prolyl-7-amido-4-methylcoumarin + H2O
L-proline + 7-amino-4-methylcoumarin
L-Ser-Gly + H2O
L-Ser + Gly
-
-
-
?
L-Thr 7-amido-4-methylcoumarin + H2O
L-Thr + 7-amino-4-methylcoumarin
-
low activity
-
-
?
L-Thr-4-nitroanilide + H2O
L-Thr + 4-nitroaniline
-
-
-
?
L-Thr-L-Leu + H2O
L-Thr + L-Leu
-
-
-
?
L-Trp-7-amido-4-methylcoumarin + H2O
L-Trp + 7-amino-4-methylcoumarin
L-Trp-L-Leu + H2O
L-Trp + L-Leu
-
-
-
?
L-Tyr 7-amido-4-methylcoumarin + H2O
L-Tyr + 7-amino-4-methylcoumarin
-
lower activity
-
-
?
L-Tyr-7-amido-4-methylcoumarin + H2O
L-Tyr + 7-amino-4-methylcoumarin
6.4% activity compared to L-Leu-7-amido-4-methylcoumarin
-
-
?
L-Tyr-L-Leu + H2O
L-Tyr + L-Leu
-
-
-
?
L-tyrosine-4-methylcoumaryl-7-amide + H2O
L-tyrosine + 7-amino-4-methylcoumarin
-
8.5% activity in comparison to L-leucine-4-methyl-coumaryl-7-amide
-
-
?
L-tyrosine-4-methylcoumaryl-7-amide + H2O
L-tyrosine + 7-amino-4-methylcoumarine
20% activity compared to L-leucyl-4-methylcoumaryl-7-amide
-
-
?
L-tyrosyl-7-amido-4-methylcoumarin + H2O
L-tyrosine + 7-amino-4-methylcoumarin
L-Val-4-nitroanilide + H2O
L-Val + 4-nitroaniline
L-Val-7-amido-4-methylcoumarin + H2O
L-Val + 7-amino-4-methylcoumarin
enzyme shows only weak activity with this substrate
-
-
?
L-Val-L-Leu + H2O
L-Val + L-Leu
-
-
-
?
L-valine-4-methylcoumaryl-7-amide + H2O
L-valine + 7-amino-4-methylcoumarin
-
2.3% activity in comparison to L-leucine-4-methyl-coumaryl-7-amide
-
-
?
Leu 4-nitroanilide + H2O
Leu + 4-nitroaniline
Leu-2-naphthylamide + H2O
Leu + 2-naphthylamine
-
-
-
-
?
Leu-2-naphthylamide + H2O
leucine + 2-naphthylamine
Leu-4-methylcoumaryl-7-amide + H2O
Leu + 7-amino-4-methyl-coumarin
-
-
-
-
?
Leu-4-methylcoumaryl-7-amide + H2O
Leu + 7-amino-4-methylcoumarin
Leu-4-nitroanilide + H2O
L-leucine + 4-nitroaniline
Leu-4-nitroanilide + H2O
Leu + 4-nitroaniline
Leu-4-trifluoroomethylcoumarin-7-amide + H2O
Leu + 7-amino-4-trifluoromethylcoumarin
-
-
-
-
?
Leu-7-amido-4-methylcoumarin + H2O
Leu + 7-amino-4-methylcoumarin
-
-
-
-
?
Leu-7-amido-4-methylcoumarin + H2O
leucine + 7-amino-4-methylcoumarin
Leu-Arg-Pro-Gly + H2O
Leu + Arg-Pro-Gly
-
-
-
-
?
Leu-enkephalin
?
-
-
-
-
?
Leu-Gly-Arg-Ser-Gly-Gly-Asp-Ile-Ile-Lys-Lys-Met-Gln-Thr-Leu + H2O
Leu + Gly-Arg-Ser-Gly-Gly-Asp-Ile-Ile-Lys-Lys-Met-Gln-Thr-Leu
-
-
-
-
?
Leu-Gly-Gly + H2O
Leu + Gly-Gly
Leu-Gly-Tyr-Leu + H2O
Leu + Gly + Tyr + Leu
-
synthetic peptide substrate, successive release of terminal amino acids with descending activity
-
-
?
Leu-Leu-Leu + H2O
Leu + Leu-Leu
Leu-p-nitroanilide + H2O
Leu + p-nitroaniline
Leu-Ser-Ile-Ile-Asn-Phe-Glu-Lys-Leu + H2O
? + Ile-Asn-Phe-Glu-Lys-Leu
-
-
-
-
?
Leu-Ser-Ile-Ile-Asn-Phe-Glu-Lys-Leu + H2O
? + Ile-Ile-Asn-Phe-Glu-Lys-Leu
-
-
-
-
?
Leu-Ser-Ile-Ile-Asn-Phe-Glu-Lys-Leu + H2O
L-leucine + Ser-Ile-Ile-Asn-Phe-Glu-Lys-Leu
-
trimming of further model epitope precursors to antigenic peptides are also tested
-
-
?
Leu-systemin + H2O
Leu + systemin
-
LAP-A1, only in vitro
-
-
?
leucyl-7-amido-4-methylcoumarin + H2O
leucine + 7-amino-4-methylcoumarin
-
-
-
?
leukotriene D4 + H2O
?
-
low activity
-
?
Lys 4-nitroanilide + H2O
Lys + 4-nitroaniline
Lys-4-nitroanilide + H2O
L-lysine + 4-nitroaniline
-
41.9% of activity towards Leu-4-nitroanilide
-
-
?
Lys-4-nitroanilide + H2O
Lys + 4-nitroaniline
Met 4-nitroanilide + H2O
Met + 4-nitroaniline
Met-4-methylcoumaryl-7-amide + H2O
Met + 7-amino-4-methyl-coumarin
-
-
-
-
?
Met-4-nitroanilide + H2O
Met + 4-nitroaniline
Met-Glu-His-Phe-Pro-Gly-Pro + H2O
?
Met-Gly + H2O
Met + Gly
-
-
?
N-(6-methoxy-2-methylpyridin-3-yl),(S)-2-amino-4-methylpentanamide + H2O
?
-
-
-
-
?
N-(6-methoxy-2-methylpyridin-3-yl)-(S)-2-amino-4-methylpentanamide + H2O
?
-
-
-
-
?
N-(6-methoxypyridin-3-yl)-(S)-2-amino-4-methylpentanamide + H2O
?
-
-
-
-
?
N-(tert-butoxycarbonyl)-L-leucine + H2O
?
-
-
-
-
?
N-succinyl-L-Leu-4-nitroanilide + H2O
N-succinyl-L-Leu + 4-nitroaniline
Neurokinin A + H2O
?
-
-
-
?
Neuromedin B + H2O
?
-
-
-
?
Phe 4-nitroanilide + H2O
Phe + 4-nitroaniline
-
-
-
?
Phe-4-methylcoumaryl-7-amide + H2O
Phe + 7-amino-4-methyl-coumarin
-
-
-
-
?
Phe-4-methylcoumaryl-7-amide + H2O
Phe + 7-amino-4-methylcoumarin
Phg-7-amido-4-methylcoumarin + H2O
Phg + 7-amino-4-methylcoumarin
-
-
-
-
?
phosphatidylinositol-dependent kinase-1 + H2O
?
Pro-4-methylcoumaryl-7-amide + H2O
Pro + 7-amino-4-methylcoumarin
Pro-4-nitroanilide + H2O
Pro + 4-nitroaniline
-
30% of the activity with Leu-4-nitroanilide
-
-
?
S-nitrosocysteinylglycine + H2O
S-nitrosocysteine + glycine
-
-
-
?
Ser-Gly + H2O
Ser + Gly
-
-
?
Ser-Leu + H2O
Ser + Leu
-
-
?
additional information
?
-
Ala-4-methylcoumaryl-7-amide + H2O
Ala + 7-amino-4-methylcoumarin
-
-
-
?
Ala-4-methylcoumaryl-7-amide + H2O
Ala + 7-amino-4-methylcoumarin
-
-
-
?
Ala-4-nitroanilide + H2O
Ala + 4-nitroaniline
-
42% of the activity with Leu-4-nitroanilide
-
-
?
Ala-4-nitroanilide + H2O
Ala + 4-nitroaniline
-
-
-
-
?
Ala-4-nitroanilide + H2O
Ala + 4-nitroaniline
-
-
-
?
Ala-Gly + H2O
Ala + Gly
-
low activity
-
?
Ala-Gly + H2O
Ala + Gly
-
-
-
?
Ala-Gly + H2O
Ala + Gly
-
low activity
-
?
Ala-Leu + H2O
Ala + Leu
-
high activity
-
?
Ala-Leu + H2O
Ala + Leu
-
-
?
Ala-Leu + H2O
Ala + Leu
-
high activity
-
?
Ala-Leu + H2O
Ala + Leu
-
high activity
-
?
amino acid amides + H2O
amino acid + NH3
-
fast hydrolysis: L-Leu
-
-
?
amino acid amides + H2O
amino acid + NH3
-
-
-
-
?
amino acid amides + H2O
amino acid + NH3
-
-
-
-
?
amino acid amides + H2O
amino acid + NH3
-
fast hydrolysis: L-Leu
-
-
?
amino acid amides + H2O
amino acid + NH3
-
fast hydrolysis: L-Leu
-
-
?
amino acid amides + H2O
amino acid + NH3
-
-
-
-
?
amino acid amides + H2O
amino acid + NH3
-
fast hydrolysis: L-Leu
-
-
?
amino acid amides + H2O
amino acid + NH3
-
fast hydrolysis: L-Leu
-
-
?
amino acid amides + H2O
amino acid + NH3
-
fast hydrolysis: L-Leu
-
-
?
amino acid amides + H2O
amino acid + NH3
-
fast hydrolysis: L-Leu
-
-
?
amino acid amides + H2O
amino acid + NH3
-
slow hydrolysis: Tyr, Phe
-
-
?
amino acid amides + H2O
amino acid + NH3
-
fast hydrolysis: L-Leu
-
-
?
amino acid amides + H2O
amino acid + NH3
-
D,L-norleucine
-
-
?
amino acid amides + H2O
amino acid + NH3
trout
-
fast hydrolysis: L-Leu
-
-
?
amino acid amides + H2O
amino acid + NH3
-
fast hydrolysis: L-Leu
-
-
?
amino acid amides + H2O
amino acid + NH3
-
fast hydrolysis: L-Leu
-
-
?
Arg 4-nitroanilide + H2O
Arg + 4-nitroaniline
-
-
-
?
Arg 4-nitroanilide + H2O
Arg + 4-nitroaniline
-
-
-
?
Arg-4-nitroanilide + H2O
Arg + 4-nitroaniline
74.5% activity compared to Leu-4-nitroanilide
-
-
?
Arg-4-nitroanilide + H2O
Arg + 4-nitroaniline
-
-
-
?
Arg-Ala + H2O
Arg + Ala
-
-
-
?
Arg-Ala + H2O
Arg + Ala
-
-
-
?
Arg-Ala + H2O
Arg + Ala
-
-
-
?
Arg-Glu + H2O
Arg + Glu
-
low activity
-
?
Arg-Glu + H2O
Arg + Glu
-
low activity
-
?
Arg-Glu + H2O
Arg + Glu
-
low activity
-
?
Arg-Gly + H2O
Arg + Gly
-
-
-
?
Arg-Gly + H2O
Arg + Gly
-
low activity
-
?
Arg-Gly + H2O
Arg + Gly
-
-
-
?
Arg-Gly + H2O
Arg + Gly
-
low activity
-
?
Arg-Gly + H2O
Arg + Gly
-
-
-
?
Arg-Gly + H2O
Arg + Gly
-
low activity
-
?
Arg-Gly-Arg + H2O
Arg + Gly-Arg
-
low activity
-
?
Arg-Gly-Arg + H2O
Arg + Gly-Arg
-
low activity
-
?
Arg-Gly-Arg + H2O
Arg + Gly-Arg
-
low activity
-
?
Arg-Gly-Asp + H2O
Arg + Gly-Asp
-
-
-
?
Arg-Gly-Asp + H2O
Arg + Gly-Asp
-
-
-
?
Arg-Gly-Asp + H2O
Arg + Gly-Asp
-
-
-
?
Arg-Gly-Gly + H2O
Arg + Gly-Gly
-
-
-
?
Arg-Gly-Gly + H2O
Arg + Gly-Gly
-
-
-
?
Arg-Gly-Gly + H2O
Arg + Gly-Gly
-
-
-
?
Arg-Gly-Leu + H2O
Arg + Gly-Leu
-
-
-
?
Arg-Gly-Leu + H2O
Arg + Gly-Leu
-
-
-
?
Arg-Gly-Leu + H2O
Arg + Gly-Leu
-
-
-
?
Arg-Gly-Phe + H2O
Arg + Gly-Phe
-
-
-
?
Arg-Gly-Phe + H2O
Arg + Gly-Phe
-
-
-
?
Arg-Gly-Phe + H2O
Arg + Gly-Phe
-
-
-
?
Arg-Gly-Ser + H2O
Arg + Gly-Ser
-
-
-
?
Arg-Gly-Ser + H2O
Arg + Gly-Ser
-
-
-
?
Arg-Gly-Ser + H2O
Arg + Gly-Ser
-
-
-
?
Arg-Ile + H2O
Arg + Ile
-
-
-
?
Arg-Ile + H2O
Arg + Ile
-
-
-
?
Arg-Ile + H2O
Arg + Ile
-
-
-
?
Arg-Leu + H2O
Arg + Leu
-
high activity
-
?
Arg-Leu + H2O
Arg + Leu
-
high activity
-
?
Arg-Leu + H2O
Arg + Leu
-
high activity
-
?
Arg-Phe + H2O
Arg + Phe
-
-
-
?
Arg-Phe + H2O
Arg + Phe
-
-
-
?
Arg-Phe + H2O
Arg + Phe
-
-
-
?
Arg-Val + H2O
Arg + Val
-
-
-
?
Arg-Val + H2O
Arg + Val
-
-
-
?
Arg-Val + H2O
Arg + Val
-
-
-
?
benzyl-L-cysteinamide + H2O
?
-
-
-
-
?
benzyl-L-cysteinamide + H2O
?
-
-
-
-
?
Cys-Gly + H2O
Cys + Gly
-
-
?
Cys-Gly + H2O
Cys + Gly
the enzyme plays a role in glutathione turnover
-
-
?
Cys-Gly + H2O
Cys + Gly
only hydrolyzed by the Mn2+-Zn2+-enzyme, not by the Zn2+-Zn2+-enzyme
-
-
?
Cys-Gly + H2O
Cys + Gly
-
low activity
-
?
Cys-Gly + H2O
Cys + Gly
-
low activity
-
?
cysteinylglycine + H2O
cysteine + glycine
involved in turnover of glutathione
-
?
cysteinylglycine + H2O
cysteine + glycine
-
-
-
?
cysteinylglycine + H2O
cysteine + glycine
-
involved in the metabolism of glutathione and glutathione S-conjugates, major cysteinylglycine-hydrolysing activity
-
?
Gly-Leu + H2O
Gly + Leu
-
low activity
-
?
Gly-Leu + H2O
Gly + Leu
-
low activity
-
?
Gly-Leu + H2O
Gly + Leu
-
low activity
-
?
Gly-Phe + H2O
Gly + Phe
-
low activity
-
?
Gly-Phe + H2O
Gly + Phe
-
-
-
?
Gly-Phe + H2O
Gly + Phe
-
-
-
?
Gly-Phe + H2O
Gly + Phe
-
-
-
-
?
Gly-Trp + H2O
Gly + Trp
-
low activity
-
?
Gly-Trp + H2O
Gly + Trp
-
low activity
-
?
Gly-Tyr + H2O
Gly + Tyr
-
low activity
-
?
Gly-Tyr + H2O
Gly + Tyr
-
low activity
-
?
Gly-Tyr + H2O
Gly + Tyr
-
low activity
-
?
His-Gly + H2O
His + Gly
-
-
-
?
His-Gly + H2O
His + Gly
-
-
-
?
His-Gly + H2O
His + Gly
-
-
-
?
His-Leu + H2O
His + Leu
-
low activity
-
?
His-Leu + H2O
His + Leu
-
-
?
His-Leu + H2O
His + Leu
-
-
-
?
His-Leu + H2O
His + Leu
-
-
-
?
His-Phe-Arg-Trp-Pro-Gly-Pro + H2O
Trp-Pro-Gly-Pro + Arg-Trp-Pro-Gly-Pro
-
ACTH-(6-9)-PGP peptide, proteolysis of the ACTH-(6-9)-PGP is mainly defined by aminopeptidases, the basic metabolite is Trp-Pro-Gly-Pro. After 180 min, Arg-Trp-Pro-Gly-Pro and Trp-Pro-Gly-Pro are generated from Phe-Arg-Trp-Pro-Gly-Pro, and phenylalalnine cleavage proceeds much less efficiently than further cleavage of arginine
-
-
?
His-Phe-Arg-Trp-Pro-Gly-Pro + H2O
Trp-Pro-Gly-Pro + Arg-Trp-Pro-Gly-Pro
-
ACTH-(6-9)-PGP peptide, proteolysis of the ACTH-(6-9)-PGP is mainly defined by aminopeptidases, the basic metabolite is Trp-Pro-Gly-Pro. After 180 min, Arg-Trp-Pro-Gly-Pro and Trp-Pro-Gly-Pro are generated from Phe-Arg-Trp-Pro-Gly-Pro, and phenylalalnine cleavage proceeds much less efficiently than further cleavage of arginine
-
-
?
L-Ala-4-nitroanilide + H2O
L-Ala + 4-nitroaniline
-
-
-
?
L-Ala-4-nitroanilide + H2O
L-Ala + 4-nitroaniline
-
-
-
-
?
L-Ala-4-nitroanilide + H2O
L-alanine + 4-nitroaniline
-
-
-
?
L-Ala-4-nitroanilide + H2O
L-alanine + 4-nitroaniline
-
-
-
?
L-Ala-7-amido-4-methylcoumarin + H2O
L-Ala + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Ala-7-amido-4-methylcoumarin + H2O
L-Ala + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Ala-7-amido-4-methylcoumarin + H2O
L-Ala + 7-amino-4-methylcoumarin
low activity
-
?
L-Ala-7-amido-4-methylcoumarin + H2O
L-Ala + 7-amino-4-methylcoumarin
low activity
-
?
L-Ala-7-amido-4-methylcoumarin + H2O
L-Ala + 7-amino-4-methylcoumarin
low activity
-
?
L-Ala-7-amido-4-methylcoumarin + H2O
L-Ala + 7-amino-4-methylcoumarin
-
-
-
?
L-Ala-7-amido-4-methylcoumarin + H2O
L-Ala + 7-amino-4-methylcoumarin
-
-
-
-
?
L-alanine 4-nitroanilide + H2O
L-alanine + 4-nitroaniline
10.8% of the activity compared to Leu-4-nitroanilide
-
-
?
L-alanine 4-nitroanilide + H2O
L-alanine + 4-nitroaniline
about 20% of the activity compared to Leu-4-nitroanilide
-
-
?
L-alanine 4-nitroanilide + H2O
L-alanine + 4-nitroaniline
about 20% of the activity compared to Leu-4-nitroanilide
-
-
?
L-alanine 4-nitroanilide + H2O
L-alanine + 4-nitroaniline
10.8% of the activity compared to Leu-4-nitroanilide
-
-
?
L-alanine-4-methylcoumarin-7-amide + H2O
L-alanine + 7-amino-4-methylcoumarin
-
-
-
-
?
L-alanine-4-methylcoumarin-7-amide + H2O
L-alanine + 7-amino-4-methylcoumarin
-
-
-
-
?
L-alanine-4-methylcoumaryl-7-amide + H2O
L-alanine + 7-amino-4-methylcoumarin
-
-
-
?
L-alanine-4-methylcoumaryl-7-amide + H2O
L-alanine + 7-amino-4-methylcoumarin
-
-
-
?
L-alanine-4-methylcoumaryl-7-amide + H2O
L-alanine + 7-amino-4-methylcoumarin
-
32.5% activity in comparison to L-leucine-4-methyl-coumaryl-7-amide
-
-
?
L-alanine-4-methylcoumaryl-7-amide + H2O
L-alanine + 7-amino-4-methylcoumarin
-
-
-
?
L-alanyl-7-amido-4-methylcoumarin + H2O
L-alanine + 7-amino-4-methylcoumarin
-
20.5% activity compared to L-leucyl-7-amido-4-methylcoumarin
-
-
?
L-alanyl-7-amido-4-methylcoumarin + H2O
L-alanine + 7-amino-4-methylcoumarin
-
-
-
?
L-alanyl-7-amido-4-methylcoumarin + H2O
L-alanine + 7-amino-4-methylcoumarin
-
-
-
-
?
L-amino acid-peptide + H2O
amino acid + peptide
-
best substrate with L-Leu at N-terminal end
-
-
?
L-amino acid-peptide + H2O
amino acid + peptide
-
Leu-Gly-Gly
-
-
?
L-amino acid-peptide + H2O
amino acid + peptide
-
fast hydrolysis of hydrophobic amino acids in N-terminal position
-
-
?
L-amino acid-peptide + H2O
amino acid + peptide
-
free N-terminal alpha-amino group required
-
-
?
L-amino acid-peptide + H2O
amino acid + peptide
-
Leu-Gly
-
-
?
L-amino acid-peptide + H2O
amino acid + peptide
-
Leu-Gly
-
-
?
L-amino acid-peptide + H2O
amino acid + peptide
-
e.g. Leu-Leu
-
-
?
L-amino acid-peptide + H2O
amino acid + peptide
-
His-Lys
-
-
?
L-amino acid-peptide + H2O
amino acid + peptide
-
no hydrolysis of D-Leu
-
-
?
L-amino acid-peptide + H2O
amino acid + peptide
-
free N-terminal alpha-amino group required
-
-
?
L-amino acid-peptide + H2O
amino acid + peptide
-
Phe-Leu
-
-
?
L-amino acid-peptide + H2O
amino acid + peptide
-
Ser-Leu
-
-
?
L-amino acid-peptide + H2O
amino acid + peptide
-
e.g. Leu-Leu
-
-
?
L-amino acid-peptide + H2O
amino acid + peptide
-
Leu-Arg
-
-
?
L-amino acid-peptide + H2O
amino acid + peptide
-
Leu-Met
-
-
?
L-amino acid-peptide + H2O
amino acid + peptide
-
fast hydrolysis of hydrophobic amino acids in N-terminal position
-
-
?
L-amino acid-peptide + H2O
amino acid + peptide
-
Leu-Gly
-
-
?
L-amino acid-peptide + H2O
amino acid + peptide
-
Ala-Ala-Ala-Ala
-
-
?
L-amino acid-peptide + H2O
amino acid + peptide
-
Leu-Gly
-
-
?
L-amino acid-peptide + H2O
amino acid + peptide
-
Leu-Gly-Gly
-
-
?
L-amino acid-peptide + H2O
amino acid + peptide
-
Leu-Gly
-
-
?
L-amino acid-peptide + H2O
amino acid + peptide
-
Leu-Gly
-
-
?
L-amino acid-peptide + H2O
amino acid + peptide
-
best substrate with L-Leu at N-terminal end
-
-
?
L-amino acid-peptide + H2O
amino acid + peptide
-
influence of amino acid in penultimate position
-
-
?
L-amino acid-peptide + H2O
amino acid + peptide
-
Leu-Gly
-
-
?
L-amino acid-peptide + H2O
amino acid + peptide
-
Leu-Gly-Gly
-
-
?
L-amino acid-peptide + H2O
amino acid + peptide
trout
-
Leu-Gly
-
-
?
L-amino acid-peptide + H2O
amino acid + peptide
-
leucyl-dipeptides
-
-
?
L-amino acid-peptide + H2O
amino acid + peptide
-
Leu-Met
-
-
?
L-amino acid-peptide + H2O
amino acid + peptide
-
Pro-Phe-Lys
-
-
?
L-amino acid-peptide + H2O
amino acid + peptide
-
free N-terminal alpha-amino group required
-
-
?
L-amino acid-peptide + H2O
amino acid + peptide
-
fast hydrolysis of hydrophobic amino acids in N-terminal position
-
-
?
L-amino acid-peptide + H2O
amino acid + peptide
-
free N-terminal alpha-amino group required
-
-
?
