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(7-methoxycoumarin-2-acetic acid)-Ala-Ser-Asp-Lys-(N3-(2,4-dinitrophenyl)-L-2,3-diaminopropyl) + H2O
?
-
-
-
?
(7-methoxycoumarin-2-acetic acid)-Ser-Asp-Lys-(N3-(2,4-dinitrophenyl)-L-2,3-diaminopropyl) + H2O
?
-
-
-
?
(7-methoxycoumarin-2-acetyl)-Tyr-Val-Ala-Asp-Ala-Phe-Lys-(2,4-dinitrophenyl)-OH + H2O
?
-
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Ala-Ser-Asp-Lys-N3-(2,4-dinitrophenyl)-L-diaminopropionionate + H2O
?
-
-
-
-
?
1-dimethylaminonaphthalene-5-sulfonyl-Gly-Gly-Gly + H2O
1-dimethylaminonaphthalene-5-sulfonyl-Gly + Gly-Gly
-
-
-
-
?
2-aminobenzoyl-Ala-Ala-Leu-Ala-Gly-nitrobenzylamide + H2O
?
-
-
-
-
?
2-aminobenzoyl-Ala-Ala-Tyr-Leu-Ala-Gly-nitrobenzylamide + H2O
?
-
-
-
-
?
2-aminobenzoyl-Ala-Tyr-Leu-Ala-Gly-nitrobenzylamide + H2O
?
-
-
-
-
?
2-aminobenzoyl-L-Phe-L-Arg-L-Lys-2,4-dinitrophenyl-L-Pro + H2O
?
-
-
-
-
?
2-aminobenzoyl-Val-Tyr-Leu-Ala-Gly-nitrobenzylamide + H2O
?
-
-
-
-
?
2-furanacryloyl-1-Phe-Gly-Gly + H2O
?
-
-
-
-
?
2-furanacryloyl-Phe-Gly-Gly + H2O
2-furanacryloyl-Phe + Gly-Gly
2-furylacryloyl-Phe-Gly-Gly + H2O
2-furylacrylic acid + Phe-Gly-Gly
-
-
-
?
3-hydroxybutyryl-Gly-Gly-Gly + H2O
3-hydroxybutyryl-Gly + Gly-Gly
-
-
-
-
?
3-hydroxybutyrylglycyl-glycyl-glycine + H2O
3-hydroxybutyrylglycine + Gly-Gly
7-amido-4-carboxymethylcoumarin-YVADAPK(Dnp)-OH + H2O
dinitrophenol + 7-amino-4-carbamoylmethylcoumarin-YVADAPK
-
-
-
-
?
Abz-FRK(Dnp)P-OH + H2O
Abz-FR + K(Dnp)P
-
-
-
-
?
Abz-LFK(Dnp)-OH + H2O
Abz-Leu + Phe-Lys(Dnp)-OH
-
-
-
-
?
Abz-LFK(Dnp)-OH + H2O
Abz-Leu-Phe + N6-(2,4-dinitrophenyl)-L-lysine
-
-
-
-
?
Abz-SDK(Dnp)P-OH + H2O
Abz-Ser-Asp + Lys(Dnp)-Pro
-
-
-
-
?
Abz-YRK(2,4-dinitrophenyl)P + H2O
?
-
-
-
-
?
acetyl-His-Pro-(NO2)Phe-His-Leu + H2O
acetyl-His-Pro-(NO2)Phe + His-Leu
-
-
-
-
?
Ala-Ala-Ala-Ala + H2O
Ala-Ala + Ala-Ala
Ala-Ala-Ala-Pro + H2O
Ala-Ala-Ala + Pro
-
-
-
?
Ala-Phe-Ala + H2O
Ala-Phe + Ala
-
-
-
-
?
amyloid beta-peptide(1-40) + H2O
amyloid beta-peptide(1-7) + amyloid beta-peptide(8-40)
amyloid beta-protein 1-40 + H2O
amyloid beta-peptide(1-7) + amyloid beta-peptide(8-40)
-
ACE cleaves amyloid beta-protein 1-40 between Asp7 and Ser8
-
-
?
amyloid beta-protein 1-42 + H2O
amyloid beta-peptide(1-40) + amyloid beta-peptide(41-42)
-
ACE cleaves amyloid beta-protein 1-42 at multiple sites
-
-
?
amyloid beta-protein 1-42 + H2O
amyloid beta-protein 1-420 + ?
angiotensin (1-9) + H2O
?
