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(3R)-3-([(5-hydroxy-1-phenyl-1H-pyrazol-3-yl)carbonyl]amino)-3-(2-methylphenyl)propanoic acid
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(3S)-3-(([1-(2-chlorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(2-methylphenyl)propanoic acid
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(3S)-3-(([1-(2-fluorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(2-methoxyphenyl)propanoic acid
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(3S)-3-(([1-(2-fluorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(2-methylphenyl)propanoic acid
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(3S)-3-(([1-(2-fluorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(3-methylphenyl)propanoic acid
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(3S)-3-(([1-(2-fluorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(4-methylphenyl)propanoic acid
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(3S)-3-(([1-(2-fluorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-[2-(trifluoromethyl)phenyl]propanoic acid
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(3S)-3-(([1-(3-chlorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(2-methylphenyl)propanoic acid
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(3S)-3-(([1-(3-fluorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(2-methylphenyl)propanoic acid
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(3S)-3-(([1-(4-fluorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(2-methylphenyl)propanoic acid
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(3S)-3-(([4-chloro-1-(2-fluorophenyl)-5-methoxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(2-methylphenyl)propanoic acid
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(3S)-3-(([4-fluoro-1-(2-fluorophenyl)-5-methoxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(2-methylphenyl)propanoic acid
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(3S)-3-(2,4-dichlorophenyl)-3-([[5-(3,3-dimethyl-2-oxobutoxy)-1-(2-fluorophenyl)-1H-pyrazol-3-yl]carbonyl]amino)propanoic acid
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(3S)-3-(2,4-dichlorophenyl)-3-[([1-(2-fluorophenyl)-5-[(2R)-2-hydroxy-3,3-dimethylbutoxy]-1H-pyrazol-3-yl]carbonyl)amino]propanoic acid
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(3S)-3-(2,4-dichlorophenyl)-3-[([1-(2-fluorophenyl)-5-[(2S)-2-hydroxy-3,3-dimethylbutoxy]-1H-pyrazol-3-yl]carbonyl)amino]propanoic acid
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(3S)-3-([(4-hydroxy-1-phenyl-1H-pyrazol-3-yl)carbonyl]amino)-3-(2-methylphenyl)propanoic acid
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(3S)-3-([(4-methoxy-1-phenyl-1H-pyrazol-3-yl)carbonyl]amino)-3-(2-methylphenyl)propanoic acid
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(3S)-3-([(5-hydroxy-1-phenyl-1H-pyrazol-3-yl)carbonyl]amino)-3-(2-methylphenyl)propanoic acid
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(3S)-3-([[5-(3,3-dimethyl-2-oxobutoxy)-1-(2-fluorophenyl)-1H-pyrazol-3-yl]carbonyl]amino)-3-(2-methylphenyl)propanoic acid
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(3S)-3-([[5-(cyclopropylmethoxy)-1-(2-fluorophenyl)-1H-pyrazol-3-yl]carbonyl]amino)-3-(2-methylphenyl)propanoic acid
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(3S)-3-([[5-ethoxy-1-(2-fluorophenyl)-1H-pyrazol-3-yl]carbonyl]amino)-3-(2-methylphenyl)propanoic acid
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(3S)-3-[([1-(2-fluorophenyl)-5-[(2S)-2-hydroxy-3,3-dimethylbutoxy]-1H-pyrazol-3-yl]carbonyl)amino]-3-(2-methylphenyl)propanoic acid
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(S)-1-chloro-4-phenyl-3-tosylamido-2-butanone
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37% residual activity at 1 mM
1,2-epoxy-3-(p-nitrophenoxy)propane
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1 mM, 14% inhibition, isoenzyme MpiCP-2
2,2'-dipyridyl
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1 mM, 21% inhibition, isoenzyme MpiCP-1; 1 mM, 22% inhibition, isoenzyme MpiCP-2
2-propanol
Citrus sp.