L-amino acid-peptide + H2O
amino acid + peptide
-
fast hydrolysis of hydrophobic amino acids in N-terminal position
-
-
?
L-Arg-4-nitroanilide + H2O
L-Arg + 4-nitroaniline
-
-
-
-
?
L-Arg-4-nitroanilide + H2O
L-Arg + 4-nitroaniline
-
pre-LAP
-
-
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
34.7% activity compared to L-Leu-7-amido-4-methylcoumarin
-
-
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
L-arginine-4-methylcoumarin-7-amide + H2O
L-arginine + 7-amino-4-methylcoumarin
-
-
-
-
?
L-arginine-4-methylcoumarin-7-amide + H2O
L-arginine + 7-amino-4-methylcoumarin
-
-
-
-
?
L-arginine-4-methylcoumaryl-7-amide + H2O
L-arginine + 7-amino-4-methylcoumarin
-
62.3% activity in comparison to L-leucine-4-methyl-coumaryl-7-amide
-
-
?
L-arginine-4-methylcoumaryl-7-amide + H2O
L-arginine + 7-amino-4-methylcoumarin
-
-
-
?
L-arginine-4-methylcoumaryl-7-amide + H2O
L-arginine + 7-amino-4-methylcoumarine
-
-
-
?
L-arginine-4-methylcoumaryl-7-amide + H2O
L-arginine + 7-amino-4-methylcoumarine
about 2% activity compared to L-leucyl-4-methylcoumaryl-7-amide
-
-
?
L-arginyl-7-amido-4-methylcoumarin + H2O
L-arginine + 7-amino-4-methylcoumarin
low activity
-
-
?
L-arginyl-7-amido-4-methylcoumarin + H2O
L-arginine + 7-amino-4-methylcoumarin
ERAP2 preferentially hydrolyzes Arg-aminomethylcoumarin and Lys-aminomethylcoumarin
-
-
?
L-arginyl-7-amido-4-methylcoumarin + H2O
L-arginine + 7-amino-4-methylcoumarin
-
70% activity compared to L-leucyl-7-amido-4-methylcoumarin
-
-
?
L-Cys-7-amido-4-methylcoumarin + H2O
L-Cys + 7-amino-4-methylcoumarin
-
-
?
L-Cys-7-amido-4-methylcoumarin + H2O
L-Cys + 7-amino-4-methylcoumarin
-
-
?
L-Cys-7-amido-4-methylcoumarin + H2O
L-Cys + 7-amino-4-methylcoumarin
-
-
?
L-glutamate 4-nitroanilide + H2O
L-glutamate + 4-nitroaniline
about 20% of the activity compared to Leu-4-nitroanilide
-
-
?
L-glutamate 4-nitroanilide + H2O
L-glutamate + 4-nitroaniline
about 20% of the activity compared to Leu-4-nitroanilide
-
-
?
L-Ile-4-nitroanilide + H2O
L-Ile + 4-nitroaniline
-
-
-
?
L-Ile-4-nitroanilide + H2O
L-Ile + 4-nitroaniline
-
-
-
-
?
L-Ile-7-amido-4-methylcoumarin + H2O
L-Ile + 7-amino-4-methylcoumarin
low activity
-
?
L-Ile-7-amido-4-methylcoumarin + H2O
L-Ile + 7-amino-4-methylcoumarin
low activity
-
?
L-Ile-7-amido-4-methylcoumarin + H2O
L-Ile + 7-amino-4-methylcoumarin
low activity
-
?
L-isoleucine 4-nitroanilide + H2O
L-isoleucine + 4-nitroaniline
14.3% of the activity compared to Leu-4-nitroanilide
-
-
?
L-isoleucine 4-nitroanilide + H2O
L-isoleucine + 4-nitroaniline
14.3% of the activity compared to Leu-4-nitroanilide
-
-
?
L-Leu 7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Leu 7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Leu 7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
-
-
-
?
L-Leu 7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
-
-
-
?
L-Leu 7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
-
-
-
?
L-Leu 7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
-
best substrate
-
-
?
L-Leu 7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
-
fluorogenic substrate assay
-
-
?
L-Leu 7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
-
-
-
?
L-Leu 7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
-
-
-
?
L-Leu-2-naphthylamide + H2O
L-Leu + 2-naphthylamine
-
-
-
-
?
L-Leu-2-naphthylamide + H2O
L-Leu + 2-naphthylamine
-
-
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
-
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
-
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
-
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
-
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
-
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
-
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
pre-LAP
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
-
-
-
?
L-Leu-4-nitroanilide + H2O
L-leucine + 4-nitroaniline
-
-
-
?
L-Leu-4-nitroanilide + H2O
L-leucine + 4-nitroaniline
-
-
-
?
L-Leu-7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
-
-
-
?
L-Leu-7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
-
best substrate
-
-
?
L-Leu-7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
-
best substrate
-
-
?
L-Leu-7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Leu-7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
best synthetic substrate
-
?
L-Leu-7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
best synthetic substrate
-
?
L-Leu-7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
best synthetic substrate
-
?
L-Leu-7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
-
-
-
?
L-Leu-7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
100% activity, LAP protein demonstrates preferential substrate specificity for Leu-7-amido-4-methylcoumarin
-
-
?
L-Leu-7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Leu-7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
-
-
-
?
L-Leu-Gly + H2O
L-Leu + Gly
-
-
-
-
?
L-Leu-Gly + H2O
L-Leu + Gly
-
-
-
?
L-Leu-Gly + H2O
L-Leu + Gly
-
-
-
-
?
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
-
-
-
?
L-Leu-p-nitroanilide + H2O
L-leucine + p-nitroaniline
-
very slow hydrolysis
-
-
?
L-Leu-p-nitroanilide + H2O
L-leucine + p-nitroaniline
-
-
-
-
?
L-Leu-p-nitroanilide + H2O
L-leucine + p-nitroaniline
-
-
-
-
?
L-Leu-p-nitroanilide + H2O
L-leucine + p-nitroaniline
-
substituted anilides, e.g. o-, m- or p-aminobenzenesulfonic acid, o- or m-anisidine, m- or p-aminobenzenesulfonylfluoride
-
-
?
L-Leu-p-nitroanilide + H2O
L-leucine + p-nitroaniline
-
Leu substituted by Ala, Gly, Lys
-
-
?
L-Leu-p-nitroanilide + H2O
L-leucine + p-nitroaniline
-
-
-
-
?
L-Leu-p-nitroanilide + H2O
L-leucine + p-nitroaniline
-
no hydrolysis
-
-
?
L-Leu-p-nitroanilide + H2O
L-leucine + p-nitroaniline
-
very slow hydrolysis
-
-
?
L-Leu-p-nitroanilide + H2O
L-leucine + p-nitroaniline
-
-
-
-
?
L-leucine 4-nitroanilide + H2O
L-leucine + 4-nitroaniline
-
-
-
?
L-leucine 4-nitroanilide + H2O
L-leucine + 4-nitroaniline
-
-
-
?
L-leucine 4-nitroanilide + H2O
L-leucine + 4-nitroaniline
-
-
-
?
L-leucine 4-nitroanilide + H2O
leucine + 4-nitroaniline
-
-
-
?
L-leucine 4-nitroanilide + H2O
leucine + 4-nitroaniline
-
-
-
?
L-leucine amide + H2O
L-leucine + NH3
-
-
-
-
?
L-leucine amide + H2O
L-leucine + NH3
-
-
-
-
?
L-leucine amide + H2O
L-leucine + NH3
-
-
-
-
?
L-leucine amide + H2O
L-leucine + NH3
-
-
-
-
?
L-leucine amide + H2O
L-leucine + NH3
-
-
-
-
?
L-leucine amide + H2O
L-leucine + NH3
-
-
-
-
?
L-leucine amide + H2O
L-leucine + NH3
-
-
-
-
?
L-leucine hydrazide + H2O
L-leucine + azide
-
-
-
-
?
L-leucine hydrazide + H2O
L-leucine + azide
-
-
-
-
?
L-leucine hydrazide + H2O
L-leucine + azide
-
-
-
-
?
L-leucine-4-methylcoumarin-7-amide + H2O
L-leucine + 7-amino-4-methylcoumarin
-
-
-
-
?
L-leucine-4-methylcoumarin-7-amide + H2O
L-leucine + 7-amino-4-methylcoumarin
-
-
-
-
?
L-leucine-4-methylcoumaryl-7-amide + H2O
L-leucine + 7-amino-4-methylcoumarin
-
-
-
?
L-leucine-4-methylcoumaryl-7-amide + H2O
L-leucine + 7-amino-4-methylcoumarin
-
-
-
?
L-leucine-4-methylcoumaryl-7-amide + H2O
L-leucine + 7-amino-4-methylcoumarin
-
-
-
-
?
L-leucine-4-methylcoumaryl-7-amide + H2O
L-leucine + 7-amino-4-methylcoumarin
-
-
-
?
L-leucine-4-methylcoumaryl-7-amide + H2O
L-leucine + 7-amino-4-methylcoumarine
-
-
-
?
L-leucine-4-methylcoumaryl-7-amide + H2O
L-leucine + 7-amino-4-methylcoumarine
-
-
-
-
?
L-leucine-4-methylcoumaryl-7-amide + H2O
L-leucine + 7-amino-4-methylcoumarine
best synthetic substrate
-
-
?
L-leucine-4-methylcoumaryl-7-amide + H2O
L-leucine + 7-amino-4-methylcoumarine
-
-
-
?
L-leucine-4-methylcoumaryl-7-amide + H2O
L-leucine + 7-amino-4-methylcoumarine
-
-
-
-
?
L-leucine-4-nitroanilide + H2O
L-leucine + 4-nitroaniline
-
-
-
-
?
L-leucine-4-nitroanilide + H2O
L-leucine + 4-nitroaniline
-
-
-
-
?
L-leucine-4-nitroanilide + H2O
L-leucine + 4-nitroaniline
-
-
-
-
?
L-leucine-4-nitroanilide + H2O
L-leucine + 4-nitroaniline
-
-
-
-
?
L-leucine-4-nitroanilide + H2O
L-leucine + 4-nitroaniline
-
-
-
-
?
L-leucine-4-nitroanilide + H2O
L-leucine + 4-nitroaniline
-
-
-
-
?
L-leucine-7-amido-4-methylcoumarin + H2O
L-leucine + 7-amino-4-methylcoumarin
-
-
-
-
?
L-leucine-7-amido-4-methylcoumarin + H2O
L-leucine + 7-amino-4-methylcoumarin
-
-
-
-
?
L-leucine-7-amido-4-methylcoumarin + H2O
L-leucine + 7-amino-4-methylcoumarin
-
-
-
?
L-leucine-p-nitroanilide + H2O
L-leucine + p-nitroaniline
-
-
-
-
?
L-leucine-p-nitroanilide + H2O
L-leucine + p-nitroaniline
-
-
-
-
?
L-leucyl-2-naphthylamide + H2O
L-leucine + 2-naphthylamine
-
-
-
-
?
L-leucyl-2-naphthylamide + H2O
L-leucine + 2-naphthylamine
-
-
-
-
?
L-leucyl-7-amido-4-methylcoumarin + H2O
L-leucine + 7-amino-4-methylcoumarin
moderate activity
-
-
?
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
ERAP1 preferentially hydrolyzes Leu-aminoacyl-aminomethylcoumarin
-
-
?
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
-
preferred substrate
-
-
?
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
best substrate
-
-
?
L-leucyl-7-amido-4-methylcoumarin + H2O
L-leucine + 7-amino-4-methylcoumarin
-
best substrate
-
-
?
L-leucylglycine + H2O
L-leucine + glycine
-
-
-
-
?
L-leucylglycine + H2O
L-leucine + glycine
-
-
-
-
?
L-Lys-4-nitroanilide + H2O
L-lysine + 4-nitroaniline
hydrolyzes L-Lys-4-nitroanilide with efficiency comparable to that of L-Leu-4-nitroanilide
-
-
?
L-Lys-4-nitroanilide + H2O
L-lysine + 4-nitroaniline
hydrolyzes L-Lys-4-nitroanilide with efficiency comparable to that of L-Leu-4-nitroanilide
-
-
?
L-lysine-4-methylcoumaryl-7-amide + H2O
L-lysine + 7-amino-4-methylcoumarin
-
-
-
?
L-lysine-4-methylcoumaryl-7-amide + H2O
L-lysine + 7-amino-4-methylcoumarin
-
-
-
?
L-lysine-4-methylcoumaryl-7-amide + H2O
L-lysine + 7-amino-4-methylcoumarin
-
-
-
?
L-lysine-4-nitroanilide + H2O
L-lysine + 4-nitroaniline
-
24.5% activity in comparison to L-leucine-4-nitroanilide
-
-
?
L-lysine-4-nitroanilide + H2O
L-lysine + 4-nitroaniline
-
24.5% activity in comparison to L-leucine-4-nitroanilide
-
-
?
L-Met-4-nitroanilide + H2O
L-Met + 4-nitroaniline
-
-
-
?
L-Met-4-nitroanilide + H2O
L-Met + 4-nitroaniline
-
-
-
-
?
L-Met-4-nitroanilide + H2O
L-Met + 4-nitroaniline
-
-
-
?
L-Met-4-nitroanilide + H2O
L-Met + 4-nitroaniline
-
pre-LAP
-
-
?
L-Met-7-amido-4-methylcoumarin + H2O
L-Met + 7-amino-4-methylcoumarin
-
no activity with Z-Met-7-amido-4-methylcoumarin
-
-
?
L-Met-7-amido-4-methylcoumarin + H2O
L-Met + 7-amino-4-methylcoumarin
-
no activity with Z-Met-7-amido-4-methylcoumarin
-
-
?
L-Met-7-amido-4-methylcoumarin + H2O
L-Met + 7-amino-4-methylcoumarin
-
-
?
L-Met-7-amido-4-methylcoumarin + H2O
L-Met + 7-amino-4-methylcoumarin
-
-
?
L-Met-7-amido-4-methylcoumarin + H2O
L-Met + 7-amino-4-methylcoumarin
-
-
?
L-Met-7-amido-4-methylcoumarin + H2O
L-Met + 7-amino-4-methylcoumarin
-
-
-
?
L-methionine 4-nitroanilide + H2O
L-methionine + 4-nitroaniline
26.3% of the activity compared to Leu-4-nitroanilide
-
-
?
L-methionine 4-nitroanilide + H2O
L-methionine + 4-nitroaniline
about 25% of the activity compared to Leu-4-nitroanilide
-
-
?
L-methionine 4-nitroanilide + H2O
L-methionine + 4-nitroaniline
about 25% of the activity compared to Leu-4-nitroanilide
-
-
?
L-methionine 4-nitroanilide + H2O
L-methionine + 4-nitroaniline
26.3% of the activity compared to Leu-4-nitroanilide
-
-
?
L-methionine-4-methylcoumaryl-7-amide + H2O
L-methionine + 7-amino-4-methylcoumarin
-
-
-
?
L-methionine-4-methylcoumaryl-7-amide + H2O
L-methionine + 7-amino-4-methylcoumarin
-
-
-
?
L-methionine-4-methylcoumaryl-7-amide + H2O
L-methionine + 7-amino-4-methylcoumarin
-
-
-
?
L-methionine-4-nitroanilide + H2O
L-methionine + 4-nitroaniline
-
29.6% activity in comparison to L-leucine-4-nitroanilide
-
-
?
L-methionine-4-nitroanilide + H2O
L-methionine + 4-nitroaniline
-
29.6% activity in comparison to L-leucine-4-nitroanilide
-
-
?
L-Phe-7-amido-4-methylcoumarin + H2O
L-Phe + 7-amino-4-methylcoumarin
-
low activity
-
-
?
L-Phe-7-amido-4-methylcoumarin + H2O
L-Phe + 7-amino-4-methylcoumarin
-
low activity
-
-
?
L-Phe-7-amido-4-methylcoumarin + H2O
L-Phe + 7-amino-4-methylcoumarin
-
-
-
?
L-phenylalanine-4-methylcoumarin-7-amide + H2O
L-phenylalanine + 7-amino-4-methylcoumarin
-
-
-
-
?
L-phenylalanine-4-methylcoumarin-7-amide + H2O
L-phenylalanine + 7-amino-4-methylcoumarin
-
-
-
-
?
L-phenylalanine-4-methylcoumaryl-7-amide + H2O
L-phenylalanine + 7-amino-4-methylcoumarin
-
-
-
?
L-phenylalanine-4-methylcoumaryl-7-amide + H2O
L-phenylalanine + 7-amino-4-methylcoumarin
-
-
-
?
L-phenylalanine-4-methylcoumaryl-7-amide + H2O
L-phenylalanine + 7-amino-4-methylcoumarin
-
-
-
?
L-phenylalanine-4-nitroanilide + H2O
L-phenylalanine + 4-nitroaniline
-
38.8% activity in comparison to L-leucine-4-nitroanilide
-
-
?
L-phenylalanine-4-nitroanilide + H2O
L-phenylalanine + 4-nitroaniline
-
38.8% activity in comparison to L-leucine-4-nitroanilide
-
-
?
L-Pro-4-nitroanilide + H2O
L-proline + 4-nitroaniline
very low activity
-
-
?
L-Pro-4-nitroanilide + H2O
L-proline + 4-nitroaniline
very low activity
-
-
?
L-proline-4-methylcoumarin-7-amide + H2O
L-proline + 7-amino-4-methylcoumarin
-
-
-
-
?
L-proline-4-methylcoumarin-7-amide + H2O
L-proline + 7-amino-4-methylcoumarin
-
-
-
-
?
L-prolyl-7-amido-4-methylcoumarin + H2O
L-proline + 7-amino-4-methylcoumarin
-
-
-
?
L-prolyl-7-amido-4-methylcoumarin + H2O
L-proline + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Trp-7-amido-4-methylcoumarin + H2O
L-Trp + 7-amino-4-methylcoumarin
low activity
-
?
L-Trp-7-amido-4-methylcoumarin + H2O
L-Trp + 7-amino-4-methylcoumarin
low activity
-
?
L-Trp-7-amido-4-methylcoumarin + H2O
L-Trp + 7-amino-4-methylcoumarin
low activity
-
?
L-tyrosyl-7-amido-4-methylcoumarin + H2O
L-tyrosine + 7-amino-4-methylcoumarin
-
7.4% activity compared to L-leucyl-7-amido-4-methylcoumarin
-
-
?
L-tyrosyl-7-amido-4-methylcoumarin + H2O
L-tyrosine + 7-amino-4-methylcoumarin
-
-
-
?
L-tyrosyl-7-amido-4-methylcoumarin + H2O
L-tyrosine + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Val-4-nitroanilide + H2O
L-Val + 4-nitroaniline
-
-
-
?
L-Val-4-nitroanilide + H2O
L-Val + 4-nitroaniline
-
-
-
-
?
Leu 4-nitroanilide + H2O
Leu + 4-nitroaniline
-
-
-
?
Leu 4-nitroanilide + H2O
Leu + 4-nitroaniline
-
-
-
?
Leu-2-naphthylamide + H2O
leucine + 2-naphthylamine
-
-
-
-
?
Leu-2-naphthylamide + H2O
leucine + 2-naphthylamine
-
-
-
-
?
Leu-2-naphthylamide + H2O
leucine + 2-naphthylamine
-
-
-
-
?
Leu-2-naphthylamide + H2O
leucine + 2-naphthylamine
-
Leu replaced by Met, Phe
-
-
?
Leu-4-methylcoumaryl-7-amide + H2O
Leu + 7-amino-4-methylcoumarin
-
-
-
?
Leu-4-methylcoumaryl-7-amide + H2O
Leu + 7-amino-4-methylcoumarin
-
-
-
?
Leu-4-nitroanilide + H2O
L-leucine + 4-nitroaniline
-
-
-
-
?
Leu-4-nitroanilide + H2O
L-leucine + 4-nitroaniline
-
-
-
-
?
Leu-4-nitroanilide + H2O
Leu + 4-nitroaniline
-
-
-
?
Leu-4-nitroanilide + H2O
Leu + 4-nitroaniline
-
best substrate
-
-
?
Leu-4-nitroanilide + H2O
Leu + 4-nitroaniline
-
-
-
?
Leu-4-nitroanilide + H2O
Leu + 4-nitroaniline
-
-
-
?
Leu-4-nitroanilide + H2O
Leu + 4-nitroaniline
-
-
-
?
Leu-4-nitroanilide + H2O
Leu + 4-nitroaniline
-
-
-
?
Leu-4-nitroanilide + H2O
Leu + 4-nitroaniline
-
-
-
-
?
Leu-4-nitroanilide + H2O
Leu + 4-nitroaniline
-
-
-
?
Leu-4-nitroanilide + H2O
Leu + 4-nitroaniline
-
-
-
?
Leu-4-nitroanilide + H2O
Leu + 4-nitroaniline
-
-
-
?
Leu-4-nitroanilide + H2O
Leu + 4-nitroaniline
-
-
-
?
Leu-4-nitroanilide + H2O
Leu + 4-nitroaniline
-
-
-
-
?
Leu-4-nitroanilide + H2O
Leu + 4-nitroaniline
-
-
-
?
Leu-4-nitroanilide + H2O
Leu + 4-nitroaniline
-
-
-
-
?
Leu-4-nitroanilide + H2O
Leu + 4-nitroaniline
-
-
-
?
Leu-7-amido-4-methylcoumarin + H2O
leucine + 7-amino-4-methylcoumarin
-
Leu replaced by Arg
-
-
?
Leu-7-amido-4-methylcoumarin + H2O
leucine + 7-amino-4-methylcoumarin
-
Leu replaced by Met
-
-
?
Leu-Arg + H2O
Leu + Arg
-
-
-
?
Leu-Arg + H2O
Leu + Arg
-
-
-
?
Leu-Arg + H2O
Leu + Arg
-
-
-
?
Leu-Asn + H2O
Leu + Asn
-
-
-
?
Leu-Asn + H2O
Leu + Asn
-
-
-
?
Leu-Asn + H2O
Leu + Asn
-
-
-
?
Leu-Asp + H2O
Leu + Asp
-
low activity
-
?
Leu-Asp + H2O
Leu + Asp
-
low activity
-
?
Leu-Gly + H2O
Leu + Gly
-
-
-
-
?
Leu-Gly + H2O
Leu + Gly
-
-
?
Leu-Gly + H2O
Leu + Gly
substrate of the Mn2+-Zn2+-enzyme and the Zn2+-Zn2+-enzyme
-
-
?
Leu-Gly + H2O
Leu + Gly
-
-
-
?
Leu-Gly + H2O
Leu + Gly
-
-
-
?
Leu-Gly + H2O
Leu + Gly
-
-
-
?
Leu-Gly + H2O
Leu + Gly
-
-
-
-
?
Leu-Gly-Gly
?
-
-
-
-
?
Leu-Gly-Gly + H2O
Leu + Gly-Gly
-
-
-
?
Leu-Gly-Gly + H2O
Leu + Gly-Gly
-
-
-
?
Leu-Gly-Gly + H2O
Leu + Gly-Gly
-
-
-
?
Leu-Leu + H2O
Leu + Leu
-
-
-
?
Leu-Leu + H2O
Leu + Leu
-
-
?
Leu-Leu + H2O
Leu + Leu
-
best dipeptide substrate
-
?
Leu-Leu + H2O
Leu + Leu
-
high activity
-
?
Leu-Leu-Leu + H2O
Leu + Leu-Leu
-
-
-
-
?
Leu-Leu-Leu + H2O
Leu + Leu-Leu
-
-
-
-
?
Leu-Met + H2O
Leu + Met
-
-
-
?
Leu-Met + H2O
Leu + Met
-
-
-
?
Leu-Met + H2O
Leu + Met
-
-
-
?
Leu-p-nitroanilide + H2O
Leu + p-nitroaniline
-
-
-
-
?
Leu-p-nitroanilide + H2O
Leu + p-nitroaniline
-
-
-
-
?
Leu-Phe + H2O
Leu + Phe
-
-
-
?
Leu-Phe + H2O
Leu + Phe
-
-
-
?
Leu-Phe + H2O
Leu + Phe
-
-
-
?
Leu-Phe + H2O
Leu + Phe
-
-
-
-
?
Leu-Ser + H2O
Leu + Ser
-
-
-
?
Leu-Ser + H2O
Leu + Ser
-
-
-
?
Leu-Ser + H2O
Leu + Ser
-
-
-
?