-
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
angiotensin I + H2O
angiotensin II + L-His-L-Leu
angiotensin II + H2O
?
-
converts Ang II to Ang(1-7)
-
-
?
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met + H2O
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly + Leu-Met
-
-
-
-
?
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met-NH2 + H2O
?
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met-NH2 + H2O
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly + Leu-Met-NH2
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Tyr-Arg + H2O
?
Drosophila sp. (in: flies)
-
-
-
-
?
Arg-Pro-Pro-Gly-Phe-Thr-Pro-Phe-Arg + H2O
?
Drosophila sp. (in: flies)
-
-
-
-
?
Asn-Arg-Val-Tyr-Ile-His-Pro-(NO2)Phe-His-Leu + H2O
Asn-Arg-Val-Tyr-Ile-His-Pro-(NO2)Phe + His-Leu
-
-
-
-
?
benzoyl-Gly-Ala-His-Leu + H2O
benzoyl-Gly-Ala + His-Leu
-
-
-
-
?
benzoyl-Gly-Ala-Leu + H2O
benzoyl-Gly + Ala-Leu
-
-
-
-
?
benzoyl-Gly-Ala-Pro + H2O
benzoyl-Gly + Ala-Pro
benzoyl-Gly-Arg-His-Leu + H2O
benzoyl-Gly-Arg + His-Leu
-
-
-
-
?
benzoyl-Gly-Arg-Leu + H2O
benzoyl-Gly + Arg-Leu
-
-
-
-
?
benzoyl-Gly-Glu-Leu + H2O
benzoyl-Gly + Glu-Leu
-
-
-
-
?
benzoyl-Gly-Gly-Gly + H2O
benzoyl-Gly + Gly-Gly
benzoyl-Gly-His-Ala + H2O
benzoyl-Gly + His-Ala
-
-
-
-
?
benzoyl-Gly-His-Arg + H2O
benzoyl-Gly + His-Arg
-
-
-
-
?
benzoyl-Gly-His-Leu + H2O
benzoyl-Gly + His-Leu
benzoyl-Gly-His-Phe + H2O
benzoyl-Gly + His-Phe
-
-
-
-
?
benzoyl-Gly-Ile-His-Leu + H2O
benzoyl-Gly-Ile + His-Leu
-
-
-
-
?
benzoyl-Gly-Phe-Arg + H2O
benzoyl-Gly + Phe-Arg
benzoyl-Gly-Phe-His-Leu + H2O
benzoyl-Gly-Phe + His-Leu
-
-
-
-
?
benzoyl-Gly-Phe-Leu + H2O
benzoyl-Gly + Phe-Leu
-
-
-
-
?
benzoyl-Gly-Pro-His-Leu + H2O
benzoyl-Gly-Pro + His-Leu
-
-
-
-
?
benzoyl-Gly-Ser-His-Leu + H2O
benzoyl-Gly-Ser + His-Leu
-
-
-
-
?
benzyloxycarbonyl-(NO2)Phe-His-Leu + H2O
benzyloxycarbonyl-(NO2)Phe + His-Leu
benzyloxycarbonyl-Gly-Gly-Gly + H2O
benzyloxycarbonyl-Gly + Gly-Gly
-
-
-
-
?
benzyloxycarbonyl-Leu-Gly-Gly + H2O
benzyloxycarbonyl-Leu + Gly-Gly
-
-
-
-
?
benzyloxycarbonyl-Phe-His-Leu + H2O
?
benzyloxycarbonyl-Phe-His-Leu + H2O
benzyloxycarbonyl-Phe + His-Leu
benzyloxycarbonyl-Phe-Tyr-Leu
benzyloxycarbonyl-Phe + Tyr-Leu
-
-
-
-
?
beta-neoendorphin + H2O
?
-
-
-
-
?
bradykinin + H2O
Arg-Pro-Pro-Gly-Phe + Ser-Pro + Phe-Arg
Drosophila sp. (in: flies)
-
i.e. Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
-
-
?
bradykinin + H2O
L-Phe-L-Arg + L-Ser-L-Pro + L-Arg-L-Pro-L-Pro-Gly-L-Phe
-
-
-
-
?
bradykinin + H2O
Phe-Arg + Ser-Pro + Arg-Pro-Pro-Gly-Phe
cholecystokinin-8 + H2O
?
-
-
-
-
?
dansyltriglycine + H2O
?
-
-
-
-
?
dynorphin + H2O
?