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above 5%
3,4-dichloroisocoumarin
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effective inhibitor
3-(([1-(2,5-dimethylphenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(4-fluorophenyl)propanoic acid
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3-(([1-(2-fluorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-phenylpropanoic acid
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3-(([1-(2-fluorophenyl)-5-methoxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(2-methylphenyl)propanoic acid
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3-(([1-(4-chlorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(2,5-dichlorophenyl)propanoic acid
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3-(2,3-dichlorophenyl)-3-(([1-(2,4-difluorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)propanoic acid
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3-(2,3-dichlorophenyl)-3-([(5-hydroxy-1-phenyl-1H-pyrazol-3-yl)carbonyl]amino)propanoic acid
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3-(4'-fluorobiphenyl-4-yl)-3-([[1-(2-fluorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl]amino)propanoic acid
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3-(5-fluoro-2-methylphenyl)-3-(([1-(2-fluorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)propanoic acid
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3-(biphenyl-4-yl)-3-([[1-(2,5-dimethylphenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl]amino)propanoic acid
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3-Phenyl-1-propanol
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inhibits hydrolysis of benzyloxycarbonyl-Phe-Leu, activates hydrolysis of benzyloxycarbonyl-Gly-Phe
3-[[(5-hydroxy-1-phenyl-1H-pyrazol-3-yl)carbonyl]amino]-3-(4-phenoxyphenyl)propanoic acid
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4-Aminobenzylsuccinic acid
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acetyl-D-Phe ethyl ester
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acetyl-D-Phe-ethyl ester
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benzyloxycarbonyl-D-Phe
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benzyloxycarbonyl-D-Phe-D-Leu
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benzyloxycarbonyl-Gly-Leu-Phe-CH2Cl
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benzyloxycarbonyl-L-phenylalanine chloromethyl ketone
benzyloxycarbonyl-L-phenylalanyl chloromethane
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diisopropylphosphorofluoridate-inactivated enzyme does not react with the inhibitor
benzyloxycarbonyl-Phe
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beta-phenyl-L-lactate
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Beta-phenylpropionate
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carboxypeptidase inhibitor IC
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carboxypeptidase Y inhibitor from baker's yeast
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MW 23400-24000, purification, chemical and physical properties
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carboxypeptidase Y inhibitor IC
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CoSO4
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62% residual activity at 10 mM
CuCl
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1 mM, 37% inhibition
CuCl2
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1 mM, 39% inhibition
CuSO4
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4% residual activity at 10 mM
D-Amino acids
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less inhibitory than the L-enantiomers, non-competitive or mixed-type
diisopropyl fluorophosphate
diisopropylfluorophosphate
E-64
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1 mM, 10% inhibition, isoenzyme MpiCP-2; 1 mM, 22% inhibition, isoenzyme MpiCP-1
Elastatinal
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1 mM, 46% inhibition, isoenzyme MpiCP-2
FeCl3
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1 mM, 92% inhibition
L-amino acids
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competitive
leupeptin
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1 mM, 24% inhibition, isoenzyme MpiCP-1; 1 mM, 60% inhibition, isoenzyme MpiCP-2
MnCl2
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1 mM, 14% inhibition
N-(N-[1-trans-3-carboxyoxiran-2-carbonyl]-L-leucyl)-agmatine
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93% residual activity at 1 mM
Nalpha-tosyl-L-Lys-chloromethyl ketone
Nalpha-tosyl-L-Phe-chloromethyl ketone
NEM
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1 mM, 71% inhibition
NH2-blocked amino acids
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p-chloromercuribenzenesulfonate
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p-chloromercuribenzoic acid
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complete inhibition at 1 mM, at 30°C and pH 3.1
p-hydroxymercuribenzene sulfonate
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mercurials inhibit the hydrolysis of the good substrate benzyloxycarbonyl-L-Phe-L-Leu, the inhibition is repressed by the competitive inhibitors benzyloxycarbonyl-D-Phe-D-Leu-Leu-Phe, trans-cinnamate and acetyl-D-Phe ethyl ester. Aromatic, methyl and ethyl mercurials do not cause complete inactivation with the poor substrates benzyloxycarbonyl-Gly-Phe and benzoyl-Gly-beta,L-phenyllactate. Propyl and butyl-mercurials enhance these activities