Leu-Trp + H2O
Leu + Trp
-
-
-
?
Leu-Trp + H2O
Leu + Trp
-
-
-
?
Leu-Trp + H2O
Leu + Trp
-
-
-
?
Leu-Tyr + H2O
Leu + Tyr
-
-
-
?
Leu-Tyr + H2O
Leu + Tyr
-
-
?
Leu-Tyr + H2O
Leu + Tyr
-
-
-
?
Leu-Tyr + H2O
Leu + Tyr
-
-
-
?
Leu-Val + H2O
Leu + Val
-
-
-
?
Leu-Val + H2O
Leu + Val
-
-
-
?
Leu-Val + H2O
Leu + Val
-
-
-
-
?
Leu-Val + H2O
Leu + Val
-
-
-
?
Leu-Val + H2O
Leu + Val
-
-
-
-
?
Lys 4-nitroanilide + H2O
Lys + 4-nitroaniline
-
-
-
?
Lys 4-nitroanilide + H2O
Lys + 4-nitroaniline
-
-
-
?
Lys-4-nitroanilide + H2O
Lys + 4-nitroaniline
20% activity compared to Leu-4-nitroanilide
-
-
?
Lys-4-nitroanilide + H2O
Lys + 4-nitroaniline
-
-
-
-
?
Lys-4-nitroanilide + H2O
Lys + 4-nitroaniline
-
-
-
?
Met 4-nitroanilide + H2O
Met + 4-nitroaniline
-
-
-
?
Met 4-nitroanilide + H2O
Met + 4-nitroaniline
-
-
-
?
Met-4-nitroanilide + H2O
Met + 4-nitroaniline
8.2% activity compared to Leu-4-nitroanilide
-
-
?
Met-4-nitroanilide + H2O
Met + 4-nitroaniline
-
-
-
?
Met-4-nitroanilide + H2O
Met + 4-nitroaniline
-
-
-
-
?
Met-4-nitroanilide + H2O
Met + 4-nitroaniline
-
-
-
?
Met-4-nitroanilide + H2O
Met + 4-nitroaniline
-
-
-
?
Met-Glu-His-Phe-Pro-Gly-Pro + H2O
?
-
semax peptide
-
-
?
Met-Glu-His-Phe-Pro-Gly-Pro + H2O
?
-
semax peptide
-
-
?
Met-Leu + H2O
Met + Leu
-
-
-
?
Met-Leu + H2O
Met + Leu
-
-
?
Met-Leu + H2O
Met + Leu
-
high activity
-
?
Met-Leu + H2O
Met + Leu
-
high activity
-
?
N-succinyl-L-Leu-4-nitroanilide + H2O
N-succinyl-L-Leu + 4-nitroaniline
-
-
-
-
?
N-succinyl-L-Leu-4-nitroanilide + H2O
N-succinyl-L-Leu + 4-nitroaniline
-
-
-
-
?
Phe-4-methylcoumaryl-7-amide + H2O
Phe + 7-amino-4-methylcoumarin
-
-
-
?
Phe-4-methylcoumaryl-7-amide + H2O
Phe + 7-amino-4-methylcoumarin
-
-
-
?
Phe-Gly + H2O
Phe + Gly
-
-
-
?
Phe-Gly + H2O
Phe + Gly
-
-
-
?
Phe-Gly + H2O
Phe + Gly
-
-
-
?
Phe-Leu + H2O
Phe + Leu
-
high activity
-
?
Phe-Leu + H2O
Phe + Leu
-
-
?
Phe-Leu + H2O
Phe + Leu
-
-
-
?
Phe-Leu + H2O
Phe + Leu
-
-
-
?
phosphatidylinositol-dependent kinase-1 + H2O
?
-
i.e. PDK1, removal of 9 amino acids from the N-terminus of the kinase, which allows S6 kinase to associate with PDK1 and the enzyme upon vascular endothelial growth factor stimulation
-
-
?
phosphatidylinositol-dependent kinase-1 + H2O
?
-
i.e. PDK1, removal of 9 amino acids from the N-terminus of the kinase
-
-
?
Pro-4-methylcoumaryl-7-amide + H2O
Pro + 7-amino-4-methylcoumarin
-
-
-
?
Pro-4-methylcoumaryl-7-amide + H2O
Pro + 7-amino-4-methylcoumarin
-
-
-
?
Pro-Leu + H2O
Pro + Leu
-
-
-
?
Pro-Leu + H2O
Pro + Leu
-
-
-
?
Pro-Leu + H2O
Pro + Leu
-
-
-
?
Proteins + H2O
?
-
oxidized beta chain of insulin
-
-
?
Proteins + H2O
?
-
Leu5-enkephalin
-
-
?
Proteins + H2O
?
-
e.g. luliberin
-
-
?
Proteins + H2O
?
-
oxidized beta chain of insulin
-
-
?
Proteins + H2O
?
-
glucagon
-
-
?
Thr-Leu + H2O
Thr + Leu
-
-
-
?
Thr-Leu + H2O
Thr + Leu
-
-
?
Thr-Leu + H2O
Thr + Leu
-
-
-
?
Thr-Leu + H2O
Thr + Leu
-
-
-
?
Trp-Leu + H2O
Trp + Leu
-
low activity
-
?
Trp-Leu + H2O
Trp + Leu
-
-
?
Trp-Leu + H2O
Trp + Leu
-
-
-
?
Trp-Leu + H2O
Trp + Leu
-
low activity
-
?
Tyr-Gly + H2O
Tyr + Gly
-
-
-
?
Tyr-Gly + H2O
Tyr + Gly
-
low activity
-
?
Tyr-Gly + H2O
Tyr + Gly
-
-
-
?
Tyr-Leu + H2O
Tyr + Leu
-
-
-
?
Tyr-Leu + H2O
Tyr + Leu
-
-
?
Tyr-Leu + H2O
Tyr + Leu
-
low activity
-
?
Tyr-Leu + H2O
Tyr + Leu
-
-
-
?
Val-Gly + H2O
Val + Gly
-
-
-
?
Val-Gly + H2O
Val + Gly
-
-
-
?
Val-Gly + H2O
Val + Gly
-
-
-
?
Val-Leu + H2O
Val + Leu
-
high activity
-
?
Val-Leu + H2O
Val + Leu
-
-
?
Val-Leu + H2O
Val + Leu
-
high activity
-
?
Val-Leu + H2O
Val + Leu
-
high activity
-
?
additional information
?
-
-
not active on Ala-para-nitranilide
-
-
?
additional information
?
-
-
not active on Ala-para-nitranilide
-
-
?
additional information
?
-
rLap1 shows the highest activity against Arg-pNA, followed by Leu-, Lys-, Met-, and Phe-4-nitroanilide in descending order
-
-
?
additional information
?
-
-
rLap1 shows the highest activity against Arg-pNA, followed by Leu-, Lys-, Met-, and Phe-4-nitroanilide in descending order
-
-
?
additional information
?
-
rLap1 shows the highest activity against Arg-pNA, followed by Leu-, Lys-, Met-, and Phe-4-nitroanilide in descending order
-
-
?
additional information
?
-
substrate specificity, overview
-
-
?
additional information
?
-
-
substrate specificity, overview
-
-
?
additional information
?
-
no activity is determined by using His-4-nitroanilide, Ile-4-nitroanilide, Ala-4-nitroanilide, Phe-4-nitroanilide, and Val-4-nitroanilide as substrates
-
-
?
additional information
?
-
-
no activity is determined by using His-4-nitroanilide, Ile-4-nitroanilide, Ala-4-nitroanilide, Phe-4-nitroanilide, and Val-4-nitroanilide as substrates
-
-
?
additional information
?
-
-
esterase activity
-
-
?
additional information
?
-
-
use in sequence determination
-
-
?
additional information
?
-
-
transferase activity
-
-
?
additional information
?
-
-
no hydrolysis of Xaa-Pro bond
-
-
?
additional information
?
-
molecular modelling of enzyme-substrate conformation, no activity with Asp-Gly
-
?
additional information
?
-
-
molecular modelling of enzyme-substrate conformation, no activity with Asp-Gly
-
?
additional information
?
-
-
the enzyme has tissue-specifici physiological roles, overview, active site structure and zinc-binding, mechanism
-
-
?
additional information
?
-
no activity with Ser-Gly and Asp-Gly
-
-
?
additional information
?
-
-
no activity with Ser-Gly and Asp-Gly
-
-
?
additional information
?
-
the enzyme prefers peptide substrates with bulky and hydrophobic N-terminal amino acid residues
-
-
?
additional information
?
-
-
the enzyme prefers peptide substrates with bulky and hydrophobic N-terminal amino acid residues
-
-
?
additional information
?
-
-
the enzyme acts as aminopeptidase and endopeptidase and might be a cysteine type peptidase, no activity with N-blocked substrate, Gly-4-nitroanilide, Arg-4-nitroanilide, and Lys-4-nitroanilide are poor substrates, Glu-4-nitroanilide is no substrate
-
-
?
additional information
?
-
-
enzyme activity is regulated on the transcriptional level
-
?
additional information
?
-
-
substrate specificity study, Asp-Leu, Pro-Gly, Lys-Gly, Ser-Gly, Arg-Lys, Arg-Asp, Gly-Ala, Gly-Val, Gly-Trp, Gly-Gln, Gly-Gly, Gly-Lys, Gly-His, and Leu-Pro are poor substrates, Gly-Asn, Asp-Gly, Gly-Arg, and Gly-Asn are no substrates
-
?
additional information
?
-
PepA-induced DNA deformations revealed by DNase I footprinting and AFM imaging of 1:1 stoichiometric PepA-DNA complexes
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
broad substrate specificity towards naturally occurring peptide hormones, while the enzyme hydrolyzes synthetic substrate in vitro with specificity for leucine, enzyme plays a role in regulation of blood pressure through the inactivation of angiotensin II and/or the generation of bradykinin in the kidney
-
?
additional information
?
-
-
A-LAP plays a key role in the MHC class I antigen-presentation pathway, the enzyme is involved in the renin-angiotensin-system, RAS, and angiotensin II metabolism, and plays a role in blood pressure decrease through inactivation of angiotensin II, overview
-
-
?
additional information
?
-
-
enzyme inhibition causes hypertension
-
-
?
additional information
?
-
-
the enzyme has tissue-specifici physiological roles, e.g. trimmíng of the N-terminus of antigenic peptides for presentation or in eye cataract, overview
-
-
?
additional information
?
-
-
the enzyme is involved in peptide trimming, e.g. for the generation of most HLA class I-binding peptide, in the endoplasmic reticulum in concert with other aminopeptidases, overview
-
-
?
additional information
?
-
the enzyme is involved in peptide trimming, e.g. for the generation of most HLA class I-binding peptide, in the endoplasmic reticulum in concert with other aminopeptidases, overview
-
-
?
additional information
?
-
-
the enzyme is involved in processing of precursor peptides, and in destruction of antigenic peptides to limit antigen presentation to MHC class I molecules in the endoplasmic reticulum lumen, pathway overview
-
-
?
additional information
?
-
-
the enzyme hydrolyses with Leu or Met in the P1 position
-
-
?
additional information
?
-
no activity with any other L-amino acid amide, N-carboxybenzyloxy-L-Leu-beta-naphthylamide, and N-carboxybenzyloxy-Gly-Gly-Leu-4-nitroanilide
-
?
additional information
?
-
no activity with any other L-amino acid amide, N-carboxybenzyloxy-L-Leu-beta-naphthylamide, and N-carboxybenzyloxy-Gly-Gly-Leu-4-nitroanilide
-
?
additional information
?
-
no activity with any other L-amino acid amide, N-carboxybenzyloxy-L-Leu-beta-naphthylamide, and N-carboxybenzyloxy-Gly-Gly-Leu-4-nitroanilide
-
?
additional information
?
-
little or no activity against L-Val 7-amido-4-methylcoumarin and L-Pro 7-amido-4-methylcoumarin is detected
-
-
?
additional information
?
-
-
the enzyme is required for DNA synthesis and plays an important role in angiogenesis by regulating the proliferation and migration of endothelial cells, mechanism via vascular endothelial growth factor and stimulation of S6 kinase, overview
-
-
?
additional information
?
-
-
PILSAP is required for the development of vascular as well as hematopoietic system in embryoid bodies
-
-
?
additional information
?
-
-
the enzyme affects RhoA activation and that influences the proper function of endothelial cells
-
-
?
additional information
?
-
MHJ_0461 binds heparin and interacts with DNA
-
-
?
additional information
?
-
-
MHJ_0461 binds heparin and interacts with DNA
-
-
?
additional information
?
-
rMHJ_0461 binds plasminogen and facilitates plasmin conversion
-
-
?
additional information
?
-
-
rMHJ_0461 binds plasminogen and facilitates plasmin conversion
-
-
?
additional information
?
-
-
alterations in intensity and number of isozymes in cold-acclimated plants, bark and leaf
-
-
?
additional information
?
-
-
no activity towards L-prolyl-7-amido-4-methylcoumarin, L-valyl-7-amido-4-methylcoumarin, L-glycyl-7-amido-4-methylcoumarin, tert-butyloxycarbonyl-Phe-Ser-Arg-7-amido-4-methylcoumarin, tert-butyloxycarbonyl-Leu-Arg-Arg-7-amido-4-methylcoumarin, and tert-butyloxycarbonyl-Leu-Lys-Arg-7-amido-4-methylcoumarin
-
-
?
additional information
?
-
-
the enzyme hydrolyses with Leu or Met in the P1 position, the residues at P1', P2'a nd P3' positions influence the activity
-
-
?
additional information
?
-
-
the enzyme is important in the generation and regulation of free amino acids that are used in protein anabolism and for maintaining osmotic stability within the infected erythrocyte, enzyme inhibition, e.g. by bestatin, blocks intraerythrocytic development of malaria parasites
-
-
?
additional information
?
-
-
the enzyme functions in the terminal stages of hemoglobin digestion
-
-
?
additional information
?
-
the enzyme generates and regulates the internal pool of free amino acids and therefore represents a target for antimalarial drugs
-
-
?
additional information
?
-
-
the enzyme generates and regulates the internal pool of free amino acids and therefore represents a target for antimalarial drugs
-
-
?
additional information
?
-
-
the type of metal ion present at site 1 influences the catalytic efficiency of the enzyme for peptide substrates
-
-
?
additional information
?
-
-
the enzyme functions in the terminal stages of hemoglobin digestion
-
-
?
additional information
?
-
the enzyme generates and regulates the internal pool of free amino acids and therefore represents a target for antimalarial drugs
-
-
?
additional information
?
-
-
the enzyme generates and regulates the internal pool of free amino acids and therefore represents a target for antimalarial drugs
-
-
?
additional information
?
-
M17 leucine aminopeptidase LAP is a cytosolic metallo-exopeptidase that catalyzes the removal of amino acids from the peptide generated in the process of hemoglobin degradation
-
-
?
additional information
?
-
-
M17 leucine aminopeptidase LAP is a cytosolic metallo-exopeptidase that catalyzes the removal of amino acids from the peptide generated in the process of hemoglobin degradation
-
-
?
additional information
?
-
-
not active on Ala-para-nitranilide
-
-
?
additional information
?
-
when assayed with short chromogenic peptides, PhTET2 is an aminopeptidase, with a clear preference for leucine as the N-terminal amino acid. The enzyme can cleave moderately long polypeptide substrates of various compositions in a fairly unspecific manner. The hydrolytic mechanism is nonprocessive. The enzyme has neither carboxypeptidase nor endoproteolytic activities, and it is devoid of N-terminal deblocking activity
-
-
?
additional information
?
-
-
when assayed with short chromogenic peptides, PhTET2 is an aminopeptidase, with a clear preference for leucine as the N-terminal amino acid. The enzyme can cleave moderately long polypeptide substrates of various compositions in a fairly unspecific manner. The hydrolytic mechanism is nonprocessive. The enzyme has neither carboxypeptidase nor endoproteolytic activities, and it is devoid of N-terminal deblocking activity
-
-
?
additional information
?
-
when assayed with short chromogenic peptides, PhTET2 is an aminopeptidase, with a clear preference for leucine as the N-terminal amino acid. The enzyme can cleave moderately long polypeptide substrates of various compositions in a fairly unspecific manner. The hydrolytic mechanism is nonprocessive. The enzyme has neither carboxypeptidase nor endoproteolytic activities, and it is devoid of N-terminal deblocking activity
-
-
?
additional information
?
-
-
proteolysis of ACTH-(6-9)-PGP peptide in rat blood and plasma occurs mainly under the effect of enzymes whose action is similar to leucine aminopeptidase
-
-
?
additional information
?
-
-
substrate synthesis and application to rats, overview. LC-MS analysis of reaction products after reaction of His-Phe-Arg-Trp-Pro-Gly-Pro with leucine aminopeptidase, carboxypeptidase Y, and rat nasal mucus, blood, and plasma
-
-
?
additional information
?
-
-
proteolysis of ACTH-(6-9)-PGP peptide in rat blood and plasma occurs mainly under the effect of enzymes whose action is similar to leucine aminopeptidase
-
-
?
additional information
?
-
-
substrate synthesis and application to rats, overview. LC-MS analysis of reaction products after reaction of His-Phe-Arg-Trp-Pro-Gly-Pro with leucine aminopeptidase, carboxypeptidase Y, and rat nasal mucus, blood, and plasma
-
-
?
additional information
?
-
substrate specificity study, overview, Lys-Leu, Gly-Leu, Arg-Leu, and Pro-Leu are poor or no substrates
-
?
additional information
?
-
no growth on QL, FL, YL, WL, IL, VL, KL, GL, RL, and PL
-
?
additional information
?
-
-
substrate specificity of SmLAP2, fluorogenic substrate assay, overview. No or poor activity with L-Pro 7-amido-4-methylcoumarin, L-Gly 7-amido-4-methylcoumarin, and L-Ser 7-amido-4-methylcoumarin
-
-
?
additional information
?
-
-
the enzyme probably is involved in fertility and parasite survival
-
-
?
additional information
?
-
-
the enzyme is digestive alkaline protease
-
-
?
additional information
?
-
-
substrate specificity study, Asp-Leu, Pro-Gly, Gly-Gly, Cys-Gly, Ser-Gly, Gly-Trp, Gly-Pro, Gly-His, Gly-Lys and Lys-Gly are poor substrates, Asp-Gly, Leu-Asp, Arg-Lys, Arg-Asp, Gly-Asn, Gly-Gln, and Leu-Pro are no substrates
-
?
additional information
?
-
-
substrate specificty of wild-type and mutant enzymes, overview
-
?
additional information
?
-
-
no activity towards substrates with Asp or Glu at position P1, Arg431 and Lys354 of LAP-A1 are involved in catalysis
-
-
?
additional information
?
-
-
the enzyme is equally active with the synthetic substrates
-
-
?
additional information
?
-
-
the substrate range of LAP is quite complex. L-Leu is not the preferred substrate of the enzyme
-
-
?
additional information
?
-
-
use in sequence determination
-
-
?
additional information
?
-
-
use in sequence determination
-
-
?
additional information
?
-
-
no hydrolysis of Xaa-Pro bond
-
-
?
additional information
?
-
-
broad substrate specificity
-
-
?
additional information
?
-
-
substrate specificity study, Asp-Leu, Pro-Gly, Gly-Gly, Ser-Gly, Arg-Lys, Gly-Ala, Gly-Gln, Gly-His, Gly-Val and Lys-Gly are poor substrates, Asp-Gly, Arg-Asp, Gly-Arg, Gly-Asn, Gly-Lys, and Leu-Pro are no substrates
-
?
additional information
?
-
-
the enzyme has tissue-specifici physiological roles, overview
-
-
?
additional information
?
-
-
substrate specificity, overview, active site structure
-
-
?
additional information
?
-
-
substrate synthesis and assay method optimization, overview
-
-
?
additional information
?
-
-
2-naphthylamine can be detected with Fast Black K reactant and monitored spectrophotometrically at 590 nm
-
-
?
additional information
?
-
little or no activity against L-Val 7-amido-4-methylcoumarin and L-Pro 7-amido-4-methylcoumarin is detected
-
-
?
additional information
?
-
little or no activity against L-Val 7-amido-4-methylcoumarin and L-Pro 7-amido-4-methylcoumarin is detected
-
-
?
additional information
?
-
PepA functions as a transcriptional repressor in regulatory cascade that controls virulence gene expression in Vibrio cholerae
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
esterase activity
-
-
?
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(4S)-4-amino-4,5-dihydro-2H-pyrazolo[3,4-f]quinoline-3-carboxylic acid
-
(4S)-4-amino-7-methyl-4,5-dihydro-2H-pyrazolo[3,4-f]quinazoline-3-carboxylic acid
-
(4S)-4-amino-8-ethyl-2,4,5,7-tetrahydropyrazolo[3,4-e]indazole-3-carboxylic acid
-
(4S)-4-amino-9-methyl-4,5-dihydro-2H-pyrazolo[3,4-f]quinoline-3-carboxylic acid
-
(4S)-4-amino-9-methyl-4,5-dihydro[1,2]oxazolo[5,4-f]quinoline-3-carboxylic acid
-
(CH3)2CHCH2CH(NH2)CO-X
-
X: e.g. succinamide,-CH3,-CH2Cl
2-amino-1,4-dihydro-2-isoquinolin-3-one
-
-
2-[(3-azaniumyl-2-hydroxy-4-phenylbutanoyl)amino]-4-methylpentanoate
the binding mode of the inhibitor is confirmed by a molecular dynamics (MD) simulation study, evaluation of the drug likeness
2-[[(1-amino-3-methylbutyl)hydroxyphosphinyl]methyl]-4-methylpentanoic acid
-
(R)-isomer and 1:1 ratio of the 2 diastereomers
2-[[(1-amino-4-phenylbutyl)hydroxyphosphinyl]methyl]-3-(4-hydroxyphenyl)propionic acid
-
-
2-[[(1-amino-4-phenylbutyl)hydroxyphosphinyl]methyl]-3-phenylpropionic acid
-
-
2-[[(1-amino-4-phenylbutyl)hydroxyphosphinyl]methyl]-4-methylpentanoic acid
-
-
3-amino-1,2,3,4-tetrahydronaphthalene-2-carbohydroxamic acid
-
-
3-[(1-amino-3-methylbutyl)hydroxyphosphinyl]-propionic acid
-
-
4,7-phenanthroline
-
0.5 mM, 95% activity
4-amino-3-(L-arginylamino)benzoic acid
-
4-amino-3-(L-tyrosylamino)benzoic acid
-
4-amino-6,7-dimethyl-2,4,5,6-tetrahydropyrrolo[2,3-g]indazole-3-carboxylic acid
-
4-chloromercuribenzoate
-
inhibition of isozymes LAP1, LAP2, and LAP3
4-chloromercuriphenylsulfonic acid
-
strong inhibition
As3+
-
arsenic is inhibitory for enzyme activity in roots as well as shoots. In both the cultivars (L. cvs. Malviya-36 and Pant-12) 50 mM As3+ treatment leads to about 5560% inhibition in roots at 20 d of growth; L. cvs. Malviya-36 and Pant-12. For seedlings in both the cultivars (L. cvs. Malviya-36 and Pant-12) 50 mM As3+ treatment leads to about 6281% inhibition in LAP activity; L. cvs. Malviya-36 and Pant-12.