-
-
-
-
?
furanacryloyl-L-Phe-Gly-Gly + H2O
furanacryloyl-L-Phe + Gly-Gly
Gly-Ala-Ala + H2O
Gly + Ala-Ala
-
-
-
?
Gly-Gly-Tyr-Arg + H2O
Gly-Gly + Tyr-Arg
-
-
-
?
Gly-His-Gly + H2O
Gly + His-Gly
-
-
-
?
Gly-Ile-His-Pro-(NO2)Phe-His-Leu + H2O
Gly-Ile-His-Pro-(NO2)Phe + His-Leu
-
-
-
-
?
Gly-Pro-(NO2)Phe-His-Leu + H2O
Gly-Pro-(NO2)Phe + His-Leu
-
-
-
-
?
gonadotropin-releasing hormone + H2O
?
a bridging interaction between Arg500 of the N-domain and Arg8 of gonadotropin-releasing hormone that involves a buried chloride ion may account for its role in the specificity of the N-domain for endoproteolytic cleavage of the substrate at the NH2-terminus in vitro
-
-
?
hippuryl-Gly-Gly + H2O
hippuric acid + Gly-Gly
hippuryl-Gly-His-Leu + H2O
hippuric acid + His-Leu
-
-
-
?
hippuryl-His-Leu + H2O
hippuric acid + His-Leu
hippuryl-histidyl-leucine + H2O
?
-
-
-
?
hippuryl-L-His-L-Leu + H2O
hippuric acid + L-His-L-Leu
hippuryl-Lys-Leu + H2O
hippuric acid + Lys-Leu
-
-
-
-
?
hippuryl-Phe-Arg + H2O
hippuric acid + Phe-Arg
His-Lys-Thr-Asp-Ser-Phe-Val-Gly-Leu-Met-NH2 + H2O
His-Lys-Thr-Asp-Ser-Phe-Val-Gly + Leu-Met-NH2
-
i.e. substance K, degraded by striatal but not by lung enzyme
-
-
?
His-Pro-(NO2)Phe-His-Leu + H2O
His-Pro-(NO2)Phe + His-Leu
-
-
-
-
?
Ile-Ser-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
?
Drosophila sp. (in: flies)
-
-
-
-
?
Leu5-enkephalin + H2O
Tyr-Gly-Gly + Phe-Leu
Luteinizing hormone-releasing hormone + H2O
?
-
degraded by striatal and by lung enzyme
-
-
?
LVVYPWTQRY + H2O
LVVYPWTQ + RY + LVVY + PW + LVVYPW + TQ
-
-
dipeptide TQ is unidentified. Sequential removal of dipeptides in three consecutive steps
?
MCA-Ala-Ser-Asp-Lys-Dap(DNP)-OH + H2O
?
Mca-APK-Dnp + H2O
?
-
-
-
-
?
Mca-RPPGFSAFK(Dnp)-OH + H2O
?
-
-
-
-
?
MCA-Tyr-Val-Ala-Asp-Ala-Pro-Lys(DNP)-OH + H2O
?
Met5-enkephalin + H2O
Tyr-Gly-Gly + Phe-Met
Met5-enkephalin-Arg6-Gly7-Leu8 + H2O
Tyr-Gly-Gly-Phe-met-Arg + Gly-Leu
-
-
-
-
?
MKRSRGPSPRR + H2O
?
Drosophila sp. (in: flies)
-
-
-
-
?
N-(1-(S)-carboxy-3-phenylpropyl)-L-Ala-L-Pro + H2O
?
-
i.e. MK-422
-
-
?
N-(1-(S)-carboxy-3-phenylpropyl)-L-Lys-L-Pro + H2O
?
-
i.e. MK-522
-
-
?
N-(3-(2-furyl)acryloyl)-L-Phe-Gly-Gly + H2O
2-furylacrylic acid + L-Phe-Gly-Gly
-
-
-
?
N-(3-(2-furyl)acryloyl)-L-Phe-Gly-Gly + H2O
N-(3-(2-furyl)acrylic acid) + Phe-Gly-Gly
-
-
-
?
N-(3-(2-furyl)acryloyl)-L-Phe-Phe-Arg + H2O
2-furylacrylic acid + L-Phe-Phe-Arg
-
-
-
?
N-(3-(2-furyl)acryloyl)-Phe-Ala-Ala + H2O
2-furylacrylic acid + Phe-Ala-Ala
-
-
-
?
N-(3-(2-furyl)acryloyl)-Phe-Ala-Gly + H2O
2-furylacrylic acid + Phe-Ala-Gly
-
-
-
?