Pb(CH3COO)2
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60% residual activity at 10 mM
PbCl2
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1 mM, 95% inhibition
Phe-Asn-Arg-Ala-Val-Asp
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Phe-Asn-Arg-Ala-Val-Val
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Phe-Asn-Arg-Pro-Val-Asp
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Phe-Asn-Arg-Pro-Val-Val
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phenylmethane sulfonylfluoride
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phenylmethylsulfonyl fluoride
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irreversible
Phenylmethylsulfonylfluoride
phosphoramidon
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1 mM, 17% inhibition, isoenzyme MpiCP-1; 1 mM, 41% inhibition, isoenzyme MpiCP-2
SDS
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1 mM, complete inhibition
SnCl2
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1 mM, complete inhibition
Tfs1p
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NatB-dependent acetylation is essential for the inhibitory activity on carboxypeptidase Y
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tosylphenylalanylchloromethane
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1 mM, 35% inhibition, isoenzyme MpiCP-1
trans-epoxysuccinyl-L-leucylamido-(4-guanidine)-butane
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ZnSO4
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69% residual activity at 10 mM
2-mercaptoethanol
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1 mM, 13% inhibition, isoenzyme MpiCP-2
2-mercaptoethanol
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1 mM, 10% inhibition
benzyloxycarbonyl-L-phenylalanine chloromethyl ketone
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benzyloxycarbonyl-L-phenylalanine chloromethyl ketone
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irreversible inhibition of peptidase and esterase activity, inhibition is retarded by the competitive inhibitors benzyloxycarbonyl-D-phenylalanine-D-leucine and trans-cinnamate
benzyloxycarbonyl-L-phenylalanine chloromethyl ketone
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CaCl2
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1 mM, 16% inhibition
CaCl2
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73% residual activity at 10 mM
carboxypeptidase Y inhibitor IC
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carboxypeptidase Y inhibitor IC
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carboxypeptidase Y inhibitor IC
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chymostatin
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IC50 at pH 5.6: 0.092 mM, IC50 at pH 6.5: above 0.1 mM
chymostatin
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1 mM, 36% inhibition, isoenzyme MpiCP-1
chymostatin
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1 mM, 89% inhibition
chymostatin
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IC50 at pH 5.6 and at pH 6.5: above 0.1 mM
chymostatin
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5% residual activity at 1 mM
chymostatin
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IC50 at pH 5.6: 0.013 mM, IC50 at pH 6.5: 0.0022 mM
Cu+
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partial
diisopropyl fluorophosphate
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diisopropyl fluorophosphate
Citrus sp.
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peel enzyme inhibited, leaf enzyme not
diisopropyl fluorophosphate
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diisopropyl fluorophosphate
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effective inhibitor
diisopropyl fluorophosphate
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diisopropyl fluorophosphate
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benzyloxycarbonyl-L-phenylalanyl chloromethane-inhibited enzyme does not react with the inhibitor
diisopropyl fluorophosphate
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diisopropyl fluorophosphate
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diisopropylfluorophosphate
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1 mM, 39% inhibition, isoenzyme MpiCP-1; 1 mM, 67% inhibition, isoenzyme MpiCP-2
diisopropylfluorophosphate
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1 mM, 63% inhibition
diisopropylfluorophosphate
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complete inhibition at 5 mM, at 30°C and pH 3.1
ebelactone B
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IC50 at pH 5.6: 0.0016 mM, IC50 at pH 6.5: 0.002 mM
ebelactone B
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IC50 at pH 5.6: 0.00002 mM, IC50 at pH 6.5: 0.00003 mM
ebelactone B
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IC50: 0.0021 mM (at pH 5.6), IC50: 0.0015 mM (at pH 6.5)
EDTA
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1 mM, 38% inhibition, isoenzyme MpiCP-1
ethanol
Citrus sp.