autogenous low molecular weight inhibitor
-
regulatory function, modulation during periods of intensive polyketide antibiotics formation
-
bacitracin
-
87.7% activity at 0.02 mM
benzyl N-(3-amino-4-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-tryptophanate
-
benzyl N-(3-amino-4-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-valinate
-
benzyl N-(4-amino-3-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-tryptophanate
-
benzyl N-[(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl]-L-leucinate
-
benzyl N-[3-amino-4-(L-leucylamino)benzoyl]-L-tryptophanate
-
benzyl N-[3-amino-4-(L-norleucylamino)benzoyl]-L-tryptophanate
-
benzyl N-[3-amino-4-(L-norleucylamino)benzoyl]-L-valinate
-
benzyl N-[3-amino-4-([(2S)-2-amino-4-[4-(benzyloxy)phenyl]butanoyl]amino)benzoyl]-L-tryptophanate
-
benzyl N-[3-amino-4-[(O-benzyl-L-tyrosyl)amino]benzoyl]-L-tryptophanate
-
benzyl N-[4-amino-3-(D-norleucylamino)benzoyl]-L-valinate
-
benzyl N-[4-amino-3-(L-norleucylamino)benzoyl]-L-tryptophanate
-
benzyl N-[4-amino-3-(L-tyrosylamino)benzoyl]-L-tryptophanate
-
benzyl N-[4-amino-3-(L-tyrosylamino)benzoyl]-L-valinate
-
benzyl N-[4-amino-3-[(O-benzyl-L-tyrosyl)amino]benzoyl]-L-tryptophanate
-
Chloroquine
1 mM, 70% inhibition
citrate
-
10 mM and 20 mM, 15% inhibition
Cys-Gly
inhibits the activity of the Zn2+-Zn2+-enzyme with substrate Leu-Gly competitively
D,L-Alpha-hydroxyisocaproamide
diisopropylfluorophosphate
-
-
Dodecylamino aliphatic alcohols
-
-
-
E-64
-
40.4% residual activity at 0.015 mM
guanidinium hydrochloride
-
hexameric LAP is almost completely inactivated, showing 0.6% residual activity, by incubation with 2.5 M GuHCl and 40 mM DTT for 3 h at room temperature
Leu
-
41.5% activity at 1 mM
Leu-Gly
inhibits the activity of the Mn2+-Zn2+-enzyme with substrate Cys-Gly competitively
leupeptin
0.01 mg/ml, 12% inhibition
methyl 3-amino-4-(L-arginylamino)benzoate
-
methyl 3-amino-4-(L-leucylamino)benzoate
-
methyl 3-amino-4-(L-norleucylamino)benzoate
-
methyl 3-amino-4-(L-tyrosylamino)benzoate
-
methyl 3-amino-4-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoate
-
methyl 4-amino-3-(L-arginylamino)benzoate
-
methyl 4-amino-3-(L-norleucylamino)benzoate
-
methyl 4-amino-3-(L-tyrosylamino)benzoate
-
methyl 4-amino-3-[[(2S)-2-amino-4-(4-hydroxyphenyl)butanoyl]amino]benzoate
-
methyl N-(3,4-diaminobenzoyl)-L-tyrosinate
-
methyl N-(3-amino-4-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-tyrosinate
-
methyl N-(4-amino-3-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-tyrosinate
-
methyl N-[3-amino-4-(L-arginylamino)benzoyl]-L-tyrosinate
-
methyl N-[3-amino-4-(L-norleucylamino)benzoyl]-L-tyrosinate
-
methyl N-[3-amino-4-(L-tyrosylamino)benzoyl]-L-tyrosinate
-
methyl N-[3-amino-4-[(O-benzyl-L-tyrosyl)amino]benzoyl]-L-tyrosinate
-
methyl N-[4-amino-3-(D-norleucylamino)benzoyl]-D-tyrosinate
-
methyl N-[4-amino-3-(L-arginylamino)benzoyl]-D-tyrosinate
-
methyl N-[4-amino-3-(L-tyrosylamino)benzoyl]-L-threoninate
-
methyl N-[4-amino-3-(L-tyrosylamino)benzoyl]-L-tyrosinate
-
methyl N2-(3,4-diaminobenzoyl)-L-argininate
-
methyl N2-(3,4-diaminobenzoyl)-L-lysinate
-
methyl N2-(3-amino-4-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-argininate
-
methyl N2-(4-amino-3-[[(2S)-2-amino-4-(4-hydroxyphenyl)butanoyl]amino]benzoyl)-L-lysinate
-
methyl N2-(4-amino-3-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-lysinate
-
methyl N2-[3-amino-4-(L-arginylamino)benzoyl]-L-lysinate
-
methyl N2-[3-amino-4-(L-norleucylamino)benzoyl]-L-lysinate
-
methyl N2-[3-amino-4-(L-tyrosylamino)benzoyl]-L-lysinate
-
methyl N2-[4-amino-3-(L-arginylamino)benzoyl]-L-lysinate
-
methyl N2-[4-amino-3-(L-leucylamino)benzoyl]-L-lysinate
-
methyl N2-[4-amino-3-(L-norleucylamino)benzoyl]-D-argininate
-
methyl N2-[4-amino-3-(L-norleucylamino)benzoyl]-L-lysinate
-
methyl N2-[4-amino-3-([(2S)-2-amino-4-[4-(benzyloxy)phenyl]butanoyl]amino)benzoyl]-L-lysinate
-
N-(3,4-diaminobenzoyl)-L-tryptophan
-
N-(3-amino-4-[[(2S)-2-amino-4-(4-hydroxyphenyl)butanoyl]amino]benzoyl)-L-tryptophan
-
N-(3-amino-4-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-valine
-
N-(4-amino-3-[[(2R)-2-amino-4-(4-hydroxyphenyl)butanoyl]amino]benzoyl)-L-tryptophan
-
N-(Leucyl)-o-aminobenzenesulfonic acid
N-[(1-hydroxy-3-methylbutyl)oxyphosphinyl]glycine dilithium salt
-
-
N-[(2R,3R)-3-amino-2-hydroxy-4-phenylbutanoyl]-D-leucine
-
N-[3-amino-4-(L-arginylamino)benzoyl]-L-tryptophan
-
N-[3-amino-4-(L-norleucylamino)benzoyl]-L-tryptophan
-
N-[3-amino-4-(L-norleucylamino)benzoyl]-L-valine
-
N-[3-amino-4-(L-tyrosylamino)benzoyl]-L-tryptophan
-
N-[4-amino-3-(D-norleucylamino)benzoyl]-L-valine
-
N-[4-amino-3-(L-arginylamino)benzoyl]-L-tryptophan
-
N-[4-amino-3-(L-arginylamino)benzoyl]-L-valine
-
N-[4-amino-3-(L-norleucylamino)benzoyl]-L-tryptophan
-
N-[4-amino-3-(L-tyrosylamino)benzoyl]-L-tryptophan
-
N-[4-amino-3-(L-tyrosylamino)benzoyl]-L-valine
-
N2-[4-amino-3-(L-leucylamino)benzoyl]-L-lysine
-
N2-[4-amino-3-(L-phenylalanylamino)benzoyl]-L-lysine
-
N2-[4-amino-3-(L-tyrosylamino)benzoyl]-L-lysine
-
p-Hydroxymercuriphenylsulfonate
-
-
pepstatin
-
83.4% residual activity at 0.15 mM
Phe
-
33.5% activity at 1 mM
phenylmethanesulfonyl fluoride
-
94.94% residual activity at 1 mM
tetraethylene pentamine
-
1 mM, completely inhibited
trans-epoxy-succinyl-L-leucylamido(4-guanidino)butane
-
E64
Trp
-
40.7% activity at 1 mM
ubenimex
suppresses the enzyme activity in vivo in K562-LAP3 cells, detection method development and evaluation, overview
zofenoprilat
competitive versus Leu-Gly with the Zn2+-Zn2+-enzyme, uncompetitive with the Mn2+-Zn2+-enzyme, binding structure analysis
1,10-phenanthroline
abolishes enzyme activity at 10 mM
1,10-phenanthroline
7.2% residual activity at 1 mM
1,10-phenanthroline
-
3.3% activity at 0.2 mM
1,10-phenanthroline
-
86.3% inhibition at 5 mM
1,10-phenanthroline
-
87.8% inhibition at 5 mM
1,10-phenanthroline
strong inhibition
1,10-phenanthroline
strong inhibition
1,10-phenanthroline
strong inhibition
1,10-phenanthroline
-
non-competitive
1,10-phenanthroline
-
31.1% residual activity at 0.2 mM
1,10-phenanthroline
30.4% residual activity at 1 mM
1,10-phenanthroline
16% inhibition at 1 mM, 77% at 10 mM
1,10-phenanthroline
-
0.5 mM, completely inhibited
1,10-phenanthroline
61.5% inhibition at 5 mM
1,10-phenanthroline
-
71% inhibition at 5 mM
1,10-phenanthroline
-
inhibits SmLAP2
1,10-phenanthroline
1 mM, 38% inhibition
1,10-phenanthroline
-
5.0 mM, 55% inhibition
1,10-phenanthroline
-
75% inhibition at 2 mM
1,10-phenanthroline
-
strong inhibition
1,10-phenanthroline
0.25 mM: 17% activity, restored by Mn2+ and Ca2+
1,7-phenanthroline
slight inhibition
1,7-phenanthroline
slight inhibition
1,7-phenanthroline
slight inhibition
1,7-phenanthroline
-
0.5 mM, 93% activity
1-butanol
-
-
2,2'-dipyridyl
-
-
2-mercaptoethanol
-
-
2-mercaptoethanol
strong inhibition
actinonin
tight-binding, competitive inhibitor
actinonin
tight-binding, competitive inhibitor
actinonin
tight-binding, competitive inhibitor
actinonin
3-((1-((2-[hydroxymethyl]-1-pyrrolidinyl)carbonyl)-2-methylpropyl)carbamoyl)octanohydroxaminic acid, actinonin in LmLAP-A is coordinated by the Mn2+ ions and hydrogen bonds
actinonin
3-((1-((2-[hydroxymethyl]-1-pyrrolidinyl)carbonyl)-2-methylpropyl)carbamoyl)octanohydroxaminic acid. Actinonin in TbLAP-A is coordinated by the Mn2+ ions and hydrogen bonds, overview
actinonin
3-((1-((2-[hydroxymethyl]-1-pyrrolidinyl)carbonyl)-2-methylpropyl)carbamoyl)octanohydroxaminic acid
Al3+
-
98% inhibition at 2 mM, complete inhibition at 10 mM
aliphatic alcohols
-
methanol to n-hexanol
aliphatic alcohols
-
methanol to n-hexanol
alpha-keto-isocaproamide
-
-
alpha-keto-isocaproamide
-
-
amastatin
-
natural inhibitor
amastatin
-
transition-state analogue
amastatin
-
transition-state analogue, low toxicity in vivo
amastatin
-
0.01 mM, 81% inhibition
amastatin
-
inhibition of LAP-A1
amastatin
-
strong inhibition
amastatin
-
natural inhibitor
amastatin
-
transition-state analogue
Amino acid hydroxamates
-
-
Amino acid hydroxamates
-
-
apstatin
strong inhibition
apstatin
strong inhibition
apstatin
strong inhibition
arphamenine A
non-tight-binding, competitive inhibitor
arphamenine A
non-tight-binding, competitive inhibitor
arphamenine A
non-tight-binding, competitive inhibitor
Ba2+
-
slight inhibitory effect at 1 mM
Ba2+
-
1 mM, 74% inhibition
bestatin
inhibits enzyme activity by 77% at 0.1 mM
bestatin
-
28.3% activity at 0.02 mM
bestatin
-
natural inhibitor
bestatin
-
transition-state analogue
bestatin
0.4% residual activity at 0.001 mM
bestatin
-
16.4% activity at 0.05 mM
bestatin
-
92.5% inhibition at 0.3 mM
bestatin
-
87.0% inhibition at 0.3 mM
bestatin
-
transition-state analogue
bestatin
strong inhibition
bestatin
strong inhibition
bestatin
strong inhibition
bestatin
-
22.3% residual activity at 0.01 mM
bestatin
18.9% residual activity at 0.05 mM
bestatin
-
transition-state analogue, complete inhibition
bestatin
antimalarial activity of aminopeptidase inhibitors
bestatin
-
a metal-chelating inhibitor of M17 aminopeptidases with antimalarial activity, the type of metal ion present at site 1 influences the mode of binding by bestatin
bestatin
17% inhibition at 0.01 mM, 88% at 0.1 mM
bestatin
[(2S,3R)-3-amino-2-hydroxy-4-phenyl-butanoyl]-L-leucine, a potent and slow binding inhibitor
bestatin
0.05 mM 35.6% inhibition
bestatin
complete inhibition at 37° and 1 mM within 20 min
bestatin
nearly complete inhibition at 0.05 mM
bestatin
-
nearly complete inhibition at 0.05 mM
bestatin
-
a specific inhibitor of aminopeptidase; a specific inhibitor of aminopeptidase, complete inhibition
bestatin
100 ng/ml, 29% inhibition, competitive
bestatin
-
0.001 mM, 58% inhibition
bestatin
-
inhibition of LAP-A1
bestatin
-
natural inhibitor
bestatin
-
transition-state analogue
bestatin
-
slow-binding, competitive
bestatin
complete inhibition at 20 nM
bestatin
0.1 mM: 3% activity, activity
Ca2+
-
70% inhibition at 2 mM
Ca2+
68.4% inhibition at 1 mM
Ca2+
-
partially inactivated at 1 mM
Ca2+
complete inhibition at 0.1-10 mM
Ca2+
-
slight inhibitory effect at 1 mM
Ca2+
40% inhibition at 1 mM, 54% at 10 mM
Cd2+
-
80% inhibition at 2 mM
Cd2+
-
strongly inactivated at 1 mM
Cd2+
-
at concentration of 1 mM, the enzyme is strongly inactivated by Cd2+ (38.2% residual activity)
Cd2+
complete inhibition at 10 mM
Cd2+
-
1 mM, 96% inhibition
Cd2+
0.1 mM, 93% loss of activity
CN-
-
-
Co2+
activates at 0.1-1.0 mM, inhibitory at 1.0-10 mM
Co2+
-
39% activation at 2 mM, 40% inhibition at 10 mM
Co2+
-
activates at 2 mM, inhibits at 10 mM and above
Co2+
17% inhibition at 1 mM, 63% at 10 mM
Co2+
0.1 mM, 86% loss of activity
Cu2+
-
86% inhibition at 2 mM, complete inhibition at 10 mM
Cu2+
-
2 mM: 4.5% activity in crude enzyme solution
Cu2+
slight inhibition at 1 mM
Cu2+
-
strongly inactivated at 1 mM
Cu2+
93% inhibition at 1 mM
Cu2+
-
at concentration of 1 mM, the enzyme is strongly inactivated by Cu2+ (2.3% residual activity)
Cu2+
complete inhibition at 0.1 mM
Cu2+
-
1 mM, 75% inhibition
Cu2+
-
at concentrations higher than 0.1 mM
Cu2+
0.1 mM, 86% loss of activity
cysteine
-
competitive
cysteine
-
20% inhibition at 2 mM
D,L-Alpha-hydroxyisocaproamide
-
-
D,L-Alpha-hydroxyisocaproamide
-
-
dithiothreitol
-
-
dithiothreitol
-
10 mM, completely inhibited
DL-thiorphan
slight inhibition at 0.1 mM
DL-thiorphan
slight inhibition at 0.1 mM
DL-thiorphan
slight inhibition at 0.1 mM
DTT
-
3.6% activity at 1 mM
DTT
complete inhibition at 1 mM, 50°C, 1 h
EDTA
abolishes enzyme activity at 1 mM
EDTA
-
almost completely inhibited at 1 mM
EDTA
significant inhibition, Co2+, Mn2+, and Ca2+ ions, but not Zn2+ ions, restore the enzyme activity
EDTA
complete inhibition at 1 mM, 50°C, 1 h, the activity can be restored by Co2+ and partially by Zn2+
EDTA
6.7% residual activity at 1 mM
EDTA
-
40.7% activity at 5 mM, 6.7% activity after extensive dialysis against 5 mM, restored to 60.1% with 0.05 mM Zn2+
EDTA
-
reactivation by divalent cations
EDTA
-
strong inhibitor, the enzyme loses 83% of its activity when it is dialyzed extensively against 1 mM EDTA in 25 mM sodium phosphate buffer (pH 7.0), whereas the loss can be restored by Zn2+ to 97% at 0.05 mM and to 81% at 0.1 mM of its original activity, the recovery of enzymatic activity by Mn2+ reaches 94% at 0.5 mM and 79% at 1 mM, on the other hand, the enzymatic activity recovery by Ca2+ and Mg2+ is lower than that by Zn2+ and Mn2+, the former reaches 46% and the latter, 26%, at 1 mM
EDTA
21.3% residual activity at 10 mM
EDTA
38% inhibition at 1 mM, 97% at 10 mM
EDTA
-
10 mM, 60% activity
EDTA
2 mM, 80% inhibition
EDTA
inactivation can be restored by divalent cations
EDTA
-
50% inhibition at 5 mM
EDTA
-
inhibits SmLAP2, complete inhibition
EDTA
1 mM, 56% inhibition
EDTA
-
10 mM, 93% inhibition
EDTA
complete inhibition at 0.15 mM
EDTA
0.1 mM, complete inhibition
EDTA
10 mM: 55% activity, restored by Mn2+ and Ca2+
EGTA
-
43.7% activity at 5 mM
EGTA
-
25.4% residual activity at 5 mM
EGTA
-
10 mM, 48% activity
Fe2+
-
15% activation at 2 mM, 55% inhibition at 10 mM
Fe2+
-
2 mM: 37.9% activity in crude enzyme solution
Fe2+
-
strongly inactivated at 1 mM
Fe2+
complete inhibition at 1-10 mM
Fe2+
-
partially inactivated by Fe2+ (53.9% residual activity at 1 mM)
Fe2+
-
1 mM, 73% inhibition
Fe3+
-
-
glycerol
-
-
GSH
slight inhibition
Hg2+
-
-
iodoacetic acid
-
slight inhibition
Isocaproic acid
-
-
L-leucine
-
competitive
L-Leucinol
-
-
L-Leucinol
non-tight-binding, competitive inhibitor
L-Leucinol
non-tight-binding, competitive inhibitor
L-Leucinol
non-tight-binding, competitive inhibitor
L-leucylthiol
-
-
leucinal
-
-
leucine phosphonic acid
-
-
leucine phosphonic acid
-
-
Mg2+
-
50% inhibition at 2 mM
Mg2+
slight inhibition at 1 mM
Mg2+
34% inhibition at 1 mM, 55% at 10 mM
Mn2+
activates at 0.1-1.0 mM, inhibitory at 1.0-10 mM
Mn2+
-
60% inhibition at 2 mM
Mn2+
slight inhibition at 1 mM
Mn2+
-
partially inactivated at 1 mM
Mn2+
-
slight inhibitory effect at 1 mM
Mn2+
19% inhibition at 1 mM, 53% at 10 mM
Mn2+
0.5 mM, around 50% inhibition
Mn2+
-
at concentrations higher than 0.1 mM
N-(Leucyl)-o-aminobenzenesulfonic acid
-
-
N-(Leucyl)-o-aminobenzenesulfonic acid
-
similar derivatives
N-ethylmaleimide
-
-
N-ethylmaleimide
-
5 mM, 95% activity
Ni2+
activates at 0.1-1.0 mM, inhibitory at 1.0-10 mM
Ni2+
92.5% inhibition at 1 mM
Ni2+
-
1 mM, 55% inhibition
Ni2+
-
at concentrations higher than 0.1 mM
nitrobestatin
-
95.1% inhibition at 0.133 mM
o-phenanthroline
10 mM, abolishes enzyme activity in presence or absence of Co2+
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
P2O4-
-
-
Pb2+
-
2 mM: 5.9% activity in crude enzyme solution
Pb2+
-
1 mM, 60% inhibition
Pb2+
0.1 mM, 84% loss of activity
phosphoramidon
slight inhibition at 0.1 mM
phosphoramidon
slight inhibition at 0.1 mM
phosphoramidon
slight inhibition at 0.1 mM
phosphoramidon
1 mM, 25% inhibition
PMSF
slight inhibition
puromycin
-
-
puromycin
slight inhibition
puromycin
slight inhibition
puromycin
slight inhibition
purpurin
-
is isolated from the natural product library and inhibits adipocyte-derived leucine aminopeptidase and angiogenesis in a zebrafish model. Purpurin inhibits A-LAP activity in a non-competitive manner showing a strong selectivity toward A-LAP versus another member of M1 family of zinc metallopeptidase, aminopeptidase N (APN). Purpurin can be developed as an anti-angiogenic agent. Purpurin also causes a partial inhibition of extension of the intersegmental vessels (ISVs) from the dorsal aorta
purpurin
-
is isolated from the natural product library and inhibits the proliferation of HUVECs in a dose-dependent manner with an IC50 value of 0.03 mM. The proliferation of other types of cells such as HeLa (cervical carcinoma) and C8161 (melanoma) is not significantly inhibited by purpurin at the same concentration range used for HUVEC. Purpurin selectively inhibits the proliferation of endothelial cells over the other types of mammalian cells. Purpurin does not significantly affect the viability of HUVEC up to 0.02 mM treatment. A marginal decrease in the HUVEC viability is observed between 0.04-0.06 mM, and the significant cytotoxicity is observed at over 0.08 mM treatment with purpurin. The treatment of purpurin does not significantly affect the expression level of A-LAP in HUVEC
SH-
-
-
Zn2+
activates at 0.1-1.0 mM, inhibitory at 1.0-10 mM
Zn2+
-
26% inhibition at 2 mM, 86% at 10 mM, and 95% at 20 mM
Zn2+
slight inhibition at 1 mM
Zn2+
-
partially inactivated at 1 mM
Zn2+
inhibitory at 10 mM, slightly activating at 1 mM
Zn2+
-
at concentration of 1 mM, the enzyme is strongly inactivated by Zn2+ (35.1% residual activity)
Zn2+
1-10 mM Zn2+ plus Mg2+ reduce the enzymatic activity
Zn2+
complete inhibition at 1.0 mM
Zn2+
0.5 mM, around 50% inhibition
Zn2+
-
1 mM, 56% inhibition
Zn2+
0.1 mM, 93% loss of activity
additional information
-
inhibition of enzymes from strains NRRL 6271 and NRRL 1988 by different metal ions at different concentrations, overview
-
additional information
-
no inhibition by bestatin, EDTA, EGTA, PMSF, and DFP
-
additional information
leupeptin, aprotinin, and pepstatin virtually have no effect on the enzyme activity
-
additional information
-
leupeptin, aprotinin, and pepstatin virtually have no effect on the enzyme activity
-
additional information
-
no inhibition by epibestatin, and by E64, chymostatin, leupeptin, and antipain
-
additional information
-
no inhibition by epibestatin, and by E64, chymostatin, leupeptin, and antipain
-
additional information
-
the enzyme is puromycin-insensitive
-
additional information
-
methanol extracts of Ceropegia rupicola, Kniphofia sumarae, and Plectranthus cf. barbatus, and the aqueous extract of Pavetta longiflora show no inhibitory effect towards aminopeptidas N
-
additional information
method development for usage of human leucine aminopeptidase to evaluate the suppression of enzyme activity by an LAP3 inhibitor
-
additional information
-
method development for usage of human leucine aminopeptidase to evaluate the suppression of enzyme activity by an LAP3 inhibitor
-
additional information
no inhibition by DTT and GSH, inhibition mechanisms
-
additional information
no inhibition by DTT, inhibition mechanisms
-
additional information
no inhibition by DTT, inhibition mechanisms
-
additional information
the structures of LAP-A in its apo and holo forms and in complex with inhibitors are practically identical. The apo LmLAP-A structure shows a completely ordered active site independent of metal or ligand binding
-
additional information
-
vascular endothelial growth factor-stimulated G1/S transition in endothelial cells inhibits the enzyme activity and/or expression leading to an arrest in G1 phase
-
additional information
de novo drug design, and structure-based virtual screening of the ZINC database and molecular docking study
-
additional information
-
de novo drug design, and structure-based virtual screening of the ZINC database and molecular docking study
-
additional information
-
not inhibited by diisopropyl fluorophosphate, phenylmethylsulfonyl fluoride, 3,4-dichloroisocoumarin, tosyl-lysine chloromethylketone, N-methylmaleimide, phosphoramidon
-
additional information
insensitive to chamostatin, E-64, leupeptin, pepstatin, aprotinin and puromycin
-
additional information
-
insensitive to chamostatin, E-64, leupeptin, pepstatin, aprotinin and puromycin
-
additional information
no inhibition by EDTA
-
additional information
-
no inhibition by EDTA
-
additional information
-
no or poor inhibition by 2 mM of iodoacetic acid, EDTA, EGTA, and citrate
-
additional information
-
computational inhibitor design
-
additional information
the structures of LAP-A in its apo and holo forms and in complex with inhibitors are practically identical
-
additional information
the structures of LAP-A in its apo and holo forms and in complex with inhibitors are practically identical. The apo TcLAP-A structure shows a completely ordered active site independent of metal or ligand binding
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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0.00887
4-[(E)-2-[4-cyano-5-(dicyanomethylidene)-2,2-dimethyl-2,5-dihydrofuran-3-yl]ethenyl]phenyl L-leucinate
-
pH 7.4, 25°C
0.0529
Ala-4-methylcoumaryl-7-amide
-
0.96 - 8.78
Ala-4-nitroanilide
3.7
Arg-4-nitroanilide
pH 8.5, 37°C
4.5
Arg-Gly
-
His-tagged recombinant enzyme, 37°C
3.3
Arg-Gly-Asp
-
His-tagged recombinant enzyme, 37°C
9.6
Arg-Gly-Phe
-
His-tagged recombinant enzyme, 37°C
1.4
Arg-Leu
-
His-tagged recombinant enzyme, 37°C
1.8
Asp-Gln
pH 8.5, 37°C, wild-type enzyme
0.6
Asp-His
pH 8.5, 37°C, wild-type enzyme
3
Asp-Ile-Gly-Gly
pH 8.5, 37°C, wild-type enzyme
0.4
Asp-Leu
pH 8.5, 37°C, wild-type enzyme
0.5
Asp-Leu-Gly
pH 8.5, 37°C, wild-type enzyme
6
Asp-Leu-Lys
pH 8.5, 37°C, wild-type enzyme
0.3
Asp-Phe
pH 8.5, 37°C, wild-type enzyme
0.3
Asp-Tyr
pH 8.5, 37°C, wild-type enzyme
0.9
Glu-Leu
pH 8.5, 37°C, wild-type enzyme
11.2
Gly-Gly
-
His-tagged recombinant enzyme, 37°C
8.6
Gly-Leu
-
His-tagged recombinant enzyme, 37°C
1
Gly-Phe
-
Zn2+-Zn2+-enzyme form
0.39
glycine-4-methylcoumaryl-7-amide
-
pH 7.0, 37°C
0.82
hArg-7-amido-4-methylcoumarin
-
pH 9, 37°C
0.185 - 24.7
L-Ala-4-nitroanilide
0.392 - 0.442
L-Ala-7-amido-4-methylcoumarin
0.169
L-alanine-4-methylcoumarin-7-amide
-
pH 8.0, 37°C, recombinant GST-tagged enzyme
0.054 - 1.16
L-alanine-4-methylcoumaryl-7-amide
0.36
L-alanyl-4-nitroanilide
-
pH 9.0, 37°C
0.79
L-Arg-7-amido-4-methylcoumarin
-
pH 9, 37°C
0.426
L-arginine-4-methylcoumarin-7-amide
-
pH 8.0, 37°C, recombinant GST-tagged enzyme
0.0084 - 0.19
L-arginine-4-methylcoumaryl-7-amide
0.0414
L-arginyl-7-amido-4-methylcoumarin
pH 8.0, 37°C, recombinant enzyme
0.043 - 0.062
L-Cys-7-amido-4-methylcoumarin
0.261
L-Ile-4-nitroanilide
pH 8, 20°C
0.054 - 0.077
L-Ile-7-amido-4-methylcoumarin
0.04456
L-Leu 7-amido-4-methylcoumarin
pH 7.2, 28°C, recombinant enzyme
8.5
L-Leu methyl ester
-
-
0.25
L-Leu-2-naphthylamide
0.035 - 12.7
L-Leu-4-nitroanilide
0.012 - 1.38
L-Leu-7-amido-4-methylcoumarin
1.56
L-Leu-benzyl ester
-
-
17.5 - 342
L-Leu-hydrazide
0.14
L-Leu-phenylazophenylamide
-
-
0.107
L-leucine-4-methylcoumarin-7-amide
-
pH 8.0, 37°C, recombinant GST-tagged enzyme
0.015 - 0.35
L-leucine-4-methylcoumaryl-7-amide
0.14 - 3
L-leucine-4-nitroanilide
0.5
L-leucine-p-naphthylamide