N-(3-(2-furyl)acryloyl)-Phe-Ala-Lys + H2O
2-furylacrylic acid + Phe-Ala-Lys
-
-
-
?
N-(3-(2-furyl)acryloyl)-Phe-Ala-Pro + H2O
2-furylacrylic acid + Phe-Ala-Pro
-
-
-
?
N-(3-(2-furyl)acryloyl)-Phe-Gly-Gly + H2O
2-furylacrylic acid + Phe-Gly-Gly
-
-
-
?
N-(3-(2-furyl)acryloyl)-Phe-Phe-Arg + H2O
2-furylacrylic acid + Phe-Phe-Arg
-
-
-
?
N-(3-[2-furyl]acryloyl)-L-phenylalanylglycylglycine + H2O
?
-
-
-
?
N-acetyl-Ala-Ala-Ala + H2O
N-acetyl-Ala + Ala-Ala
-
-
-
?
N-benzyloxycarbonyl-L-Phe-L-His-L-Leu + H2O
N-benzyloxycarbonyl-L-Phe + L-His-L-Leu
N-benzyloxycarbonyl-Phe-His-Leu + H2O
N-benzyloxycarbonyl-Phe + His-Leu
-
-
-
?
N-hippuryl-His-Leu + H2O
hippuric acid + His-Leu
N-hippuryl-His-Leu + H2O
N-hippuric acid + His-Leu
-
-
-
-
?
N-[3-(2-furyl)acryloyl]-L-Phe-Gly-Gly + H2O
2-furylacrylic acid + L-Phe-Gly-Gly
-
-
-
-
?
N-[3-(2-furyl)acryloyl]-L-phenylalanyl-glycyl-glycine + H2O
?
-
-
-
-
?
N-[3-(2-furyl)acryloyl]-L-phenylalanyl-glycyl-glycine + H2O
N-[3-(2-furyl)acryloyl]-L-phenylalanine + glycyl-glycine
N-[3-(2-furyl)acryloyl]-L-phenylalanylglycylglycine + H2O
?
N-[3-(2-furyl)acryloyl]-Phe-Gly-Gly + H2O
N-[3-(2-furyl)acryloyl]-Phe + Gly-Gly
-
-
-
-
?
neurotensin + H2O
pGlu-Leu-Tyr-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Tyr + Ile-Leu
o-aminobenzoyl-FDK-(dinitrophenyl)-P-OH + H2O
o-aminobenzoyl-FD + K-(dinitrophenyl)-P-OH
-
-
-
?
o-aminobenzoyl-FRK-(dinitrophenyl)-P-OH + H2O
o-aminobenzoyl-FR + K-(dinitrophenyl)-P-OH
-
-
-
?
o-aminobenzoyl-GFSPFAQ-(N-2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoyl-GFSPFA + Gln-(N-2,4-dinitrophenyl)ethylenediamine
-
-
-
?
o-aminobenzoyl-GFSPFEQ-(N-2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoyl-GFSPFE + Gln-(N-2,4-dinitrophenyl)ethylenediamine
-
-
-
?
o-aminobenzoyl-GFSPFFQ-(N-2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoyl-GFSPFF + Gln-(N-2,4-dinitrophenyl)ethylenediamine
-
-
-
?
o-aminobenzoyl-GFSPFLQ-(N-2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoyl-GFSPFL + Gln-(N-2,4-dinitrophenyl)ethylenediamine
-
-
-
?
o-aminobenzoyl-GFSPFQQ-(N-2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoyl-GFSPFQ + Gln-(N-2,4-dinitrophenyl)ethylenediamine
-
-
-
?
o-aminobenzoyl-GFSPFRA-(N-2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoyl-GFSPFR + Ala-(N-2,4-dinitrophenyl)ethylenediamine
-
-
-
?
o-aminobenzoyl-GFSPFRF-(N-2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoyl-GFSPFR + Phe-(N-2,4-dinitrophenyl)ethylenediamine
-
-
-
?
o-aminobenzoyl-GFSPFRI-(N-2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoyl-GFSPFR + Ile-(N-2,4-dinitrophenyl)ethylenediamine
-
-
-
?
o-aminobenzoyl-GFSPFRN-(N-2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoyl-GFSPFR + Asn-(N-2,4-dinitrophenyl)ethylenediamine
-
-
-
?
o-aminobenzoyl-GFSPFRQ-(N-2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoyl-GFSPFR + Gln-(N-2,4-dinitrophenyl)ethylenediamine
-
-
-
?
