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(2R,3R)-(2-hydroxy-3-amino-4-phenyl-butanoic acid)-thiazolidide
(2R,3R)-3-amino-1-oxo-4-phenyl-1-(1,3-thiazolidin-3-yl)butan-2-ol
(2R,3R)-3-amino-2-hydroxy-4-phenylbutanoyl-L-Pro
(2R,3S)-(2-hydroxy-3-amino-4-phenyl-butanoic acid)-thiazolidide
(2R,3S)-3-amino-1-oxo-4-phenyl-1-(1,3-thiazolidin-3-yl)butan-2-ol
(2R,3S)-3-amino-2-hydroxy-4-phenylbutanoyl-L-Pro
(2S,3R)-(2-hydroxy-3-amino-4-phenyl-butanoic acid)-Pro-methyl ester
(2S,3R)-(2-hydroxy-3-amino-4-phenyl-butanoic acid)-Pro-Phe-methyl ester
(2S,3R)-(2-hydroxy-3-amino-4-phenyl-butanoic acid)-thiazolidide
(2S,3R)-(2-hydroxy-3-amino-5-methylhexanoic acid)-thiazolidide
(2S,3R)-2-hydroxy-3-amino-4-phenyl-butanoic acid pyrrolidide
(2S,3R)-3-amino-1-oxo-4-phenyl-1-(1,3-thiazolidin-3-yl)butan-2-ol
(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl pyrrolidide
(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl-L-Pro
(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl-L-Pro-L-Phe-OMe
(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl-L-Pro-OMe
(2S,3R)-3-amino-2-hydroxy-5-methylhexanoyl-thiazolidide
(2S,3R)-3-amino-5-methyl-1-oxo-1-(1,3-thiazolidin-3-yl)hexan-2-ol
(2S,3S)-(2-hydroxy-3-amino-4-phenyl-butanoic acid)-Pro-methyl ester
(2S,3S)-3-amino-2-hydroxy-4-phenylbutanoyl-L-Pro-OMe
2-hydroxy-3-aminoacyl-Pro-OH dipeptides
-
2-mercaptomethyl-3-guanidinoethylthiopropanoic acid
4-chloromercuriphenyl sulfonic acid
4-hydroxymercuribenzenesulfonate
-
-
acetyl-Phe(NO2)-Pro-Pro-HN-CH2-CH2-NH-2-aminobenzoyl
-
0.5 mM, 30% inhibition of hydrolysis of (4-nitr)Phe-Pro-Pro-HN-CH2-CH2-NH-o-aminobenzoyl
Arg-Pro
substrate inhibition at concentrations above 3 mM
cilazaprilat
-
inhibits hydrolysis of Gly-Pro-Hyp, Gly-Pro-4-methyl-7-coumarylamide, substance P, and beta-casomorphin. Weak inhibition of hydrolysis of Arg-Pro-Pro. No effect on hydrolysis of bradykinin
Cr6+
CrVI, a heavy metal endocrine-disrupting chemical industrially widely used, gestational exposure to CrVI increases germ cell/oocyte apoptosis and advance germ cell nest (GCN) breakdown. CrVI increases X-prolyl aminopeptidase (Xpnpep) 2 (a marker for premature ovarian failure in humans) during germ cell nest (GCN) breakdown, it decreases Xpnpep2 during postnatal follicle development, and increases colocalization of Xpnpep2 with collagens Col3 and Col4. Phenotype, overview
diethyldicarbonate
50% inhibition at 0.011 mM
diisopropylphosphofluoridate
-
-
enalapril
-
significant inhibition after repeated oral dosage
enalaprilat
-
inhibition only in presence of Mn2+
enaprilat
-
inhibits hydrolysis of Gly-Pro-Hyp, Gly-Pro-4-methylcoumarin 7-amide, substance P, and beta-casomorphin. Weak inhibition of hydrolysis of Arg-Pro-Pro. No effect on hydrolysis of bradykinin
Fe2+
slight activation at 0.05 mM, complete inhibition at 1 mM
glutathione
10% inhibition at 1 mM in absence of cations
hydrazine
inactivates wild-type hcAMPP and R535A mutant enzymes
L-Ala-(N-methyl)L-Ala-L-Ala
competitive
L-Ala-L-Ala-L-Ala
competitive
L-Ala-L-Pro-L-Ala
competitive; competitive, 50% inhibition at 0.22 mM