-
-
0.084
L-leucyl-2-naphthylamide
-
pH 7.0, temperature not specified in the publication
0.00925
L-leucyl-4-nitroanilide
-
pH 9.0, 37°C
0.00155 - 0.0135
L-leucyl-7-amido-4-methylcoumarin
14.2
L-leucylamide
-
native enzyme, pH 8.0, 25°C
0.094 - 8.9
L-Lys-4-nitroanilide
0.3641 - 0.81
L-lysine-4-methylcoumaryl-7-amide
0.099
L-Lysyl-4-nitroanilide
-
pH 9.0, 37°C
0.053 - 0.0597
L-Met-4-nitroanilide
0.105 - 0.154
L-Met-7-amido-4-methylcoumarin
0.12
L-methionine-4-methyl-coumaryl-7-amide
-
0.1092
L-methionine-4-methylcoumaryl-7-amide
pH 8.5, 37°C
0.083
L-methionyl-4-nitroanilide
-
pH 9.0, 37°C
0.0038
L-methionyl-7-amido-4-methylcoumarin
pH 8.0, 37°C, recombinant enzyme
0.0842 - 0.091
L-Phe-4-nitroanilide
0.3
L-phenylalanine-4-methyl-coumaryl-7-amide
-
0.01
L-phenylalanine-4-methylcoumarin-7-amide
-
pH 8.0, 37°C, recombinant GST-tagged enzyme
0.108 - 0.245
L-phenylalanine-4-methylcoumaryl-7-amide
0.782
L-phenylalanine-4-nitroanilide
-
pH 8.5, 50°C
0.216 - 13.1
L-Pro-4-nitroanilide
0.124
L-proline-4-methylcoumarin-7-amide
-
pH 8.0, 37°C, recombinant GST-tagged enzyme
0.025 - 0.05
L-proline-4-methylcoumaryl-7-amide
5.2
L-Ser-Gly
pH 7.4, 25°C
0.198 - 0.204
L-Thr-4-nitroanilide
0.072 - 0.118
L-Trp-7-amido-4-methylcoumarin
0.055
L-tyrosine-4-methylcoumaryl-7-amide
-
pH 7.0, 37°C
0.372
L-Val-4-nitroanilide
pH 8, 20°C
0.019
L-valine-4-methylcoumaryl-7-amide
-
pH 7.0, 37°C
0.01212
Leu-4-methylcoumaryl-7-amide
-
0.22 - 8.8
Leu-4-nitroanilide
35.8
Leu-7-amino-4-trilfluoromethylcoumarin
-
-
0.17 - 0.97
Leu-p-nitroanilide
0.06
Leu-Phe
-
Zn2+-Zn2+-enzyme form
1
Leu-Tyr
pH 8.5, 37°C, wild-type enzyme
0.01 - 1.25
leucine-7-amido-4-methylcoumarin
0.59 - 3.6
Lys-4-nitroanilide
0.17 - 4.4
Met-4-nitroanilide
0.065
N-(6-methoxy-2-methylpyridin-3-yl),(S)-2-amino-4-methylpentanamide
-
pH not specified in the publication, temperature not specified in the publication
0.065
N-(6-methoxypyridin-3-yl)-(S)-2-amino-4-methylpentanamide
-
pH 8.0, 31°C
0.00792
Phe-4-methylcoumaryl-7-amide
-
1.33
Phg-7-amido-4-methylcoumarin
-
pH 9, 37°C
0.2349
Pro-4-methylcoumaryl-7-amide
-
0.194
Pro-4-nitroanilide
-
pH 7.0, 37°C
additional information
additional information
-
0.96
Ala-4-nitroanilide
-
pH 7.5, 30°C
8.78
Ala-4-nitroanilide
-
pH 7.0, 37°C
0.42
Cys-Gly
pH 6.9, 25°C
0.57
Cys-Gly
pH 7.4, 25°C
0.59
Cys-Gly
pH 8.3, 25°C
0.185
L-Ala-4-nitroanilide
pH 8, 20°C
0.202
L-Ala-4-nitroanilide
pH 8, 20°C
24.7
L-Ala-4-nitroanilide
pH 7.5, 80°C
0.392
L-Ala-7-amido-4-methylcoumarin
pH 8.0, 37°C, recombinant His-tagged enzyme
0.408
L-Ala-7-amido-4-methylcoumarin
pH 8.0, 37°C, recombinant His-tagged enzyme
0.442
L-Ala-7-amido-4-methylcoumarin
pH 8.0, 37°C, recombinant His-tagged enzyme
0.054
L-alanine-4-methylcoumaryl-7-amide
-
pH 7.0, 37°C
0.095
L-alanine-4-methylcoumaryl-7-amide
pH 8.0, 37°C, recombinant GST-tagged enzyme
0.2396
L-alanine-4-methylcoumaryl-7-amide
pH 8.5, 37°C
1.16
L-alanine-4-methylcoumaryl-7-amide
-
0.0084
L-arginine-4-methylcoumaryl-7-amide
-
pH 7.0, 37°C
0.189
L-arginine-4-methylcoumaryl-7-amide
pH 8.0, 37°C, recombinant GST-tagged enzyme
0.19
L-arginine-4-methylcoumaryl-7-amide
-
0.043
L-Cys-7-amido-4-methylcoumarin
pH 8.0, 37°C, recombinant His-tagged enzyme
0.044
L-Cys-7-amido-4-methylcoumarin
pH 8.0, 37°C, recombinant His-tagged enzyme
0.062
L-Cys-7-amido-4-methylcoumarin
pH 8.0, 37°C, recombinant His-tagged enzyme
0.054
L-Ile-7-amido-4-methylcoumarin
pH 8.0, 37°C, recombinant His-tagged enzyme
0.06
L-Ile-7-amido-4-methylcoumarin
pH 8.0, 37°C, recombinant His-tagged enzyme
0.077
L-Ile-7-amido-4-methylcoumarin
pH 8.0, 37°C, recombinant His-tagged enzyme
0.25
L-Leu-2-naphthylamide
-
-
0.25
L-Leu-2-naphthylamide
-
similar value
0.035
L-Leu-4-nitroanilide
pH 8, 20°C
0.036
L-Leu-4-nitroanilide
pH 8, 20°C
0.5
L-Leu-4-nitroanilide
-
-
1.1
L-Leu-4-nitroanilide
-
-
1.2
L-Leu-4-nitroanilide
pH 7.5, 50°C, enzyme activated by heating at 70°C
1.8
L-Leu-4-nitroanilide
pH 7.5, 50°C
6
L-Leu-4-nitroanilide
-
Zn2+-Zn2+-enzyme form
6.3
L-Leu-4-nitroanilide
pH 7.5, 35°C
12.7
L-Leu-4-nitroanilide
pH 7.5, 80°C
0.012
L-Leu-7-amido-4-methylcoumarin
native enzyme, pH 7.5, 37°C
0.0182
L-Leu-7-amido-4-methylcoumarin
pH 7.5, 37°, Vmax: 10.7 microM/min
0.167
L-Leu-7-amido-4-methylcoumarin
pH 8.0, 37°C, recombinant His-tagged enzyme
0.1859
L-Leu-7-amido-4-methylcoumarin
recombinant enzyme, pH 7.5, 37°C
0.189
L-Leu-7-amido-4-methylcoumarin
pH 8.0, 37°C, recombinant His-tagged enzyme
0.229
L-Leu-7-amido-4-methylcoumarin
pH 8.0, 37°C, recombinant His-tagged enzyme
1.38
L-Leu-7-amido-4-methylcoumarin
-
pH 9, 37°C
1.8
L-Leu-Gly
-
wild-type, pH 9.2, 37°C
2
L-Leu-Gly
-
mutant E429D, pH 9.2, 37°C
5.1
L-Leu-Gly
-
mutant R431K, pH 9.2, 37°C
7.2
L-Leu-Gly
-
similar value
7.2
L-Leu-Gly
-
similar value
17.5
L-Leu-hydrazide
-
-
0.51
L-Leu-L-Val
-
-
0.51
L-Leu-L-Val
-
similar value
0.015
L-leucine-4-methylcoumaryl-7-amide
-
pH 7.0, 37°C
0.102
L-leucine-4-methylcoumaryl-7-amide
pH 8.5, 37°C
0.102
L-leucine-4-methylcoumaryl-7-amide
pH 8.0, 37°C, recombinant GST-tagged enzyme
0.109
L-leucine-4-methylcoumaryl-7-amide
pH 8.0, 37°C, native enzyme
0.19
L-leucine-4-methylcoumaryl-7-amide
-
0.35
L-leucine-4-methylcoumaryl-7-amide
-
pH 8.0, 37°C, recombinant enzyme in presence of Zn2+ and Mg2+, best ion combination at metal binding sites 1 and 2
0.14
L-leucine-4-nitroanilide
-
-
0.244
L-leucine-4-nitroanilide
-
pH 8.5, 50°C
3
L-leucine-4-nitroanilide
-
pH 8.0, 31°C
3
L-leucine-4-nitroanilide
-
pH not specified in the publication, temperature not specified in the publication
0.00155
L-leucyl-7-amido-4-methylcoumarin
-
in 25 mM sodium phosphate buffer (pH 7.0) containing 1 mM dithiothreitol and 0.02% NaN3, at 37°C
0.0135
L-leucyl-7-amido-4-methylcoumarin
pH 8.0, 37°C, recombinant enzyme
0.094
L-Lys-4-nitroanilide
pH 8, 20°C
0.103
L-Lys-4-nitroanilide
pH 8, 20°C
5
L-Lys-4-nitroanilide
pH 7.5, 35°C
8.9
L-Lys-4-nitroanilide
pH 7.5, 80°C
0.3641
L-lysine-4-methylcoumaryl-7-amide
pH 8.5, 37°C
0.81
L-lysine-4-methylcoumaryl-7-amide
-
0.053
L-Met-4-nitroanilide
pH 8, 20°C
0.0597
L-Met-4-nitroanilide
pH 8, 20°C
0.105
L-Met-7-amido-4-methylcoumarin
pH 8.0, 37°C, recombinant His-tagged enzyme
0.137
L-Met-7-amido-4-methylcoumarin
pH 8.0, 37°C, recombinant His-tagged enzyme
0.154
L-Met-7-amido-4-methylcoumarin
pH 8.0, 37°C, recombinant His-tagged enzyme
1.3
L-Met-Gly
pH 8.3, 25°C
2.8
L-Met-Gly
pH 6.9, 25°C
0.0842
L-Phe-4-nitroanilide
pH 8, 20°C
0.091
L-Phe-4-nitroanilide
pH 8, 20°C
0.108
L-phenylalanine-4-methylcoumaryl-7-amide
pH 8.0, 37°C, recombinant GST-tagged enzyme
0.245
L-phenylalanine-4-methylcoumaryl-7-amide
pH 8.5, 37°C
0.216
L-Pro-4-nitroanilide
pH 8, 20°C
0.239
L-Pro-4-nitroanilide
pH 8, 20°C
13.1
L-Pro-4-nitroanilide
pH 7.5, 80°C
0.025
L-proline-4-methylcoumaryl-7-amide
-
pH 7.0, 37°C
0.05
L-proline-4-methylcoumaryl-7-amide
pH 8.0, 37°C, recombinant GST-tagged enzyme
0.198
L-Thr-4-nitroanilide
pH 8, 20°C
0.204
L-Thr-4-nitroanilide
pH 8, 20°C
0.072
L-Trp-7-amido-4-methylcoumarin
pH 8.0, 37°C, recombinant His-tagged enzyme
0.104
L-Trp-7-amido-4-methylcoumarin
pH 8.0, 37°C, recombinant His-tagged enzyme
0.118
L-Trp-7-amido-4-methylcoumarin
pH 8.0, 37°C, recombinant His-tagged enzyme
0.22
Leu-4-nitroanilide
-
pH 7.5, 30°C
0.248
Leu-4-nitroanilide
-
pH 7.0, 37°C
0.97
Leu-4-nitroanilide
pH 8.5, 50°C, recombinant enzyme
1.28
Leu-4-nitroanilide
-
-
2
Leu-4-nitroanilide
-
Mg2+-Zn2+-enzyme form
4.1
Leu-4-nitroanilide
-
Zn2+-Zn2+-enzyme form
4.5
Leu-4-nitroanilide
pH 8.5, 37°C
8.8
Leu-4-nitroanilide
-
pH 8.0, 37°C
1.5
Leu-Gly
-
37°C
2.2
Leu-Gly
-
free recombinant enzyme, 37°C
3.2
Leu-Gly
-
His-tagged recombinant enzyme, 37°C
7.2
Leu-Gly
-
similar value
8.4
Leu-Gly
-
Mg2+-Zn2+-enzyme form
1.9
Leu-Gly-Gly
-
His-tagged recombinant enzyme, 37°C
2.9
Leu-Leu
-
His-tagged recombinant enzyme, 37°C
4
Leu-Leu
pH 8.5, 37°C, wild-type enzyme
0.17
Leu-p-nitroanilide
-
pH 7.0, 37°C
0.22
Leu-p-nitroanilide
-
pH 7.0, 37°C
0.23
Leu-p-nitroanilide
wild type enzyme, in 20 mM Tris-HCl buffer (pH 8.0) containing 1 mM NiCl2
0.52
Leu-p-nitroanilide
mutant enzyme N345Q, in 20 mM Tris-HCl buffer (pH 8.0) containing 1 mM NiCl2
0.97
Leu-p-nitroanilide
mutant enzyme N345L, in 20 mM Tris-HCl buffer (pH 8.0) containing 1 mM NiCl2
4.02
leucinamide
-
-
4.02
leucinamide
-
similar value
4.02
leucinamide
-
similar value
17
leucinamide
-
similar value
0.01
leucine-7-amido-4-methylcoumarin
-
-
1.25
leucine-7-amido-4-methylcoumarin
-
-
0.59
Lys-4-nitroanilide
-
pH 7.5, 30°C
3.6
Lys-4-nitroanilide
pH 8.5, 37°C
0.17
Met-4-nitroanilide
-
pH 7.5, 30°C
4.4
Met-4-nitroanilide
pH 8.5, 37°C
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
metal ion binding kinetics to the recombinant enzyme, metal ion occupying site 1 can influence enzyme substrate kinetics, overview
-
additional information
additional information
-
dynamics of ACTH-(6-9)-PGP peptide hydrolysis with leucine aminopeptidase and carboxypeptidase Y and reaction kinetics, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0002
Ala-4-methylcoumaryl-7-amide
-
761
Asp-Gln
pH 8.5, 37°C, wild-type enzyme
418
Asp-His
pH 8.5, 37°C, wild-type enzyme
26
Asp-Ile-Gly-Gly
pH 8.5, 37°C, wild-type enzyme
666
Asp-Leu
pH 8.5, 37°C, wild-type enzyme
950
Asp-Leu-Gly
pH 8.5, 37°C, wild-type enzyme
13
Asp-Leu-Lys
pH 8.5, 37°C, wild-type enzyme
500
Asp-Phe
pH 8.5, 37°C, wild-type enzyme
500
Asp-Tyr
pH 8.5, 37°C, wild-type enzyme
866
Glu-Leu
pH 8.5, 37°C, wild-type enzyme
0.5
Gly-Phe
-
Zn2+-Zn2+-enzyme form
45.6
glycine-4-methylcoumaryl-7-amide
-
pH 7.0, 37°C
0.1584
hArg-7-amido-4-methylcoumarin
-
pH 9, 37°C
0.078 - 0.12
L-Ala-4-nitroanilide
1.61 - 2.94
L-Ala-7-amido-4-methylcoumarin
0.03
L-alanine-4-methylcoumarin-7-amide
-
pH 8.0, 37°C, recombinant GST-tagged enzyme
0.01 - 38.7
L-alanine-4-methylcoumaryl-7-amide
0.1395
L-Arg-7-amido-4-methylcoumarin
-
pH 9, 37°C
0.041
L-arginine-4-methylcoumarin-7-amide
-
pH 8.0, 37°C, recombinant GST-tagged enzyme
12.1 - 37.79
L-arginine-4-methylcoumaryl-7-amide
0.13 - 17.3
L-arginyl-7-amido-4-methylcoumarin
2.19 - 6
L-Cys-7-amido-4-methylcoumarin
0.01
L-Ile-4-nitroanilide
pH 8, 20°C
0.09 - 0.19
L-Ile-7-amido-4-methylcoumarin
0.0157 - 19
L-Leu-4-nitroanilide
0.057 - 34.84
L-Leu-7-amido-4-methylcoumarin
0.089
L-leucine-4-methylcoumarin-7-amide
-
pH 8.0, 37°C, recombinant GST-tagged enzyme
0.0094 - 198.8
L-leucine-4-methylcoumaryl-7-amide
50.9
L-leucine-4-nitroanilide
-
pH 8.5, 50°C
0.83 - 26.4
L-leucyl-7-amido-4-methylcoumarin
112
L-leucylamide
-
native enzyme, pH 8.0, 25°C
0.0104 - 0.194
L-Lys-4-nitroanilide
0.002
L-lysine-4-methylcoumaryl-7-amide
pH 8.5, 37°C
0.18 - 0.2
L-Met-4-nitroanilide
3.3 - 5.52
L-Met-7-amido-4-methylcoumarin
0.085
L-methionine-4-methylcoumaryl-7-amide
pH 8.5, 37°C
0.33
L-methionyl-7-amido-4-methylcoumarin
pH 8.0, 37°C, recombinant enzyme
0.04 - 0.05
L-Phe-4-nitroanilide
0.0002
L-phenylalanine-4-methylcoumarin-7-amide
-
pH 8.0, 37°C, recombinant GST-tagged enzyme
0.075 - 24.61
L-phenylalanine-4-methylcoumaryl-7-amide
37
L-phenylalanine-4-nitroanilide
-
pH 8.5, 50°C
0.02 - 0.021
L-Pro-4-nitroanilide
0.0016
L-proline-4-methylcoumarin-7-amide
-
pH 8.0, 37°C, recombinant GST-tagged enzyme
1.3 - 2.03
L-proline-4-methylcoumaryl-7-amide
0.01 - 0.02
L-Thr-4-nitroanilide
0.07 - 0.22
L-Trp-7-amido-4-methylcoumarin
13.8
L-tyrosine-4-methylcoumaryl-7-amide
-
pH 7.0, 37°C
0.01
L-Val-4-nitroanilide
pH 8, 20°C
1.5
L-valine-4-methylcoumaryl-7-amide
-
pH 7.0, 37°C
0.039
Leu-4-methylcoumaryl-7-amide
-
0.003 - 0.04
Leu-4-nitroanilide
13960 - 14000
Leu-Gly-Gly
0.17 - 5.92
Leu-p-nitroanilide
270
Leu-Phe
-
Zn2+-Zn2+-enzyme form
351
Leu-Tyr
pH 8.5, 37°C, wild-type enzyme
0.00145
Phe-4-methylcoumaryl-7-amide
-
0.3952
Phg-7-amido-4-methylcoumarin
-
pH 9, 37°C
0.00059
Pro-4-methylcoumaryl-7-amide
-
additional information
L-Met-7-amido-4-methylcoumarin
pH 8.0, 37°C, recombinant His-tagged enzyme
13500
Arg-Gly
-
His-tagged recombinant enzyme, 37°C
13520
Arg-Gly
-
His-tagged recombinant enzyme, 37°C
3780
Arg-Gly-Asp
-
His-tagged recombinant enzyme, 37°C
3781
Arg-Gly-Asp
-
His-tagged recombinant enzyme, 37°C
6070
Arg-Gly-Phe
-
His-tagged recombinant enzyme, 37°C
6073
Arg-Gly-Phe
-
His-tagged recombinant enzyme, 37°C
19380
Arg-Leu
-
His-tagged recombinant enzyme, 37°C
19400
Arg-Leu
-
His-tagged recombinant enzyme, 37°C
2.6
Cys-Gly
pH 6.9, 25°C
56.66
Cys-Gly
pH 6.9, 25°C
118.3
Cys-Gly
pH 8.3, 25°C
10860
Gly-Gly
-
His-tagged recombinant enzyme, 37°C
10900
Gly-Gly
-
His-tagged recombinant enzyme, 37°C
5140
Gly-Leu
-
His-tagged recombinant enzyme, 37°C
5141
Gly-Leu
-
His-tagged recombinant enzyme, 37°C
0.078
L-Ala-4-nitroanilide
pH 7.5, 80°C
0.12
L-Ala-4-nitroanilide
pH 8, 20°C
1.61
L-Ala-7-amido-4-methylcoumarin
pH 8.0, 37°C, recombinant His-tagged enzyme
1.89
L-Ala-7-amido-4-methylcoumarin
pH 8.0, 37°C, recombinant His-tagged enzyme
2.01
L-Ala-7-amido-4-methylcoumarin
pH 8.0, 37°C, recombinant His-tagged enzyme
2.94
L-Ala-7-amido-4-methylcoumarin
pH 8.0, 37°C, recombinant His-tagged enzyme
2.94
L-Ala-7-amido-4-methylcoumarin
pH 8.0, 37°C, recombinant His-tagged enzyme
2.94
L-Ala-7-amido-4-methylcoumarin
pH 8.0, 37°C, recombinant His-tagged enzyme
0.01
L-alanine-4-methylcoumaryl-7-amide
pH 8.5, 37°C
8.2
L-alanine-4-methylcoumaryl-7-amide
pH 8.0, 37°C, recombinant GST-tagged enzyme
38.7
L-alanine-4-methylcoumaryl-7-amide
-
pH 7.0, 37°C
12.1
L-arginine-4-methylcoumaryl-7-amide
-
pH 7.0, 37°C
37.79
L-arginine-4-methylcoumaryl-7-amide
pH 8.0, 37°C, recombinant GST-tagged enzyme
0.13
L-arginyl-7-amido-4-methylcoumarin
pH 8.0, 37°C, recombinant enzyme
17.3
L-arginyl-7-amido-4-methylcoumarin
-
in 25 mM sodium phosphate buffer (pH 7.0) containing 1 mM dithiothreitol and 0.02% NaN3, at 37°C
2.19
L-Cys-7-amido-4-methylcoumarin
pH 8.0, 37°C, recombinant His-tagged enzyme
2.72
L-Cys-7-amido-4-methylcoumarin
pH 8.0, 37°C, recombinant His-tagged enzyme
2.94
L-Cys-7-amido-4-methylcoumarin
pH 8.0, 37°C, recombinant His-tagged enzyme
3 - 6
L-Cys-7-amido-4-methylcoumarin
pH 8.0, 37°C, recombinant His-tagged enzyme
3 - 6
L-Cys-7-amido-4-methylcoumarin
pH 8.0, 37°C, recombinant His-tagged enzyme
3.34
L-Cys-7-amido-4-methylcoumarin
pH 8.0, 37°C, recombinant His-tagged enzyme
0.09
L-Ile-7-amido-4-methylcoumarin
pH 8.0, 37°C, recombinant His-tagged enzyme
0.19
L-Ile-7-amido-4-methylcoumarin
pH 8.0, 37°C, recombinant His-tagged enzyme
0.19
L-Ile-7-amido-4-methylcoumarin
pH 8.0, 37°C, recombinant His-tagged enzyme
0.0157
L-Leu-4-nitroanilide
pH 7.5, 35°C
0.23
L-Leu-4-nitroanilide
pH 8, 20°C
0.27
L-Leu-4-nitroanilide
pH 8, 20°C
0.285
L-Leu-4-nitroanilide
pH 7.5, 80°C
0.7
L-Leu-4-nitroanilide
-
Zn2+-Zn2+-enzyme form
5.4
L-Leu-4-nitroanilide
pH 7.5, 50°C
19
L-Leu-4-nitroanilide
pH 7.5, 50°C, enzyme activated by heating at 70°C
0.057 - 0.65
L-Leu-7-amido-4-methylcoumarin
pH 8.0, 37°C, recombinant His-tagged enzyme
0.1204
L-Leu-7-amido-4-methylcoumarin
-
pH 9, 37°C
0.41
L-Leu-7-amido-4-methylcoumarin
pH 8.0, 37°C, recombinant His-tagged enzyme
0.52
L-Leu-7-amido-4-methylcoumarin
pH 8.0, 37°C, recombinant His-tagged enzyme
12.47
L-Leu-7-amido-4-methylcoumarin
native enzyme, pH 7.5, 37°C
34.84
L-Leu-7-amido-4-methylcoumarin
recombinant enzyme, pH 7.5, 37°C
30
L-Leu-Gly
-
mutant R431K, pH 9.2, 37°C
108
L-Leu-Gly
-
mutant E429D, pH 9.2, 37°C
120
L-Leu-Gly
-
wild-type, pH 9.2, 37°C
0.0094
L-leucine-4-methylcoumaryl-7-amide
-
pH 8.0, 37°C, recombinant enzyme in presence of Zn2+ and Mg2+, best ion combination at metal binding sites 1 and 2
0.107
L-leucine-4-methylcoumaryl-7-amide
pH 8.5, 37°C
34.6
L-leucine-4-methylcoumaryl-7-amide
-
pH 7.0, 37°C
198.8
L-leucine-4-methylcoumaryl-7-amide
pH 8.0, 37°C, recombinant GST-tagged enzyme
0.83
L-leucyl-7-amido-4-methylcoumarin
pH 8.0, 37°C, recombinant enzyme
26.4
L-leucyl-7-amido-4-methylcoumarin
-
in 25 mM sodium phosphate buffer (pH 7.0) containing 1 mM dithiothreitol and 0.02% NaN3, at 37°C
0.0104
L-Lys-4-nitroanilide
pH 7.5, 35°C
0.05
L-Lys-4-nitroanilide
pH 8, 20°C
0.07
L-Lys-4-nitroanilide
pH 8, 20°C
0.194
L-Lys-4-nitroanilide
pH 7.5, 80°C
0.18
L-Met-4-nitroanilide
pH 8, 20°C
0.2
L-Met-4-nitroanilide
pH 8, 20°C
3.3
L-Met-7-amido-4-methylcoumarin
pH 8.0, 37°C, recombinant His-tagged enzyme
3.3
L-Met-7-amido-4-methylcoumarin
pH 8.0, 37°C, recombinant His-tagged enzyme
4.99
L-Met-7-amido-4-methylcoumarin
pH 8.0, 37°C, recombinant His-tagged enzyme
5.08
L-Met-7-amido-4-methylcoumarin
pH 8.0, 37°C, recombinant His-tagged enzyme
5.52
L-Met-7-amido-4-methylcoumarin
pH 8.0, 37°C, recombinant His-tagged enzyme
0.04
L-Phe-4-nitroanilide
pH 8, 20°C
0.05
L-Phe-4-nitroanilide
pH 8, 20°C
0.075
L-phenylalanine-4-methylcoumaryl-7-amide
pH 8.5, 37°C
24.61
L-phenylalanine-4-methylcoumaryl-7-amide
pH 8.0, 37°C, recombinant GST-tagged enzyme
0.02
L-Pro-4-nitroanilide
pH 8, 20°C
0.021
L-Pro-4-nitroanilide
pH 7.5, 80°C
1.3
L-proline-4-methylcoumaryl-7-amide
-
pH 7.0, 37°C
2.03
L-proline-4-methylcoumaryl-7-amide
pH 8.0, 37°C, recombinant GST-tagged enzyme
0.01
L-Thr-4-nitroanilide
pH 8, 20°C
0.02
L-Thr-4-nitroanilide
pH 8, 20°C
0.07
L-Trp-7-amido-4-methylcoumarin
pH 8.0, 37°C, recombinant His-tagged enzyme
0.21
L-Trp-7-amido-4-methylcoumarin
pH 8.0, 37°C, recombinant His-tagged enzyme
0.22
L-Trp-7-amido-4-methylcoumarin
pH 8.0, 37°C, recombinant His-tagged enzyme
0.003
Leu-4-nitroanilide
-
Zn2+-Zn2+-enzyme form
0.04
Leu-4-nitroanilide
-
Mg2+-Zn2+-enzyme form
191.7
Leu-Gly
pH 6.9, 25°C
1670
Leu-Gly
-
Mg2+-Zn2+-enzyme form
14100
Leu-Gly
-
His-tagged recombinant enzyme, 37°C
14400
Leu-Gly
-
free recombinant enzyme, 37°C
14440
Leu-Gly
-
free recombinant enzyme, 37°C
13960
Leu-Gly-Gly
-
His-tagged recombinant enzyme, 37°C
14000
Leu-Gly-Gly
-
His-tagged recombinant enzyme, 37°C
918
Leu-Leu
pH 8.5, 37°C, wild-type enzyme
34490
Leu-Leu
-
His-tagged recombinant enzyme, 37°C
34500
Leu-Leu
-
His-tagged recombinant enzyme, 37°C
0.17
Leu-p-nitroanilide
mutant enzyme N345L, in 20 mM Tris-HCl buffer (pH 8.0) containing 1 mM NiCl2
0.63
Leu-p-nitroanilide
mutant enzyme N345Q, in 20 mM Tris-HCl buffer (pH 8.0) containing 1 mM NiCl2
5.92
Leu-p-nitroanilide
wild type enzyme, in 20 mM Tris-HCl buffer (pH 8.0) containing 1 mM NiCl2
135.8
Met-Gly
pH 6.9, 25°C
486.3
Met-Gly
pH 7.4, 25°C
988.3
Met-Gly
pH 8.3, 25°C
17
Ser-Gly
pH 7.4, 25°C
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0.18
1,10-phenanthroline
Morimus funereus
-
-
1
2-amino-1,4-dihydro-2-isoquinolin-3-one
Bos taurus
-
-
0.12
3-amino-2-tetralone
Bos taurus
-
-
0.1
4-amino-3-(L-arginylamino)benzoic acid
Homo sapiens
pH and temperature not specified in the publication
0.0032 - 0.1
4-amino-3-(L-tyrosylamino)benzoic acid
0.011 - 0.013
benzyl N-(3-amino-4-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-tryptophanate
0.1
benzyl N-(3-amino-4-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-valinate
Homo sapiens
pH and temperature not specified in the publication
0.0239
benzyl N-(4-amino-3-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-tryptophanate
Homo sapiens
pH and temperature not specified in the publication
0.0089 - 0.021
benzyl N-[3-amino-4-(L-leucylamino)benzoyl]-L-tryptophanate
0.000709 - 0.0025
benzyl N-[3-amino-4-(L-norleucylamino)benzoyl]-L-tryptophanate
0.0062 - 0.1
benzyl N-[3-amino-4-(L-norleucylamino)benzoyl]-L-valinate
0.07
benzyl N-[3-amino-4-([(2S)-2-amino-4-[4-(benzyloxy)phenyl]butanoyl]amino)benzoyl]-L-tryptophanate
Homo sapiens
pH and temperature not specified in the publication
0.0011 - 0.02
benzyl N-[3-amino-4-[(O-benzyl-L-tyrosyl)amino]benzoyl]-L-tryptophanate
0.1
benzyl N-[4-amino-3-(D-norleucylamino)benzoyl]-L-valinate
Homo sapiens
pH and temperature not specified in the publication
0.00098 - 0.0016
benzyl N-[4-amino-3-(L-norleucylamino)benzoyl]-L-tryptophanate
0.0098 - 0.04
benzyl N-[4-amino-3-(L-tyrosylamino)benzoyl]-L-tryptophanate
0.05
benzyl N-[4-amino-3-(L-tyrosylamino)benzoyl]-L-valinate
Homo sapiens
pH and temperature not specified in the publication
0.1
benzyl N-[4-amino-3-[(O-benzyl-L-tyrosyl)amino]benzoyl]-L-tryptophanate
Homo sapiens
pH and temperature not specified in the publication
0.0000005 - 0.025
bestatin
0.0205
bestatin methyl ester
Plasmodium falciparum
inhibitory activity against recombinant enzyme
0.47
cysteine
Morimus funereus
-
-
0.0025
methyl 3-amino-4-(L-arginylamino)benzoate
Homo sapiens
pH and temperature not specified in the publication
0.1
methyl 3-amino-4-(L-leucylamino)benzoate
Homo sapiens
pH and temperature not specified in the publication
0.0011
methyl 3-amino-4-(L-norleucylamino)benzoate
Homo sapiens
pH and temperature not specified in the publication
0.058
methyl 3-amino-4-(L-tyrosylamino)benzoate
Homo sapiens
pH and temperature not specified in the publication
0.058 - 0.1
methyl 3-amino-4-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoate
0.0037
methyl 4-amino-3-(L-arginylamino)benzoate
Homo sapiens
pH and temperature not specified in the publication
0.0098 - 0.1
methyl 4-amino-3-(L-norleucylamino)benzoate
0.1
methyl 4-amino-3-(L-tyrosylamino)benzoate
Homo sapiens
pH and temperature not specified in the publication
0.1
methyl 4-amino-3-[[(2S)-2-amino-4-(4-hydroxyphenyl)butanoyl]amino]benzoate
Homo sapiens
pH and temperature not specified in the publication
0.1
methyl N-(3,4-diaminobenzoyl)-L-tyrosinate
Homo sapiens
pH and temperature not specified in the publication
0.0055 - 0.0094
methyl N-(3-amino-4-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-tyrosinate
0.0077 - 0.1
methyl N-(4-amino-3-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-tyrosinate
0.0014 - 0.0026
methyl N-[3-amino-4-(L-arginylamino)benzoyl]-L-tyrosinate
0.000755 - 0.1
methyl N-[3-amino-4-(L-norleucylamino)benzoyl]-L-tyrosinate
0.015 - 0.016
methyl N-[3-amino-4-(L-tyrosylamino)benzoyl]-L-tyrosinate
0.016
methyl N-[3-amino-4-[(O-benzyl-L-tyrosyl)amino]benzoyl]-L-tyrosinate
Homo sapiens
pH and temperature not specified in the publication
0.0064 - 0.1
methyl N-[4-amino-3-(D-norleucylamino)benzoyl]-D-tyrosinate
0.000518 - 0.0096
methyl N-[4-amino-3-(L-arginylamino)benzoyl]-D-tyrosinate
0.039 - 0.1
methyl N-[4-amino-3-(L-tyrosylamino)benzoyl]-L-threoninate
0.033 - 0.11
methyl N-[4-amino-3-(L-tyrosylamino)benzoyl]-L-tyrosinate
0.035
methyl N2-(3,4-diaminobenzoyl)-L-argininate
Homo sapiens
pH and temperature not specified in the publication
0.1
methyl N2-(3,4-diaminobenzoyl)-L-lysinate
Homo sapiens
pH and temperature not specified in the publication
0.011 - 0.012
methyl N2-(3-amino-4-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-argininate