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above 5%
HgCl2
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1 mM, 54% inhibition
HgCl2
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complete inhibition at 1 mM, at 30°C and pH 3.1
lactacystin
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IC50 at pH 5.6: 0.0052 mM, IC50 at pH 6.5: 0.0018 mM
lactacystin
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CatA is inhibited by 0.03 mM lactacystin
lactacystin
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IC50 at pH 5.6: 0.048 mM, IC50 at pH 6.5: 0.031 mM
lactacystin
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IC50 at pH 5.6: 0.0014 mM, IC50 at pH 6.5: 0.0043 mM
Monoiodoacetic acid
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1 mM, 14% inhibition; 1 mM, 25% inhibition
Monoiodoacetic acid
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complete inhibition at 1 mM, at 30°C and pH 3.1
Nalpha-tosyl-L-Lys-chloromethyl ketone
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1 mM, 13% inhibition, isoenzyme MpiCP-2
Nalpha-tosyl-L-Lys-chloromethyl ketone
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1 mM, 13% inhibition
Nalpha-tosyl-L-Phe-chloromethyl ketone
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1 mM, 12% inhibition, isoenzyme MpiCP-2
Nalpha-tosyl-L-Phe-chloromethyl ketone
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1 mM, 57% inhibition
omuralide
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might inhibit cathepsin A at the S1 subsite in the active-site cleft through direct binding to the active serine residue
omuralide
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IC50 at pH 5.6: 0.000099 mM, IC50 at pH 6.5: 0.000012 mM
omuralide
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IC50 at pH 5.6: 0.000096 mM, IC50 at pH 6.5: 0.000078 mM
omuralide
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IC50 at pH 5.6: 0.0000048 mM, IC50 at pH 6.5: 0.000002 mM
p-hydroxymercuribenzoate
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p-hydroxymercuribenzoate
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mercurials inhibit the hydrolysis of the good substrate benzyloxycarbonyl-L-Phe-L-Leu, the inhibition is repressed by the competitive inhibitors benzyloxycarbonyl-D-Phe-D-Leu-Leu-Phe, trans-cinnamate and acetyl-D-Phe ethyl ester. Aromatic, methyl and ethyl mercurials do not cause complete inactivation with the poor substrates benzyloxycarbonyl-Gly-Phe and benzoyl-Gly-beta,L-phenyllactate. Propyl and butyl-mercurials enhance these activities
PCMB
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1 mM, 28% inhibition, isoenzyme MpiCP-1; 1 mM, 97% inhibition, isoenzyme MpiCP-2
PCMB
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1 mM, 95% inhibition
pepstatin A
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1 mM, 11% inhibition, isoenzyme MpiCP-2; 1 mM, 19% inhibition, isoenzyme MpiCP-1
pepstatin A
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1 mM, 8% inhibition
Phenylmethylsulfonylfluoride
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1 mM, 61% inhibition, isoenzyme MpiCP-1; 1 mM, complete inhibition, isoenzyme MpiCP-2
Phenylmethylsulfonylfluoride
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1 mM, 72% inhibition
Phenylmethylsulfonylfluoride
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48% residual activity at 1 mM
piperastatin A
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IC50 at pH 5.6: 0.018 mM, IC50 at pH 6.5: 0.032 mM
piperastatin A
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1 mM, 17% inhibition, isoenzyme MpiCP-2; 1 mM, 87% inhibition, isoenzyme MpiCP-1
piperastatin A
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1 mM, 70% inhibition
piperastatin A
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IC50 at pH 5.6: 0.0041 mM, IC50 at pH 6.5: 0.0045 mM
piperastatin A
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IC50 at pH 5.6 and at pH 6.5: above 0.1 mM
poststatin
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IC50 at pH 5.6 and at pH 6.5: above 0.1 mM
poststatin
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IC50 at pH 5.6: 0.089 mM, IC50 at pH 6.5: 0.029 mM
poststatin
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IC50 at pH 5.6 and at pH 6.5: above 0.1 mM
additional information
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sublethal dose of sortin 1 cause reversible defects in vacuole biogenesis and root development. Treatment with sortin 1 results in carboxypeptidase Y secretion
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additional information
Citrus sp.
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not inhibition by EDTA
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additional information
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CathA inhibitor affects spermatophore wall digestion
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additional information
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not inhibited by trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane
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additional information
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no inhibition with 1 mM EDTA or chymostatin
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additional information
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20 mM 2-mercaptoethanol strongly inhibits the traffic of phaseolin, causing mainly accumulation in the endoplasmic reticulum or cis-Golgi cisternae, the inhibitory effect is more marked on the vacuolar sorting machinery
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additional information
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no inhibition by 1,10-phenanthroline; not inhibition by EDTA
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additional information
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in crude extract from baker's yeast carboxypeptidase Y is predominantly found in an inactive form
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additional information
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studies on the carboxypeptidase Y-inhibitor complex of yeast
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additional information
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not inhibited by ICh, a homolog of carboxypeptidase inhibitor IC
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