L-Pro-L-Leu
product inhibition, a third metal binding site is formed by two conserved His-residues and L-Pro-L-Leu
Leu-Pro
substrate inhibition at concentrations above 4 mM
N-benzyloxycarbonyl-Pro-prolinal
-
-
N-[1-(R,S)-carboxy-(2-phenylethyl)]-thiopropanoic acid
-
-
nitrilotriacetic acid
-
-
pepstatin A
complete inhibition at 0.1-5.0 mM
Peptides with N-terminal Pro
-
product inhibition
phenylmethylsulfonyl fluoride
Pro-HN-CH2-CH2-NH-2-aminobenzoyl
Ser-Pro
substrate inhibition at concentrations above 10 mM
(2R,3R)-(2-hydroxy-3-amino-4-phenyl-butanoic acid)-thiazolidide
-
-
(2R,3R)-(2-hydroxy-3-amino-4-phenyl-butanoic acid)-thiazolidide
-
-
(2R,3R)-3-amino-1-oxo-4-phenyl-1-(1,3-thiazolidin-3-yl)butan-2-ol
-
-
(2R,3R)-3-amino-1-oxo-4-phenyl-1-(1,3-thiazolidin-3-yl)butan-2-ol
-
-
(2R,3R)-3-amino-2-hydroxy-4-phenylbutanoyl-L-Pro
-
-
(2R,3R)-3-amino-2-hydroxy-4-phenylbutanoyl-L-Pro
-
-
(2R,3S)-(2-hydroxy-3-amino-4-phenyl-butanoic acid)-thiazolidide
-
-
(2R,3S)-(2-hydroxy-3-amino-4-phenyl-butanoic acid)-thiazolidide
-
-
(2R,3S)-3-amino-1-oxo-4-phenyl-1-(1,3-thiazolidin-3-yl)butan-2-ol
-
-
(2R,3S)-3-amino-1-oxo-4-phenyl-1-(1,3-thiazolidin-3-yl)butan-2-ol
-
-
(2R,3S)-3-amino-2-hydroxy-4-phenylbutanoyl-L-Pro
-
-
(2R,3S)-3-amino-2-hydroxy-4-phenylbutanoyl-L-Pro
-
-
(2S,3R)-(2-hydroxy-3-amino-4-phenyl-butanoic acid)-Pro-methyl ester
-
-
(2S,3R)-(2-hydroxy-3-amino-4-phenyl-butanoic acid)-Pro-methyl ester
-
-
(2S,3R)-(2-hydroxy-3-amino-4-phenyl-butanoic acid)-Pro-Phe-methyl ester
-
-
(2S,3R)-(2-hydroxy-3-amino-4-phenyl-butanoic acid)-Pro-Phe-methyl ester
-
-
(2S,3R)-(2-hydroxy-3-amino-4-phenyl-butanoic acid)-thiazolidide
-
-
(2S,3R)-(2-hydroxy-3-amino-4-phenyl-butanoic acid)-thiazolidide
-
-
(2S,3R)-(2-hydroxy-3-amino-5-methylhexanoic acid)-thiazolidide
-
-
(2S,3R)-(2-hydroxy-3-amino-5-methylhexanoic acid)-thiazolidide
-
-
(2S,3R)-2-hydroxy-3-amino-4-phenyl-butanoic acid pyrrolidide
-
-
(2S,3R)-2-hydroxy-3-amino-4-phenyl-butanoic acid pyrrolidide
-
-
(2S,3R)-3-amino-1-oxo-4-phenyl-1-(1,3-thiazolidin-3-yl)butan-2-ol
-
-
(2S,3R)-3-amino-1-oxo-4-phenyl-1-(1,3-thiazolidin-3-yl)butan-2-ol
-
-
(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl pyrrolidide
-
-
(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl pyrrolidide
-
-
(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl-L-Pro
-
-
(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl-L-Pro
-
-
(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl-L-Pro-L-Phe-OMe
-
-
(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl-L-Pro-L-Phe-OMe
-
-
(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl-L-Pro-OMe
-
-
(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl-L-Pro-OMe
-
-
(2S,3R)-3-amino-2-hydroxy-5-methylhexanoyl-thiazolidide
-
-
(2S,3R)-3-amino-2-hydroxy-5-methylhexanoyl-thiazolidide
-
-
(2S,3R)-3-amino-5-methyl-1-oxo-1-(1,3-thiazolidin-3-yl)hexan-2-ol
-
-
(2S,3R)-3-amino-5-methyl-1-oxo-1-(1,3-thiazolidin-3-yl)hexan-2-ol
-
-
(2S,3S)-(2-hydroxy-3-amino-4-phenyl-butanoic acid)-Pro-methyl ester
-
-
(2S,3S)-(2-hydroxy-3-amino-4-phenyl-butanoic acid)-Pro-methyl ester