0.0048 - 0.1
methyl N2-(4-amino-3-[[(2S)-2-amino-4-(4-hydroxyphenyl)butanoyl]amino]benzoyl)-L-lysinate
0.002 - 0.0249
methyl N2-(4-amino-3-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-lysinate
0.011
methyl N2-[3-amino-4-(L-arginylamino)benzoyl]-L-lysinate
Homo sapiens
pH and temperature not specified in the publication
0.03
methyl N2-[3-amino-4-(L-norleucylamino)benzoyl]-L-lysinate
Homo sapiens
pH and temperature not specified in the publication
0.1
methyl N2-[3-amino-4-(L-tyrosylamino)benzoyl]-L-lysinate
Homo sapiens
pH and temperature not specified in the publication
0.017 - 0.042
methyl N2-[4-amino-3-(L-arginylamino)benzoyl]-L-lysinate
0.052
methyl N2-[4-amino-3-(L-leucylamino)benzoyl]-L-lysinate
Homo sapiens
pH and temperature not specified in the publication
0.0025 - 0.0107
methyl N2-[4-amino-3-(L-norleucylamino)benzoyl]-D-argininate
0.0083 - 0.018
methyl N2-[4-amino-3-(L-norleucylamino)benzoyl]-L-lysinate
0.013 - 0.1
methyl N2-[4-amino-3-([(2S)-2-amino-4-[4-(benzyloxy)phenyl]butanoyl]amino)benzoyl]-L-lysinate
0.0019 - 0.1
N-(3,4-diaminobenzoyl)-L-tryptophan
0.008 - 0.0094
N-(3-amino-4-[[(2S)-2-amino-4-(4-hydroxyphenyl)butanoyl]amino]benzoyl)-L-tryptophan
0.1
N-(3-amino-4-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-valine
Homo sapiens
pH and temperature not specified in the publication
0.038 - 0.1
N-(4-amino-3-[[(2R)-2-amino-4-(4-hydroxyphenyl)butanoyl]amino]benzoyl)-L-tryptophan
0.0011 - 0.0038
N-[3-amino-4-(L-arginylamino)benzoyl]-L-tryptophan
0.000237 - 0.0028
N-[3-amino-4-(L-norleucylamino)benzoyl]-L-tryptophan
0.038
N-[3-amino-4-(L-norleucylamino)benzoyl]-L-valine
Homo sapiens
pH and temperature not specified in the publication
0.0048 - 0.019
N-[3-amino-4-(L-tyrosylamino)benzoyl]-L-tryptophan
0.1
N-[4-amino-3-(D-norleucylamino)benzoyl]-L-valine
Homo sapiens
pH and temperature not specified in the publication
0.000589 - 0.0012
N-[4-amino-3-(L-arginylamino)benzoyl]-L-tryptophan
0.005
N-[4-amino-3-(L-arginylamino)benzoyl]-L-valine
Homo sapiens
pH and temperature not specified in the publication
0.0036 - 0.0038
N-[4-amino-3-(L-norleucylamino)benzoyl]-L-tryptophan
0.012 - 0.1
N-[4-amino-3-(L-tyrosylamino)benzoyl]-L-tryptophan
0.1
N-[4-amino-3-(L-tyrosylamino)benzoyl]-L-valine
Homo sapiens
pH and temperature not specified in the publication
0.0021 - 0.0068
N2-[4-amino-3-(L-leucylamino)benzoyl]-L-lysine
0.0026
N2-[4-amino-3-(L-phenylalanylamino)benzoyl]-L-lysine
Homo sapiens
pH and temperature not specified in the publication
0.0045
N2-[4-amino-3-(L-tyrosylamino)benzoyl]-L-lysine
Homo sapiens
pH and temperature not specified in the publication
0.008
nitrobestatin
Plasmodium falciparum
inhibitory activity against recombinant enzyme
0.02
purpurin
Danio rerio
-
pH 7.4, 37°C
0.0032
4-amino-3-(L-tyrosylamino)benzoic acid
Homo sapiens
pH and temperature not specified in the publication
0.1
4-amino-3-(L-tyrosylamino)benzoic acid
Homo sapiens
pH and temperature not specified in the publication
0.011
benzyl N-(3-amino-4-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-tryptophanate
Homo sapiens
pH and temperature not specified in the publication
0.013
benzyl N-(3-amino-4-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-tryptophanate
Homo sapiens
pH and temperature not specified in the publication
0.0089
benzyl N-[3-amino-4-(L-leucylamino)benzoyl]-L-tryptophanate
Homo sapiens
pH and temperature not specified in the publication
0.021
benzyl N-[3-amino-4-(L-leucylamino)benzoyl]-L-tryptophanate
Homo sapiens
pH and temperature not specified in the publication
0.000709
benzyl N-[3-amino-4-(L-norleucylamino)benzoyl]-L-tryptophanate
Homo sapiens
pH and temperature not specified in the publication
0.0025
benzyl N-[3-amino-4-(L-norleucylamino)benzoyl]-L-tryptophanate
Homo sapiens
pH and temperature not specified in the publication
0.0062
benzyl N-[3-amino-4-(L-norleucylamino)benzoyl]-L-valinate
Homo sapiens
pH and temperature not specified in the publication
0.1
benzyl N-[3-amino-4-(L-norleucylamino)benzoyl]-L-valinate
Homo sapiens
pH and temperature not specified in the publication
0.0011
benzyl N-[3-amino-4-[(O-benzyl-L-tyrosyl)amino]benzoyl]-L-tryptophanate
Homo sapiens
pH and temperature not specified in the publication
0.02
benzyl N-[3-amino-4-[(O-benzyl-L-tyrosyl)amino]benzoyl]-L-tryptophanate
Homo sapiens
pH and temperature not specified in the publication
0.00098
benzyl N-[4-amino-3-(L-norleucylamino)benzoyl]-L-tryptophanate
Homo sapiens
pH and temperature not specified in the publication
0.0016
benzyl N-[4-amino-3-(L-norleucylamino)benzoyl]-L-tryptophanate
Homo sapiens
pH and temperature not specified in the publication
0.0098
benzyl N-[4-amino-3-(L-tyrosylamino)benzoyl]-L-tryptophanate
Homo sapiens
pH and temperature not specified in the publication
0.04
benzyl N-[4-amino-3-(L-tyrosylamino)benzoyl]-L-tryptophanate
Homo sapiens
pH and temperature not specified in the publication
0.0000005
bestatin
Bos taurus
-
-
0.00144
bestatin
Pagrus major
-
in 25 mM sodium phosphate buffer (pH 7.0) containing 1 mM dithiothreitol and 0.02% NaN3, at 37°C
0.00441
bestatin
Sus scrofa
-
substrate 4-[(E)-2-[4-cyano-5-(dicyanomethylidene)-2,2-dimethyl-2,5-dihydrofuran-3-yl]ethenyl]phenyl L-leucinate, pH 7.4, 25°C
0.007
bestatin
Sus scrofa
-
pH 8.0, 31°C, versus substrate L-leucine-4-nitroanilide
0.007
bestatin
Sus scrofa
-
substrate N-(6-methoxy-2-methylpyridin-3-yl),(S)-2-amino-4-methylpentanamide, pH not specified in the publication, temperature not specified in the publication
0.01487
bestatin
Plasmodium vivax
pH and temperature not specified in the publication
0.0149
bestatin
Plasmodium falciparum
inhibitory activity against recombinant enzyme
0.025
bestatin
Sus scrofa
-
pH 8.0, 31°C, versus substrate N-(6-methoxypyridin-3-yl)-(S)-2-amino-4-methylpentanamide
0.025
bestatin
Sus scrofa
-
substrate L-leucine-4-nitroanilide, pH not specified in the publication, temperature not specified in the publication
0.058
methyl 3-amino-4-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoate
Homo sapiens
pH and temperature not specified in the publication
0.1
methyl 3-amino-4-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoate
Homo sapiens
pH and temperature not specified in the publication
0.0098
methyl 4-amino-3-(L-norleucylamino)benzoate
Homo sapiens
pH and temperature not specified in the publication
0.1
methyl 4-amino-3-(L-norleucylamino)benzoate
Homo sapiens
pH and temperature not specified in the publication
0.0055
methyl N-(3-amino-4-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-tyrosinate
Homo sapiens
pH and temperature not specified in the publication
0.0094
methyl N-(3-amino-4-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-tyrosinate
Homo sapiens
pH and temperature not specified in the publication
0.0077
methyl N-(4-amino-3-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-tyrosinate
Homo sapiens
pH and temperature not specified in the publication
0.1
methyl N-(4-amino-3-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-tyrosinate
Homo sapiens
pH and temperature not specified in the publication
0.0014
methyl N-[3-amino-4-(L-arginylamino)benzoyl]-L-tyrosinate
Homo sapiens
pH and temperature not specified in the publication
0.0026
methyl N-[3-amino-4-(L-arginylamino)benzoyl]-L-tyrosinate
Homo sapiens
pH and temperature not specified in the publication
0.000755
methyl N-[3-amino-4-(L-norleucylamino)benzoyl]-L-tyrosinate
Homo sapiens
pH and temperature not specified in the publication
0.1
methyl N-[3-amino-4-(L-norleucylamino)benzoyl]-L-tyrosinate
Homo sapiens
pH and temperature not specified in the publication
0.015
methyl N-[3-amino-4-(L-tyrosylamino)benzoyl]-L-tyrosinate
Homo sapiens
pH and temperature not specified in the publication
0.016
methyl N-[3-amino-4-(L-tyrosylamino)benzoyl]-L-tyrosinate
Homo sapiens
pH and temperature not specified in the publication
0.0064
methyl N-[4-amino-3-(D-norleucylamino)benzoyl]-D-tyrosinate
Homo sapiens
pH and temperature not specified in the publication
0.1
methyl N-[4-amino-3-(D-norleucylamino)benzoyl]-D-tyrosinate
Homo sapiens
pH and temperature not specified in the publication
0.000518
methyl N-[4-amino-3-(L-arginylamino)benzoyl]-D-tyrosinate
Homo sapiens
pH and temperature not specified in the publication
0.0096
methyl N-[4-amino-3-(L-arginylamino)benzoyl]-D-tyrosinate
Homo sapiens
pH and temperature not specified in the publication
0.039
methyl N-[4-amino-3-(L-tyrosylamino)benzoyl]-L-threoninate
Homo sapiens
pH and temperature not specified in the publication
0.1
methyl N-[4-amino-3-(L-tyrosylamino)benzoyl]-L-threoninate
Homo sapiens
pH and temperature not specified in the publication
0.033
methyl N-[4-amino-3-(L-tyrosylamino)benzoyl]-L-tyrosinate
Homo sapiens
pH and temperature not specified in the publication
0.11
methyl N-[4-amino-3-(L-tyrosylamino)benzoyl]-L-tyrosinate
Homo sapiens
pH and temperature not specified in the publication
0.011
methyl N2-(3-amino-4-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-argininate
Homo sapiens
pH and temperature not specified in the publication
0.012
methyl N2-(3-amino-4-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-argininate
Homo sapiens
pH and temperature not specified in the publication
0.0048
methyl N2-(4-amino-3-[[(2S)-2-amino-4-(4-hydroxyphenyl)butanoyl]amino]benzoyl)-L-lysinate
Homo sapiens
pH and temperature not specified in the publication
0.1
methyl N2-(4-amino-3-[[(2S)-2-amino-4-(4-hydroxyphenyl)butanoyl]amino]benzoyl)-L-lysinate
Homo sapiens
pH and temperature not specified in the publication
0.002
methyl N2-(4-amino-3-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-lysinate
Homo sapiens
pH and temperature not specified in the publication
0.0249
methyl N2-(4-amino-3-[[(2S)-2-amino-4-phenylbutanoyl]amino]benzoyl)-L-lysinate
Homo sapiens
pH and temperature not specified in the publication
0.017
methyl N2-[4-amino-3-(L-arginylamino)benzoyl]-L-lysinate
Homo sapiens
pH and temperature not specified in the publication
0.042
methyl N2-[4-amino-3-(L-arginylamino)benzoyl]-L-lysinate
Homo sapiens
pH and temperature not specified in the publication
0.0025
methyl N2-[4-amino-3-(L-norleucylamino)benzoyl]-D-argininate
Homo sapiens
pH and temperature not specified in the publication
0.0107
methyl N2-[4-amino-3-(L-norleucylamino)benzoyl]-D-argininate
Homo sapiens
pH and temperature not specified in the publication
0.0083
methyl N2-[4-amino-3-(L-norleucylamino)benzoyl]-L-lysinate
Homo sapiens
pH and temperature not specified in the publication
0.018
methyl N2-[4-amino-3-(L-norleucylamino)benzoyl]-L-lysinate
Homo sapiens
pH and temperature not specified in the publication
0.013
methyl N2-[4-amino-3-([(2S)-2-amino-4-[4-(benzyloxy)phenyl]butanoyl]amino)benzoyl]-L-lysinate
Homo sapiens
pH and temperature not specified in the publication
0.1
methyl N2-[4-amino-3-([(2S)-2-amino-4-[4-(benzyloxy)phenyl]butanoyl]amino)benzoyl]-L-lysinate
Homo sapiens
pH and temperature not specified in the publication
0.0019
N-(3,4-diaminobenzoyl)-L-tryptophan
Homo sapiens
pH and temperature not specified in the publication
0.1
N-(3,4-diaminobenzoyl)-L-tryptophan
Homo sapiens
pH and temperature not specified in the publication
0.008
N-(3-amino-4-[[(2S)-2-amino-4-(4-hydroxyphenyl)butanoyl]amino]benzoyl)-L-tryptophan
Homo sapiens
pH and temperature not specified in the publication
0.0094
N-(3-amino-4-[[(2S)-2-amino-4-(4-hydroxyphenyl)butanoyl]amino]benzoyl)-L-tryptophan
Homo sapiens
pH and temperature not specified in the publication
0.038
N-(4-amino-3-[[(2R)-2-amino-4-(4-hydroxyphenyl)butanoyl]amino]benzoyl)-L-tryptophan
Homo sapiens
pH and temperature not specified in the publication
0.1
N-(4-amino-3-[[(2R)-2-amino-4-(4-hydroxyphenyl)butanoyl]amino]benzoyl)-L-tryptophan
Homo sapiens
pH and temperature not specified in the publication
0.0011
N-[3-amino-4-(L-arginylamino)benzoyl]-L-tryptophan
Homo sapiens
pH and temperature not specified in the publication
0.0038
N-[3-amino-4-(L-arginylamino)benzoyl]-L-tryptophan
Homo sapiens
pH and temperature not specified in the publication
0.000237
N-[3-amino-4-(L-norleucylamino)benzoyl]-L-tryptophan
Homo sapiens
pH and temperature not specified in the publication
0.0028
N-[3-amino-4-(L-norleucylamino)benzoyl]-L-tryptophan
Homo sapiens
pH and temperature not specified in the publication
0.0048
N-[3-amino-4-(L-tyrosylamino)benzoyl]-L-tryptophan
Homo sapiens
pH and temperature not specified in the publication
0.019
N-[3-amino-4-(L-tyrosylamino)benzoyl]-L-tryptophan
Homo sapiens
pH and temperature not specified in the publication
0.000589
N-[4-amino-3-(L-arginylamino)benzoyl]-L-tryptophan
Homo sapiens
pH and temperature not specified in the publication
0.0012
N-[4-amino-3-(L-arginylamino)benzoyl]-L-tryptophan
Homo sapiens
pH and temperature not specified in the publication
0.0036
N-[4-amino-3-(L-norleucylamino)benzoyl]-L-tryptophan
Homo sapiens
pH and temperature not specified in the publication
0.0038
N-[4-amino-3-(L-norleucylamino)benzoyl]-L-tryptophan
Homo sapiens
pH and temperature not specified in the publication
0.012
N-[4-amino-3-(L-tyrosylamino)benzoyl]-L-tryptophan
Homo sapiens
pH and temperature not specified in the publication
0.1
N-[4-amino-3-(L-tyrosylamino)benzoyl]-L-tryptophan
Homo sapiens
pH and temperature not specified in the publication
0.0021
N2-[4-amino-3-(L-leucylamino)benzoyl]-L-lysine
Homo sapiens
pH and temperature not specified in the publication
0.0068
N2-[4-amino-3-(L-leucylamino)benzoyl]-L-lysine
Homo sapiens
pH and temperature not specified in the publication
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evolution
leucine aminopeptidases (LAPs) are members of the aminopeptidase M1/M17 family
evolution
phylogenetic analysis reveals that AcLAP clusters into a clade closely related with LAPs from Amoebozoa, including Dictyostelium sp.. The enzyme contains the highly conserved M17 aminopeptidase family signature sequence (NTDAEGRL, residues 425-432) and highly conserved amino acid residues for metal binding (D350, D368, D427, E429) and catalytic site formation (K357, R431). The enzyme belongs to the M17 family of proteases
evolution
-
the adipocyte-derived leucine aminopeptidase (A-LAP) is a member of the M1 family of zinc metallopeptidases
evolution
-
the adipocyte-derived leucine aminopeptidase (A-LAP) is a member of the M1 family of zinc metallopeptidases
evolution
the enzyme belongs to the M17 family of proteases
evolution
the enzyme belongs to the M17 family of proteases
evolution
the enzyme belongs to the M17 peptidase family
evolution
the leucine aminopeptidase (LAP) is a member of the M17 family of metalloproteases
evolution
the leucine aminopeptidase (LAP) is a member of the M17 family of metalloproteases
evolution
the leucine aminopeptidase (LAP) is a member of the M17 family of metalloproteases
evolution
-
the leucine aminopeptidases (LAPs) are members of the M17 family of Zn metalloproteases
evolution
the putative substrate binding site GGMEN, zinc-binding motif HEXXHX18E and the catalytic residues involved in aminopeptidase activity are all conserved, PtLAP is a member of M1 leucine aminopeptidases
evolution
-
the enzyme belongs to the M17 family of proteases
-
evolution
-
the putative substrate binding site GGMEN, zinc-binding motif HEXXHX18E and the catalytic residues involved in aminopeptidase activity are all conserved, PtLAP is a member of M1 leucine aminopeptidases
-
malfunction
disruption of the LAP-A hexameric structure increases chaperone activity
malfunction
-
disruption of the pepZ gene results in an attenuation of virulence in both localized and systemic models of infection
malfunction
-
inhibition of LAP with bestatin does not adversely affect growth of Staphylococcus aureus or biofilm formation
malfunction
-
lysates from pepZ mutant cells show leucine aminopeptidase activity comparable to that of the wild-type strain suggesting that the majority of leucine aminopeptidase activity observed in Staphylococcus aureus cells comes from PepS, and not LAP
malfunction
-
bestatin and knockdown of LAP3 upregulate phosphorylation of Hsp27 and downregulate expression of fascin. Phosphorylation of Akt and expression of matrix metalloproteinase-2/9 can also be downregulated. LAP3 overexpression showed the opposite results
malfunction
-
knockdown of A-LAP expression by siRNA inhibits HUVEC angiogenesis
malfunction
lack of extracellular PaAP in biofilms leading to bacterial cell death implies that PaAP might function as a nutrient recycler within a biofilm. Biomass reduction of mutant DELTApaaP grown under a continuous media flow has one day delay compared with the DELTApaaP pellicles grown on static media. Lack of extracellular PaAP triggers bacterial cell death and bacterial cell death in DELTApaaP biofilms is independent of Psl, while the disruption of DELTApaaP biofilms is a result of the degradation of Psl matrix by PslG released from the dead bacteria within biofilms, which in turn led to the dispersion of live bacteria from biofilms into effluents
malfunction
lack or downregulation of AcLAP activity causes ultrastructural changes of the cell wall in Acanthamoeba castellanii that are closely associated with inhibition of cyst formation
malfunction
S-Lap1 gene mutant homozygotes are male sterile. The male sterile phenotype of S-Lap enzyme mutants is caused by defects in paracrystalline material accumulation and abnormal structure of the elongated major mitochondrial derivatives and elongated spermatids
malfunction
S-Lap2 gene mutant homozygotes are male sterile. The male sterile phenotype of S-Lap enzyme mutants is caused by defects in paracrystalline material accumulation and abnormal structure of the elongated major mitochondrial derivatives and elongated spermatids
malfunction
S-Lap3 gene mutant homozygotes are male sterile. The male sterile phenotype of S-Lap enzyme mutants is caused by defects in paracrystalline material accumulation and abnormal structure of the elongated major mitochondrial derivatives and elongated spermatids
malfunction
S-Lap4 gene mutant homozygotes are male semi-sterile. The male sterile phenotype of S-Lap enzyme mutants is caused by defects in paracrystalline material accumulation and abnormal structure of the elongated major mitochondrial derivatives and elongated spermatids
malfunction
S-Lap5 gene mutant homozygotes are male sterile. The male sterile phenotype of S-Lap enzyme mutants is caused by defects in paracrystalline material accumulation and abnormal structure of the elongated major mitochondrial derivatives and elongated spermatids
malfunction
S-Lap6 gene mutant homozygotes are male sterile. The male sterile phenotype of S-Lap enzyme mutants is caused by defects in paracrystalline material accumulation and abnormal structure of the elongated major mitochondrial derivatives and elongated spermatids
malfunction
S-Lap7 gene mutant homozygotes are male sterile. The male sterile phenotype of S-Lap enzyme mutants is caused by defects in paracrystalline material accumulation and abnormal structure of the elongated major mitochondrial derivatives and elongated spermatids
malfunction
S-Lap8 gene mutant homozygotes are male sterile. The male sterile phenotype of S-Lap enzyme mutants is caused by defects in paracrystalline material accumulation and abnormal structure of the elongated major mitochondrial derivatives and elongated spermatids
malfunction
TbLAP1 knockdown results in delayed cytokinesis and ectopic expression leading to kDNA loss and decreased cell proliferation. Knockdown of TbLAP1 by RNAi leads to accumulation of 2K2N cells. Recombinant Ectopic expression of HA-tagged TbLAP1 in procyclic Trypanosoma brucei induces a significant growth defect, which is manifested by the accumulation of 0K1N cells and a defect in mt membrane potential. RNAi-mediated downregulation of TbLAP1 results in a growth defect
malfunction
-
lack of extracellular PaAP in biofilms leading to bacterial cell death implies that PaAP might function as a nutrient recycler within a biofilm. Biomass reduction of mutant DELTApaaP grown under a continuous media flow has one day delay compared with the DELTApaaP pellicles grown on static media. Lack of extracellular PaAP triggers bacterial cell death and bacterial cell death in DELTApaaP biofilms is independent of Psl, while the disruption of DELTApaaP biofilms is a result of the degradation of Psl matrix by PslG released from the dead bacteria within biofilms, which in turn led to the dispersion of live bacteria from biofilms into effluents
-
malfunction
-
lack of extracellular PaAP in biofilms leading to bacterial cell death implies that PaAP might function as a nutrient recycler within a biofilm. Biomass reduction of mutant DELTApaaP grown under a continuous media flow has one day delay compared with the DELTApaaP pellicles grown on static media. Lack of extracellular PaAP triggers bacterial cell death and bacterial cell death in DELTApaaP biofilms is independent of Psl, while the disruption of DELTApaaP biofilms is a result of the degradation of Psl matrix by PslG released from the dead bacteria within biofilms, which in turn led to the dispersion of live bacteria from biofilms into effluents
-
malfunction
-
lack of extracellular PaAP in biofilms leading to bacterial cell death implies that PaAP might function as a nutrient recycler within a biofilm. Biomass reduction of mutant DELTApaaP grown under a continuous media flow has one day delay compared with the DELTApaaP pellicles grown on static media. Lack of extracellular PaAP triggers bacterial cell death and bacterial cell death in DELTApaaP biofilms is independent of Psl, while the disruption of DELTApaaP biofilms is a result of the degradation of Psl matrix by PslG released from the dead bacteria within biofilms, which in turn led to the dispersion of live bacteria from biofilms into effluents
-
malfunction
-
lack of extracellular PaAP in biofilms leading to bacterial cell death implies that PaAP might function as a nutrient recycler within a biofilm. Biomass reduction of mutant DELTApaaP grown under a continuous media flow has one day delay compared with the DELTApaaP pellicles grown on static media. Lack of extracellular PaAP triggers bacterial cell death and bacterial cell death in DELTApaaP biofilms is independent of Psl, while the disruption of DELTApaaP biofilms is a result of the degradation of Psl matrix by PslG released from the dead bacteria within biofilms, which in turn led to the dispersion of live bacteria from biofilms into effluents