o-aminobenzoyl-GFSPFRR-(N-2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoyl-GFSPFR + Arg-(N-2,4-dinitrophenyl)ethylenediamine
-
-
-
?
o-aminobenzoyl-GFSPFRS-(N-2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoyl-GFSPFR + Ser-(N-2,4-dinitrophenyl)ethylenediamine
-
-
-
?
o-aminobenzoyl-GFSPFSQ-(N-2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoyl-GFSPFS + Gln-(N-2,4-dinitrophenyl)ethylenediamine
-
-
-
?
o-aminobenzoyl-Phe-Arg-Lys(2,4-dinitrophenyl)-Pro-hydroxide + H2O
?
-
-
-
?
o-aminobenzoyl-SDK-(dinitrophenyl)-P-OH + H2O
o-aminobenzoyl-SD + K-(dinitrophenyl)-P-OH
-
-
-
?
o-aminobenzoyl-SRK-(dinitrophenyl)-P-OH + H2O
o-aminobenzoyl-SR + K-(dinitrophenyl)-P-OH
-
-
-
?
o-aminobenzoyl-TDK-(dinitrophenyl)-P-OH + H2O
o-aminobenzoyl-TD + K-(dinitrophenyl)-P-OH
-
-
-
?
o-aminobenzoyl-TRK-(dinitrophenyl)-P-OH + H2O
o-aminobenzoyl-TR + K-(dinitrophenyl)-P-OH
-
-
-
?
o-aminobenzoyl-YDK-(dinitrophenyl)-P-OH + H2O
o-aminobenzoyl-YD + K-(dinitrophenyl)-P-OH
-
-
-
?
o-aminobenzoyl-YRK-(dinitrophenyl)-P-OH + H2O
o-aminobenzoyl-YR + K-(dinitrophenyl)-P-OH
-
-
-
?
p-hydroxyhippuryl-His-Leu + H2O
?
-
-
-
?
p-nitrobenzyloxycarbonyl-Gly + H2O
?
-
-
-
-
?
p-nitrobenzyloxycarbonyl-Gly-Gly-Gly + H2O
?
-
-
-
-
?
Phe-Gly-Gly-Phe + H2O
Phe-Gly + Gly-Phe
-
-
-
?
physalaemin + H2O
pGlu-Ala-Asp-Pro-Asn-Lys-Phe-Tyr-Gly + Leu-Met-NH2
-
degraded by striatal and by lung enzyme
-
-
?
Pro-(NO2)Phe-His-Leu + H2O
Pro-(NO2)Phe + His-Leu
-
-
-
-
?
Substance P + H2O
?
-
-
-
-
?
tert-butoxycarbonyl-Phe-Ala-Pro + H2O
tert-butoxycarbonyl-Phe + Ala-Pro
-
-
-
-
?
tert-butoxycarbonyl-Phe-Phe-Gly + H2O
tert-butoxycarbonyl-Phe + Phe-Gly
-
-
-
-
?
TOAC1-angiotensin I + H2O
?
-
-
-
-
?
TOAC3-angiotensin I + H2O
?
-
-
-
-
?
Tyr-Gly-Gly + H2O
Tyr + Gly-Gly
-
-
-
-
?
Tyr-Gly-Gly-Phe-Leu + H2O
Tyr-Gly-Gly + Phe-Leu
-
-
-
?
Tyr-Gly-Gly-Phe-Met + H2O
Tyr-Gly-Gly + Phe-Met
-
-
-
?
Tyr-Gly-Gly-Phe-Met-Arg-Gly-Leu + H2O
Tyr-Gly-Gly-Phe-Met-Arg + Gly-Leu
-
-
-
-
?
Tyr-Ile-His-Pro-(NO2)Phe-His-Leu + H2O
Tyr-Ile-His-Pro-(NO2)Phe + His-Leu
-
-
-
-
?
Z-Phe-His-Leu + H2O
Z-Phe + His-Leu
-
-
-
?
Z-phenylalanyl-histidyl-leucine + H2O
Z-phenylalanine + histidyl-leucine
-
-
-
?
[Arg10]angiotensin I + H2O
?
-
-
-
-
?
[D-Ala2,Leu5]enkephalin + H2O
Tyr-D-Ala-Gly + Phe-Leu
-
-
-
-
?
[Leu5]enkephalin + H2O
?
Drosophila sp. (in: flies)
-
-
-
-
?
[Leu5]enkephalinamide + H2O
?