-
-
(2S,3S)-3-amino-2-hydroxy-4-phenylbutanoyl-L-Pro-OMe
-
-
(2S,3S)-3-amino-2-hydroxy-4-phenylbutanoyl-L-Pro-OMe
-
-
1,10-phenanthroline
-
-
1,10-phenanthroline
complete inhibition at 0.1 mM
1,10-phenanthroline
-
50% inhibition at 0.01 mM
1,10-phenanthroline
50% inhibition at 0.036 mM
1,10-phenanthroline
complete inhibition at 5.0 mM
2-hydroxy-3-aminoacyl-Pro-OH dipeptides
-
slow-binding inhibitors
-
2-hydroxy-3-aminoacyl-Pro-OH dipeptides
-
slow-binding inhibitors
-
2-mercaptoethanol
-
2-mercaptoethanol
50% inhibition at 0.043 mM
2-mercaptomethyl-3-guanidinoethylthiopropanoic acid
-
-
2-mercaptomethyl-3-guanidinoethylthiopropanoic acid
-
-
4-chloromercuriphenyl sulfonic acid
-
inhibits cleavage of Arg-Pro-Pro
4-chloromercuriphenyl sulfonic acid
-
-
4-chloromercuriphenyl sulfonic acid
-
-
4-chloromercuriphenyl sulfonic acid
-
inhibits hydrolysis of Gly-Pro-Hyp, activates hydrolysis of bradykinin
4-hydroxymercuribenzoate
-
partial
4-hydroxymercuribenzoate
-
-
4-hydroxymercuribenzoate
-
-
amastatin
-
-
Aprotinin
-
slight
apstatin
-
-
apstatin
92% inhibition at 0.01 mM, enzyme binding structure modeling, molecular interactions between APP-1 and the ligand, overview. Comparison between Caenorhabditis elegans APP-1-apstatin structure and Escherichia coli APP-1-apstatin structure
apstatin
-
binds to the active site with its N-terminal amino group coordinated to one of the two Mn(II) ions at the metal center
apstatin
complete inhibition at 0.1 mM
apstatin
-
specific inhibitor, in vivo
apstatin
-
50% inhibition at 0.0023 mM
apstatin
-
a APP inhibitor
apstatin
-
selective for aminopeptidase P
Ba2+
-
-
Ba2+
slight inhibition at 1-5 mM
bestatin
-
-
bestatin
50% inhibition at 0.1 mM
bradykinin
-
-
bradykinin
-
hydrolysis of Gly-Pro-Hyp
Ca2+
-
only inhibits Mn2+-activated enzyme
Ca2+
activates the enzyme at concentrations of 0.01-0.1 mM with substrate substance P, inhibits above 1 mM
Ca2+
83.1% inhibition at 1 mM
Ca2+
-
1 mM CaCl2, 27% inhibition
Ca2+
stimulation of enzyme activity at 0.4 mM, inhibition at 4 mM
Ca2+
slight inhibition at 1-5 mM
captopril
-
-
Cd2+
-
-
Cd2+
complete inhibition at 0.01-5.0 mM
Co2+
strong activation at 0.01-1.0 mM, inhibitory at 10 mM
Co2+
-
only inhibits Mn2+-activated enzyme
Co2+
-
stimulatory at 0.01 mM, inhibitory above 0.1 mM
Co2+
activates the enzyme at concentrations of 0.01-0.1 mM with substrate substance P, inhibits above 1 mM
Co2+
-
1.5 mM CoCl2, complete inhibition
Co2+
-
1 mM CoCl2, 90% inhibition
Co2+
stimulation of enzyme activity at 0.4 mM, inhibition at 4 mM
Cu2+
-
-
Cu2+
56% inhibition at 0.1 mM
Cu2+
complete inhibition at 1 mM
Cu2+
-
inhibitory effect at 1 mM
Cu2+
complete inhibition at 4 mM
Cu2+
-
0.04-4.0 mM 4CuCl2
dithiothreitol
-
DTT
-
EDTA
10 mM EDTA inhibits enzyme activity to 0.26 times of the control level
EDTA
80% inhibition at 0.1 mM
EDTA
-
reactivation by Mn2+, Co2+, Cd2+, or Ni2+
EDTA
-
0.1-1 mM, completely
EDTA
49% inhibition at 1 mM
EDTA
-
the activity of the enzyme drops to 10% after treatment with 50 mM EDTA
EDTA
50% inhibition at 0.34 m