-
malfunction
-
lack of extracellular PaAP in biofilms leading to bacterial cell death implies that PaAP might function as a nutrient recycler within a biofilm. Biomass reduction of mutant DELTApaaP grown under a continuous media flow has one day delay compared with the DELTApaaP pellicles grown on static media. Lack of extracellular PaAP triggers bacterial cell death and bacterial cell death in DELTApaaP biofilms is independent of Psl, while the disruption of DELTApaaP biofilms is a result of the degradation of Psl matrix by PslG released from the dead bacteria within biofilms, which in turn led to the dispersion of live bacteria from biofilms into effluents
-
malfunction
-
lack of extracellular PaAP in biofilms leading to bacterial cell death implies that PaAP might function as a nutrient recycler within a biofilm. Biomass reduction of mutant DELTApaaP grown under a continuous media flow has one day delay compared with the DELTApaaP pellicles grown on static media. Lack of extracellular PaAP triggers bacterial cell death and bacterial cell death in DELTApaaP biofilms is independent of Psl, while the disruption of DELTApaaP biofilms is a result of the degradation of Psl matrix by PslG released from the dead bacteria within biofilms, which in turn led to the dispersion of live bacteria from biofilms into effluents
-
malfunction
-
TbLAP1 knockdown results in delayed cytokinesis and ectopic expression leading to kDNA loss and decreased cell proliferation. Knockdown of TbLAP1 by RNAi leads to accumulation of 2K2N cells. Recombinant Ectopic expression of HA-tagged TbLAP1 in procyclic Trypanosoma brucei induces a significant growth defect, which is manifested by the accumulation of 0K1N cells and a defect in mt membrane potential. RNAi-mediated downregulation of TbLAP1 results in a growth defect
-
malfunction
-
lack of extracellular PaAP in biofilms leading to bacterial cell death implies that PaAP might function as a nutrient recycler within a biofilm. Biomass reduction of mutant DELTApaaP grown under a continuous media flow has one day delay compared with the DELTApaaP pellicles grown on static media. Lack of extracellular PaAP triggers bacterial cell death and bacterial cell death in DELTApaaP biofilms is independent of Psl, while the disruption of DELTApaaP biofilms is a result of the degradation of Psl matrix by PslG released from the dead bacteria within biofilms, which in turn led to the dispersion of live bacteria from biofilms into effluents
-
physiological function
-
LAP may play regulatory roles in protein biosynthesis and degradation in basophilic cells
physiological function
LAP plays a central role in hatching of the miracidium from the schistosome egg
physiological function
-
LAP plays a vital role in the development of oocytes, vitellogenesis
physiological function
lapA is a late wound-response gene of tomato, LapA is involved in protection against Manduca sexta damage
physiological function
the enzyme is responsible for the catabolism of host hemoglobin
physiological function
-
the M17 leucine aminopeptidase of the intraerythrocytic stages of the malaria parasite Plasmodium falciparum plays a role in releasing amino acids from host hemoglobin that are used for parasite protein synthesis, growth, and development
physiological function
-
enzymatic properties to participate in generating or destroying MHC class I-presented peptides
physiological function
-
key roles in senescence, stress response and amino acid turn over
physiological function
-
immunization with recombinant Fasciola gigantica LAP (FgLAP) elicits high levels of immune responses and protection against Fasciola gigantica in mice
physiological function
-
LAP is required for survival inside human macrophages
physiological function
LAP-A exhibits chaperone activity which is independant of its peptidase activity
physiological function
rMHJ_0461 binds plasminogen and facilitates plasmin conversion
physiological function
AcLAP is a typical M17 family enzyme that plays an essential role during encystation of Acanthamoeba castellanii
physiological function
-
adipocyte-derived leucine aminopeptidase (A-LAP) plays a crucial role in angiogenesis
physiological function
-
adipocyte-derived leucine aminopeptidase (A-LAP) plays a crucial role in angiogenesis
physiological function
enzyme Lap1 improves the degree of hydrolysis of casein and soy protein hydrolysates and also decreases their bitterness, indicating its potential utility in food production
physiological function
expression of leucine aminopeptidase 3 (LAP3) is associated with the prognosis for and malignant transformation of many types of tumors
physiological function
-
isozyme SmLAP1 is involved in digestion
physiological function
leucine aminopeptidase is an important metalloexopeptidase that catalyze the hydrolysis of N-terminal leucine residues from polypeptides and proteins
physiological function
leucine aminopeptidases (LAPs) are metallopeptidases that catalyze the hydrolysis of leucine residues and other N-terminal residues from proteins and peptides. The extracellular enzyme PtLAP executes the degradation of organic matters, contributes to the adaptive survival of microbe in deep-sea environment and may play important roles in marine biogeochemical cycles. The recombinant enzyme rPtLAP can significantly promote the proliferation of tumor cells, including the cell lines HCT116, BEL-7402 and Hela, while displays no effect on that of normal cell line 3T3
physiological function
leucine aminopeptidases (LAPs) of the M17 peptidase family have important functions in regulating the balance of catabolism and anabolism, cell maintenance, growth and defense
physiological function
M17 leucine amino peptidase (M17 LAP) plays an important role in the hydrolysis of amino acids essential for growth and development of Plasmodium vivax
physiological function
-
overexpression of leucine aminopeptidase 3 (LAP3) is involved in proliferation, migration, and invasion of several tumor cells and plays a crucial role in tumor metastasis, role of LAP3 in the regulation of cancer cell migration and invasion, overview. High LAP3 expression is correlated with the grade of malignancy, phenotypes, overview. LAP3 promotes fascin expression through the p38-Hsp27-NF-kappaB signaling pathway
physiological function
sperm-leucylaminopeptidases are required for male fertility as structural components of mitochondrial paracrystalline material in Drosophila melanogaster sperm
physiological function
the enzyme is not required for the growth of this parasite either in vitro or in vivo. Role of LAP-A in leucine starvation, overview
physiological function
the enzyme is not required for the growth of this parasite either in vitro or in vivo. Role of LAP-A in leucine starvation, overview
physiological function
the enzyme is not required for the growth of this parasite either in vitro or in vivo. Role of LAP-A in leucine starvation, overview
physiological function
the extracellular aminopeptidase PaAP can release amino acids from the N-terminus of peptide or protein. It modulates biofilm development of Pseudomonas aeruginosa by affecting matrix exopolysaccharide Psl and bacterial cell death. PaAP is a quorum sensing-regulated protein, thus its expression is largely activated at high bacterial density. PaAP might function as a nutrient recycler within a biofilm
physiological function
the leucine aminopeptidase is involved in kinetoplast DNA segregation in Trypanosoma brucei. TbLAP1 is a mt protein that dynamically associates with kDNA during the cell cycle. The protein localizes to kDNA and the umbilicus, the prominent proteinaceous structure which in the mammalian parasite Trypanosoma brucei connecting progeny kDNAs at late stages of segregation, indicating a role of TbLAP1 in resolving kDNA replication. TbLAP1 is required for correct segregation of kinetoplast DNA and the separation of daughter kinetoplast DNA, overview
physiological function
trigger enzymes combine metabolic function with regulation of gene expression. Escherichia coli aminopeptidase A (PepA) is a trigger enzyme endowed with catalytic activity and DNA-binding properties prominent in transcriptional regulation and site-specific DNA recombination. PepA is a repressor in its own right, capable of specifically inhibiting transcription initiation at promoter P1 of the carAB operon, encoding carbamoylphosphate synthase. Furthermore, PepA binding constrains a single positive supercoil in the carP1 control region. Such a topological event is understood to constitute an impediment to transcription initiation and may serve as a mechanism to regulate gene expression. The observed inhibitory effect of PepA at carP1 is specific
physiological function
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the extracellular aminopeptidase PaAP can release amino acids from the N-terminus of peptide or protein. It modulates biofilm development of Pseudomonas aeruginosa by affecting matrix exopolysaccharide Psl and bacterial cell death. PaAP is a quorum sensing-regulated protein, thus its expression is largely activated at high bacterial density. PaAP might function as a nutrient recycler within a biofilm
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physiological function
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enzyme Lap1 improves the degree of hydrolysis of casein and soy protein hydrolysates and also decreases their bitterness, indicating its potential utility in food production
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physiological function
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LAP may play regulatory roles in protein biosynthesis and degradation in basophilic cells
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physiological function
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M17 leucine amino peptidase (M17 LAP) plays an important role in the hydrolysis of amino acids essential for growth and development of Plasmodium vivax
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physiological function
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the extracellular aminopeptidase PaAP can release amino acids from the N-terminus of peptide or protein. It modulates biofilm development of Pseudomonas aeruginosa by affecting matrix exopolysaccharide Psl and bacterial cell death. PaAP is a quorum sensing-regulated protein, thus its expression is largely activated at high bacterial density. PaAP might function as a nutrient recycler within a biofilm
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physiological function
-
the extracellular aminopeptidase PaAP can release amino acids from the N-terminus of peptide or protein. It modulates biofilm development of Pseudomonas aeruginosa by affecting matrix exopolysaccharide Psl and bacterial cell death. PaAP is a quorum sensing-regulated protein, thus its expression is largely activated at high bacterial density. PaAP might function as a nutrient recycler within a biofilm
-
physiological function
-
the extracellular aminopeptidase PaAP can release amino acids from the N-terminus of peptide or protein. It modulates biofilm development of Pseudomonas aeruginosa by affecting matrix exopolysaccharide Psl and bacterial cell death. PaAP is a quorum sensing-regulated protein, thus its expression is largely activated at high bacterial density. PaAP might function as a nutrient recycler within a biofilm
-
physiological function
-
the extracellular aminopeptidase PaAP can release amino acids from the N-terminus of peptide or protein. It modulates biofilm development of Pseudomonas aeruginosa by affecting matrix exopolysaccharide Psl and bacterial cell death. PaAP is a quorum sensing-regulated protein, thus its expression is largely activated at high bacterial density. PaAP might function as a nutrient recycler within a biofilm
-
physiological function
-
the extracellular aminopeptidase PaAP can release amino acids from the N-terminus of peptide or protein. It modulates biofilm development of Pseudomonas aeruginosa by affecting matrix exopolysaccharide Psl and bacterial cell death. PaAP is a quorum sensing-regulated protein, thus its expression is largely activated at high bacterial density. PaAP might function as a nutrient recycler within a biofilm
-
physiological function
-
the leucine aminopeptidase is involved in kinetoplast DNA segregation in Trypanosoma brucei. TbLAP1 is a mt protein that dynamically associates with kDNA during the cell cycle. The protein localizes to kDNA and the umbilicus, the prominent proteinaceous structure which in the mammalian parasite Trypanosoma brucei connecting progeny kDNAs at late stages of segregation, indicating a role of TbLAP1 in resolving kDNA replication. TbLAP1 is required for correct segregation of kinetoplast DNA and the separation of daughter kinetoplast DNA, overview
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physiological function
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leucine aminopeptidases (LAPs) are metallopeptidases that catalyze the hydrolysis of leucine residues and other N-terminal residues from proteins and peptides. The extracellular enzyme PtLAP executes the degradation of organic matters, contributes to the adaptive survival of microbe in deep-sea environment and may play important roles in marine biogeochemical cycles. The recombinant enzyme rPtLAP can significantly promote the proliferation of tumor cells, including the cell lines HCT116, BEL-7402 and Hela, while displays no effect on that of normal cell line 3T3
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physiological function
-
the extracellular aminopeptidase PaAP can release amino acids from the N-terminus of peptide or protein. It modulates biofilm development of Pseudomonas aeruginosa by affecting matrix exopolysaccharide Psl and bacterial cell death. PaAP is a quorum sensing-regulated protein, thus its expression is largely activated at high bacterial density. PaAP might function as a nutrient recycler within a biofilm
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additional information
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regulation of the tick molecules involved in nutrient metabolism for the reproduction, including blood digestion and vitellogenesis, would help in controlling the tick population and tick-borne pathogens
additional information
recombinant Lap1 enzyme has a conserved functional charge/dipole complex and a hydrogen bond network of Zn2-D179-S228-Q177-D229-S158 around its active center. An acidic Asp residue is found at the bottom of the substrate binding pocket, which explains its preference for basic N-terminal amino acid substrates such as Arg and Lys. Three-dimensional structure modelling of rLap1 and substrate-docking analysis
additional information
-
recombinant Lap1 enzyme has a conserved functional charge/dipole complex and a hydrogen bond network of Zn2-D179-S228-Q177-D229-S158 around its active center. An acidic Asp residue is found at the bottom of the substrate binding pocket, which explains its preference for basic N-terminal amino acid substrates such as Arg and Lys. Three-dimensional structure modelling of rLap1 and substrate-docking analysis
additional information
structure comparisons of plasmodial LAP-As from Trypanosoma brucei subsp. brucei, Trypanosoma cruzi, and Leishmania major, overview. Structural differences in LmLAP-A compared to TbLAP-A and TcLAP-A are mostly located in the loop regions
additional information
structure comparisons of plasmodial LAP-As from Trypanosoma brucei subsp. brucei, Trypanosoma cruzi, and Leishmania major, overview. Structural differences in LmLAP-A compared to TbLAP-A and TcLAP-A are mostly located in the loop regions
additional information
structure comparisons of plasmodial LAP-As from Trypanosoma brucei subsp. brucei, Trypanosoma cruzi, and Leishmania major, overview. Structural differences in LmLAP-A compared to TbLAP-A and TcLAP-A are mostly located in the loop regions
additional information
structure homology modelling of Plasmodium vivax LAP using the crystal structure of Plasmodium falciparum LAP, PDB ID 3KQX, as template, overview
additional information
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structure homology modelling of Plasmodium vivax LAP using the crystal structure of Plasmodium falciparum LAP, PDB ID 3KQX, as template, overview
additional information
the enzyme contains a signal peptide (residues 1-21), a peptidase_M1 domain (Pfam 01433, residues 32-398) and a leuk-A4-hydro_C domain (SMART 001263, residues 474-612) in PtLAP. Both of the putative substrate binding site GGMEN and zinc-binding motif HEXXHX18E in peptidase_M1 domain are conserved in PtLAP, locating from ressidues 282-286 and 309-332, respectively. The catalytic residues involved in aminopeptidase activity are Glu285 and Tyr395 in PtLAP, which probably act as a general base and a proton donor
additional information
-
recombinant Lap1 enzyme has a conserved functional charge/dipole complex and a hydrogen bond network of Zn2-D179-S228-Q177-D229-S158 around its active center. An acidic Asp residue is found at the bottom of the substrate binding pocket, which explains its preference for basic N-terminal amino acid substrates such as Arg and Lys. Three-dimensional structure modelling of rLap1 and substrate-docking analysis
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additional information
-
structure homology modelling of Plasmodium vivax LAP using the crystal structure of Plasmodium falciparum LAP, PDB ID 3KQX, as template, overview
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additional information
-
the enzyme contains a signal peptide (residues 1-21), a peptidase_M1 domain (Pfam 01433, residues 32-398) and a leuk-A4-hydro_C domain (SMART 001263, residues 474-612) in PtLAP. Both of the putative substrate binding site GGMEN and zinc-binding motif HEXXHX18E in peptidase_M1 domain are conserved in PtLAP, locating from ressidues 282-286 and 309-332, respectively. The catalytic residues involved in aminopeptidase activity are Glu285 and Tyr395 in PtLAP, which probably act as a general base and a proton donor
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R440A
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essential residue in catalysis
N345L
the mutation results in 93% reduction in LAP activity
N345Q
the mutation results in 72% reduction in LAP activity
N435E
the mutation results in complete loss of the LAP activity
N435L
the mutation results in complete loss of the LAP activity
N435Q
the mutation results in complete loss of the LAP activity
N435R
the mutation results in complete loss of the LAP activity
D375A
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leukotriene A4 hydrolase mutant
K528A
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gene A-LAP, site-directed mutagenesis, the mutant enzyme shows reduced activity
K528H
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gene A-LAP, site-directed mutagenesis, the mutant enzyme shows reduced activity
K528M
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gene A-LAP, site-directed mutagenesis, the mutant enzyme shows reduced activity
E343A
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site-directed mutagenesis, inactive, dominant-negative mutant
E365A
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site-directed mutagenesis, inactive mutant
K310V
increased specificty for Leu as Xaa, no activity with Asp-Leu in opposite to the wild-type enzyme
R402W
reduced activity with Asp-Leu compared to the wild-type enzyme
D347G
-
oligonucleotide site-directed mutagenesis, formation of a stable hexamer corresponding to the wild-type enzyme, nearly catalytically inactive with dipeptide substrates
D347I
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oligonucleotide site-directed mutagenesis, no formation of stable hexamer, inactive mutant
D347S
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oligonucleotide site-directed mutagenesis, no formation of stable hexamer, inactive mutant
D347V
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oligonucleotide site-directed mutagenesis, no formation of stable hexamer, inactive mutant
D347Y
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oligonucleotide site-directed mutagenesis, formation of a more complex structure compared to the wild-type enzyme
D354E
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oligonucleotide site-directed mutagenesis, no formation of stable hexamer, inactive mutant
D354M
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oligonucleotide site-directed mutagenesis, reduced catalytic activity with dipeptide substrates compared to the wild-type
D354R
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oligonucleotide site-directed mutagenesis, no formation of stable hexamer, reduced catalytic activity with dipeptide substrates compared to the wild-type
E429A
-
oligonucleotide site-directed mutagenesis, no formation of stable hexamer, inactive mutant
E429G
-
oligonucleotide site-directed mutagenesis, no formation of stable hexamer, inactive mutant
E429Q
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oligonucleotide site-directed mutagenesis, no formation of stable hexamer, inactive mutant
E429R
inactive mutant with disrupted hexameric structure has increased chaperone activity
E429S
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oligonucleotide site-directed mutagenesis, formation of a stable hexamer corresponding to the wild-type enzyme
E429W
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oligonucleotide site-directed mutagenesis, formation of a stable hexamer corresponding to the wild-type enzyme, nearly catalytically inactive with dipeptide substrates
E429X
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site-directed mutagenesis, inactive mutants, overview
K354G
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oligonucleotide site-directed mutagenesis, formation of a more complex structure compared to the wild-type enzyme
K354M