EDTA
90% inhibition at 0.1 mM
EGTA
-
-
Hg2+
-
-
Mg2+
activates the enzyme at concentrations of 0.01-0.1 mM with substrate substance P, inhibits above 1 mM
Mg2+
38.2% inhibition at 1 mM
Mg2+
slight inhibition at 1-5 mM
Mn2+
-
-
Mn2+
activates the enzyme at concentrations of 0.01-0.1 mM with substrate substance P, inhibits above 1 mM with substrates substance P and bradykinin
Mn2+
activates at up to 5 mM, a trimetal manganese cluster is observed at the active site involving residues Asp260, Asp271, Glu384, Glu408, and His354, elucidating the binding structure and mechanism of inhibition by metal ions. Inhibitory at 8-15 mM. There is a Mn2+ ion concentration-dependent activity regulation pattern
Mn2+
-
above, 0.01 mM, hydrolysis of bradykinin and Arg-Pro-Pro
NaCl
-
above 0.25 M
NaCl
activates the wild-type enzyme at 160 mM, inhibits the enzyme mutant R353A at 160 mM
NaCl
-
2 M, complete inhibition
NEM
-
-
NEM
50% inhibition at 0.079 mM
Ni2+
-
Ni2+
complete inhibition at 0.001 mM
Ni2+
93.5% inhibition at 1 mM
Ni2+
-
inhibitory effect at 1 mM
Pb2+
-
-
PCMB
-
inhibits cleavage of Arg-Pro-Pro
phenylmethylsulfonyl fluoride
-
-
phenylmethylsulfonyl fluoride
-
-
phenylmethylsulfonyl fluoride
-
-
PMSF
-
-
PMSF
60% inhibition at 5.0 mM
Pro-HN-CH2-CH2-NH-2-aminobenzoyl
-
-
Pro-HN-CH2-CH2-NH-2-aminobenzoyl
-
0.01 mM, complete inhibition of hydrolysis of (4-nitro)Phe-Pro-Pro-HN-CH2-CH2-NH-2-aminobenzoyl
Pro-HN-CH2-CH2-NH-2-aminobenzoyl
-
-
ramiprilat
-
inhibition only in presence of Mn2+
ramiprilat
-
inhibits hydrolysis of Gly-Pro-Hyp, Gly-Pro-4-methylcoumarin 7-amide, substance P or beta-casomorphin. Weak inhibition of hydrolysis of Arg-Pro-Pro. No effect on hydrolysis of bradykinin
Zn2+
complete inhibition at 1 mM
Zn2+
complete inhibition at 0.001 mM
Zn2+
complete inhibition at 0.1 mM
Zn2+
-
inhibitory effect at 1 mM
Zn2+
the Zn2+ ion has high affinity for APPro and inhibits the hydrolysis reaction by occupying a third metal binding site
Zn2+
-
10 mM, complete inhibition
Zn2+
-
1 mM ZnSO4, 96% inhibition
Zn2+
complete inhibition at 4 mM
Zn2+
complete inhibition at 0.01-5.0 mM
additional information
no inhibition by 4-(2-aminoethyl)benzensulfonylfluoride, tosyl lysyl chloromethyl ketone, and tosyl phenylalanyl chloromethyl ketone
-
additional information
-
no inhibition by 4-(2-aminoethyl)benzensulfonylfluoride, tosyl lysyl chloromethyl ketone, and tosyl phenylalanyl chloromethyl ketone
-
additional information
not inhibitory: L-Ala-(N-methyl)-L-Ala-L-Ala, L-Ala-L-Ala-L-Ala
-
additional information
-
not inhibitory: L-Ala-(N-methyl)-L-Ala-L-Ala, L-Ala-L-Ala-L-Ala
-
additional information
no significant inhibition by amastatin and enalaprilat
-
additional information
-
no significant inhibition by amastatin and enalaprilat
-
additional information
-
not inhibitory: bestatin, phosphoamidon
-
additional information
-
more intense processing conditions, above 100-200 MPa and 20-30°C, lead to enzyme inactivation with PepX HP-induced conformational changes, investigated by circular dichroism spectroscopy, kinetic analysis, overview
-