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oligonucleotide site-directed mutagenesis, formation of a more complex structure compared to the wild-type enzyme
K354N
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oligonucleotide site-directed mutagenesis, formation of a more complex structure compared to the wild-type enzyme
K354T
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oligonucleotide site-directed mutagenesis, formation of a more complex structure compared to the wild-type enzyme
K354W
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oligonucleotide site-directed mutagenesis, formation of a more complex structure compared to the wild-type enzyme
K354X
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site-directed mutagenesis, inactive mutants, overview
R431G
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oligonucleotide site-directed mutagenesis, no formation of stable hexamer, inactive mutant
R431Q
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oligonucleotide site-directed mutagenesis, formation of a stable hexamer corresponding to the wild-type enzyme
R431V
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oligonucleotide site-directed mutagenesis, formation of a stable hexamer corresponding to the wild-type enzyme
R431W
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oligonucleotide site-directed mutagenesis, formation of a stable hexamer corresponding to the wild-type enzyme
K528R
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A-LAP polymorphism, leads to hypertension
K528R
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gene A-LAP, natural polymorphism and site-directed mutagenesis, hypertension-associated mutant, the mutant enzyme shows reduced activity
D347E
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oligonucleotide site-directed mutagenesis, formation of a more complex structure compared to the wild-type enzyme, nearly catalytically inactive with dipeptide substrates
D347E
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site-directed mutagenesis, inactive mutant
D347N
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oligonucleotide site-directed mutagenesis, no formation of stable hexamer, inactive mutant
D347N
mutation leads to inactivation of peptidase activity but does not have an impact on chaperone activity
D347R
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site-directed mutagenesis, reduced activity
D347R
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oligonucleotide site-directed mutagenesis, formation of a stable hexamer corresponding to the wild-type enzyme, reduced catalytic activity with dipeptide substrates compared to the wild-type
D347R
inactive mutant with disrupted hexameric structure has increased chaperone activity
E429D
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oligonucleotide site-directed mutagenesis, formation of a stable hexamer corresponding to the wild-type enzyme, activity with dipeptide substrates is similar or slightly reduced compared to the wild-type enzyme
E429D
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site-directed mutagenesis, 95% activity compared to wild-type enzyme
E429V
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oligonucleotide site-directed mutagenesis, formation of a stable hexamer corresponding to the wild-type enzyme, reduced catalytic activity with dipeptide substrates compared to the wild-type
E429V
mutation leads to inactivation of peptidase activity but does not have an impact on chaperone activity
K354E
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oligonucleotide site-directed mutagenesis, formation of a more complex structure compared to the wild-type enzyme
K354E
inactive mutant with disrupted hexameric structure has increased chaperone activity
K354R
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oligonucleotide site-directed mutagenesis, formation of a stable hexamer corresponding to the wild-type enzyme
K354R
mutation leads to inactivation of peptidase activity but does not have an impact on chaperone activity
R431A
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oligonucleotide site-directed mutagenesis, formation of a stable hexamer corresponding to the wild-type enzyme, nearly catalytically inactive with dipeptide substrates
R431A
mutation leads to inactivation of peptidase activity but does not have an impact on chaperone activity
R431K
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oligonucleotide site-directed mutagenesis, reduced catalytic activity with dipeptide substrates compared to the wild-type
R431K
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site-directed mutagenesis, 4fold reduced activity
additional information
AcLAP knockout using siRNA, AcLAP knockdown affects encystation of Acanthamoeba castellanii
additional information
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AcLAP knockout using siRNA, AcLAP knockdown affects encystation of Acanthamoeba castellanii
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant Mi(ET)S-Lap3MB01319, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant Mi(ET)S-Lap3MB01319, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant Mi(ET)S-Lap3MB01319, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant Mi(ET)S-Lap3MB01319, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant Mi(ET)S-Lap3MB01319, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant Mi(ET)S-Lap3MB01319, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant Mi(ET)S-Lap3MB01319, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant Mi(ET)S-Lap3MB01319, overview
additional information
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construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant Mi(ET)S-Lap3MB01319, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant Mi(ET1)S-Lap4MB11296, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant Mi(ET1)S-Lap4MB11296, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant Mi(ET1)S-Lap4MB11296, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant Mi(ET1)S-Lap4MB11296, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant Mi(ET1)S-Lap4MB11296, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant Mi(ET1)S-Lap4MB11296, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant Mi(ET1)S-Lap4MB11296, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant Mi(ET1)S-Lap4MB11296, overview
additional information
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construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant Mi(ET1)S-Lap4MB11296, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant Mi(MIC)S-Lap2MI14597, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant Mi(MIC)S-Lap2MI14597, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant Mi(MIC)S-Lap2MI14597, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant Mi(MIC)S-Lap2MI14597, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant Mi(MIC)S-Lap2MI14597, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant Mi(MIC)S-Lap2MI14597, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant Mi(MIC)S-Lap2MI14597, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant Mi(MIC)S-Lap2MI14597, overview
additional information
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construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant Mi(MIC)S-Lap2MI14597, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant S-Lap8KK106866, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant S-Lap8KK106866, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant S-Lap8KK106866, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant S-Lap8KK106866, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant S-Lap8KK106866, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant S-Lap8KK106866, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant S-Lap8KK106866, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant S-Lap8KK106866, overview
additional information
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construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, mutant S-Lap8KK106866, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, overview
additional information
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construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, overview
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, overview. Despite the mitochondrial localization, S-Lap1resc-HA construct is not able to rescue the male sterile phenotype of the S-Lap1DELTA7 mutant, indicating that the C-terminal tag may modify the structure of the protein, which could prevent its normal function
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, overview. Despite the mitochondrial localization, S-Lap1resc-HA construct is not able to rescue the male sterile phenotype of the S-Lap1DELTA7 mutant, indicating that the C-terminal tag may modify the structure of the protein, which could prevent its normal function
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, overview. Despite the mitochondrial localization, S-Lap1resc-HA construct is not able to rescue the male sterile phenotype of the S-Lap1DELTA7 mutant, indicating that the C-terminal tag may modify the structure of the protein, which could prevent its normal function
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, overview. Despite the mitochondrial localization, S-Lap1resc-HA construct is not able to rescue the male sterile phenotype of the S-Lap1DELTA7 mutant, indicating that the C-terminal tag may modify the structure of the protein, which could prevent its normal function
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, overview. Despite the mitochondrial localization, S-Lap1resc-HA construct is not able to rescue the male sterile phenotype of the S-Lap1DELTA7 mutant, indicating that the C-terminal tag may modify the structure of the protein, which could prevent its normal function
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, overview. Despite the mitochondrial localization, S-Lap1resc-HA construct is not able to rescue the male sterile phenotype of the S-Lap1DELTA7 mutant, indicating that the C-terminal tag may modify the structure of the protein, which could prevent its normal function
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, overview. Despite the mitochondrial localization, S-Lap1resc-HA construct is not able to rescue the male sterile phenotype of the S-Lap1DELTA7 mutant, indicating that the C-terminal tag may modify the structure of the protein, which could prevent its normal function
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, overview. Despite the mitochondrial localization, S-Lap1resc-HA construct is not able to rescue the male sterile phenotype of the S-Lap1DELTA7 mutant, indicating that the C-terminal tag may modify the structure of the protein, which could prevent its normal function
additional information
-
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, overview. Despite the mitochondrial localization, S-Lap1resc-HA construct is not able to rescue the male sterile phenotype of the S-Lap1DELTA7 mutant, indicating that the C-terminal tag may modify the structure of the protein, which could prevent its normal function
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, overview. Despite the mitochondrial localization, S-Lap1resc-HA construct is not able to rescue the male sterile phenotype of the S-Lap1DELTA7 mutant, indicating that the C-terminal tag may modify the structure of the protein, which could prevent its normal function. Strong reduction of S-Lap1-HAint in the pellet fraction of testis samples from the S-Lap1-HAint-containing S-Lap2MI14597, S-Lap3MB01319, S-Lap4MB11296, S-Lap5DELTA14, and S-Lap6MI06848 mutants, where the S-Lap1-HAint protein is present mainly in the supernatant, suggesting a problem with paracrystalline formation
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, overview. Despite the mitochondrial localization, S-Lap1resc-HA construct is not able to rescue the male sterile phenotype of the S-Lap1DELTA7 mutant, indicating that the C-terminal tag may modify the structure of the protein, which could prevent its normal function. Strong reduction of S-Lap1-HAint in the pellet fraction of testis samples from the S-Lap1-HAint-containing S-Lap2MI14597, S-Lap3MB01319, S-Lap4MB11296, S-Lap5DELTA14, and S-Lap6MI06848 mutants, where the S-Lap1-HAint protein is present mainly in the supernatant, suggesting a problem with paracrystalline formation
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, overview. Despite the mitochondrial localization, S-Lap1resc-HA construct is not able to rescue the male sterile phenotype of the S-Lap1DELTA7 mutant, indicating that the C-terminal tag may modify the structure of the protein, which could prevent its normal function. Strong reduction of S-Lap1-HAint in the pellet fraction of testis samples from the S-Lap1-HAint-containing S-Lap2MI14597, S-Lap3MB01319, S-Lap4MB11296, S-Lap5DELTA14, and S-Lap6MI06848 mutants, where the S-Lap1-HAint protein is present mainly in the supernatant, suggesting a problem with paracrystalline formation
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, overview. Despite the mitochondrial localization, S-Lap1resc-HA construct is not able to rescue the male sterile phenotype of the S-Lap1DELTA7 mutant, indicating that the C-terminal tag may modify the structure of the protein, which could prevent its normal function. Strong reduction of S-Lap1-HAint in the pellet fraction of testis samples from the S-Lap1-HAint-containing S-Lap2MI14597, S-Lap3MB01319, S-Lap4MB11296, S-Lap5DELTA14, and S-Lap6MI06848 mutants, where the S-Lap1-HAint protein is present mainly in the supernatant, suggesting a problem with paracrystalline formation
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, overview. Despite the mitochondrial localization, S-Lap1resc-HA construct is not able to rescue the male sterile phenotype of the S-Lap1DELTA7 mutant, indicating that the C-terminal tag may modify the structure of the protein, which could prevent its normal function. Strong reduction of S-Lap1-HAint in the pellet fraction of testis samples from the S-Lap1-HAint-containing S-Lap2MI14597, S-Lap3MB01319, S-Lap4MB11296, S-Lap5DELTA14, and S-Lap6MI06848 mutants, where the S-Lap1-HAint protein is present mainly in the supernatant, suggesting a problem with paracrystalline formation
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, overview. Despite the mitochondrial localization, S-Lap1resc-HA construct is not able to rescue the male sterile phenotype of the S-Lap1DELTA7 mutant, indicating that the C-terminal tag may modify the structure of the protein, which could prevent its normal function. Strong reduction of S-Lap1-HAint in the pellet fraction of testis samples from the S-Lap1-HAint-containing S-Lap2MI14597, S-Lap3MB01319, S-Lap4MB11296, S-Lap5DELTA14, and S-Lap6MI06848 mutants, where the S-Lap1-HAint protein is present mainly in the supernatant, suggesting a problem with paracrystalline formation
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, overview. Despite the mitochondrial localization, S-Lap1resc-HA construct is not able to rescue the male sterile phenotype of the S-Lap1DELTA7 mutant, indicating that the C-terminal tag may modify the structure of the protein, which could prevent its normal function. Strong reduction of S-Lap1-HAint in the pellet fraction of testis samples from the S-Lap1-HAint-containing S-Lap2MI14597, S-Lap3MB01319, S-Lap4MB11296, S-Lap5DELTA14, and S-Lap6MI06848 mutants, where the S-Lap1-HAint protein is present mainly in the supernatant, suggesting a problem with paracrystalline formation
additional information
construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, overview. Despite the mitochondrial localization, S-Lap1resc-HA construct is not able to rescue the male sterile phenotype of the S-Lap1DELTA7 mutant, indicating that the C-terminal tag may modify the structure of the protein, which could prevent its normal function. Strong reduction of S-Lap1-HAint in the pellet fraction of testis samples from the S-Lap1-HAint-containing S-Lap2MI14597, S-Lap3MB01319, S-Lap4MB11296, S-Lap5DELTA14, and S-Lap6MI06848 mutants, where the S-Lap1-HAint protein is present mainly in the supernatant, suggesting a problem with paracrystalline formation
additional information
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construction of mutants of lap genes S-Lap1 to S-Lap8, comparisons of the phenotypes of the mutant alleles of S-Lap genes, overview. Despite the mitochondrial localization, S-Lap1resc-HA construct is not able to rescue the male sterile phenotype of the S-Lap1DELTA7 mutant, indicating that the C-terminal tag may modify the structure of the protein, which could prevent its normal function. Strong reduction of S-Lap1-HAint in the pellet fraction of testis samples from the S-Lap1-HAint-containing S-Lap2MI14597, S-Lap3MB01319, S-Lap4MB11296, S-Lap5DELTA14, and S-Lap6MI06848 mutants, where the S-Lap1-HAint protein is present mainly in the supernatant, suggesting a problem with paracrystalline formation
additional information
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reduction of the numbers of laid eggs in the HlLAP gene knockdown ticks may be due to the degeneration of immature oocytes following deprivation of nutrients such as amino acids supplied not only by midgut HlLAP but also by the ovarian HlLAP
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knockdown of A-LAP expression by siRNA
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overexpression and knockdown of the enzyme in breast cancer cells indicate that LAP3 can promote metastasis. A lentiviral vector is introduced to overexpression or knockdown LAP3 in MDA-MB-231 and MCF-7 cells
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RNAi-mediated depletion of LAP-A, phenotype, overview
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construction of an enzyme deletion mutant DELTApaaP
additional information
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construction of an enzyme deletion mutant DELTApaaP
additional information
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construction of an enzyme deletion mutant DELTApaaP
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additional information
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construction of an enzyme deletion mutant DELTApaaP
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additional information
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construction of an enzyme deletion mutant DELTApaaP
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additional information
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construction of an enzyme deletion mutant DELTApaaP
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additional information
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construction of an enzyme deletion mutant DELTApaaP
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additional information
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construction of an enzyme deletion mutant DELTApaaP
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additional information
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construction of an enzyme deletion mutant DELTApaaP
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additional information
RNA interference targeting leucine aminopeptidase blocks hatching of Schistosoma mansoni eggs, overview. Knockdown of eitherSmLAP1 orSmLAP2, or both together, is accompanied by over 80% inhibition of hatching of schistosome eggs
additional information
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RNA interference targeting leucine aminopeptidase blocks hatching of Schistosoma mansoni eggs, overview. Knockdown of eitherSmLAP1 orSmLAP2, or both together, is accompanied by over 80% inhibition of hatching of schistosome eggs
additional information
construction of transgenic P35S:LapA tomato lines that are silenced in LapA or overexpress LapA. LapAManduca sexta larvae damage less foliage and display delays in growth and development when feeding on LapA-overexpressing transgenic plant leaves. Transgenic ectopic expression of LapA is not sufficient to induce Ser proteinase inhibitor Pin or polyphenol oxidase transcripts in non-wounded leaves. Larvae consume more foliage and attain larger masses when feeding on LapA-SI plants. Jasmonic acid does not complement the wound-signaling phenotype of LapA-SI plants. Phenotypes, overview
additional information
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construction of transgenic P35S:LapA tomato lines that are silenced in LapA or overexpress LapA. LapAManduca sexta larvae damage less foliage and display delays in growth and development when feeding on LapA-overexpressing transgenic plant leaves. Transgenic ectopic expression of LapA is not sufficient to induce Ser proteinase inhibitor Pin or polyphenol oxidase transcripts in non-wounded leaves. Larvae consume more foliage and attain larger masses when feeding on LapA-SI plants. Jasmonic acid does not complement the wound-signaling phenotype of LapA-SI plants. Phenotypes, overview
additional information
LAP-A exhibits chaperone activity which is independant of its peptidase activity
additional information
LAP-A exhibits chaperone activity which is independant of its peptidase activity
additional information
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LAP-A exhibits chaperone activity which is independant of its peptidase activity
additional information
knockdown of TbLAP1 by RNAi resulting in a growth defect
additional information
RNA interference (RNAi), double knockout (dKO), and overexpression of the protein in bloodstream form (BF) and procyclic form (PF) Trypanosoma brucei subsp. brucei parasites in culture. RNAi-mediated depletion of LAP-A, phenotype, overview
additional information
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knockdown of TbLAP1 by RNAi resulting in a growth defect
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additional information
RNAi-mediated depletion of LAP-A, phenotype, overview
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