Drosophila sp. (in: flies)
-
-
-
-
?
[Met5]enkephalin + H2O
?
Drosophila sp. (in: flies)
-
-
-
-
?
[Met5]enkephalinamide + H2O
?
Drosophila sp. (in: flies)
-
-
-
-
?
[Phe9,Arg10]angiotensin I + H2O
?
-
-
-
-
?
[Phe9]angiotensin I + H2O
?
-
-
-
-
?
additional information
?
-
2-furanacryloyl-Phe-Gly-Gly + H2O
2-furanacryloyl-Phe + Gly-Gly
-
-
-
-
?
2-furanacryloyl-Phe-Gly-Gly + H2O
2-furanacryloyl-Phe + Gly-Gly
-
-
-
-
?
2-furanacryloyl-Phe-Gly-Gly + H2O
2-furanacryloyl-Phe + Gly-Gly
-
3-(2-furanacryloyl)-Phe-Gly-Gly
-
-
?
2-furanacryloyl-Phe-Gly-Gly + H2O
2-furanacryloyl-Phe + Gly-Gly
-
-
-
-
?
3-hydroxybutyrylglycyl-glycyl-glycine + H2O
3-hydroxybutyrylglycine + Gly-Gly
-
-
-
-
?
3-hydroxybutyrylglycyl-glycyl-glycine + H2O
3-hydroxybutyrylglycine + Gly-Gly
-
synthetic substrate for use in an spectrophotometric assay of ACE inhibitory activity, method development involving automation of the measurement with immobilized aminoacylase and 3-hydroxybutyrate dehydrogenase, optimization, detailed overview. Application to the screening of ACE inhibitors
-
-
?
Ala-Ala-Ala-Ala + H2O
Ala-Ala + Ala-Ala
-
-
-
-
?
Ala-Ala-Ala-Ala + H2O
Ala-Ala + Ala-Ala
-
-
-
?
Ala-Ala-Ala-Ala + H2O
Ala-Ala + Ala-Ala
-
-
-
?
amyloid beta-peptide(1-40) + H2O
amyloid beta-peptide(1-7) + amyloid beta-peptide(8-40)
-
cleavage at the Asp7-Ser9 bond
-
?
amyloid beta-peptide(1-40) + H2O
amyloid beta-peptide(1-7) + amyloid beta-peptide(8-40)
-
cleavage at the Asp7-Ser9 bond. Compared with amyloid beta-peptide(1-40), aggregation and cytotoxic effects of the degradation products amyloid beta-peptide(1-7) and amyloid beta-peptide(8-40) are reduced ot virtually absent. The enzyme inhibits aggregation, deposition, and cytotoxicity of amyloid beta-peptide in vitro may affect susceptibility to Alzheimers disease
-
?
amyloid beta-protein 1-42 + H2O
amyloid beta-protein 1-420 + ?
-
angiotensin-converting enzyme converts amyloid beta-protein 1-42 to amyloid beta-protein1-40. ACE regulates Abeta1-42/Abeta1-40 ratio in vivo by converting secreted Abeta1-42 to Abeta1-40 and degrading Abetas.The upregulation of ACE activity can be a novel therapeutic strategy for Alzheimers disease
-
-
?
amyloid beta-protein 1-42 + H2O
amyloid beta-protein 1-420 + ?
-
angiotensin-converting enzyme converts amyloid beta-protein1-42 to amyloid beta-protein1-40. ACE regulates Abeta1-42/Abeta1-40 ratio in vivo by converting secreted Abeta1-42 to Abeta1-40 and degrading Abetas. The upregulation of ACE activity can be a novel therapeutic strategy for Alzheimers disease
-
-
?
angiotensin I + H2O
?
-
-
-
-
?
angiotensin I + H2O
?
-
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
-
the enzyme plays an important role in blood pressure homeostasis
-
?
angiotensin I + H2O
angiotensin II + His-Leu
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
-
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
-
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
Drosophila sp. (in: flies)
-
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
-
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
-
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
-
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
-
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
-
i.e. DRVYIHPFHL
i.e. DRVYIHPF
-
?
angiotensin I + H2O
angiotensin II + His-Leu
-
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
-
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
-
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
-
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
-
about 5% of the activity with hippury-Lys-Leu
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
-
the effect on angiotensin I containing the paramagnetic 2,2,6,6-tetramethylpiperidine-1-oxyl-4-amino-4-carboxylic acid (TOAC) at positions 1, 3, 8, and 9 is studied. TOAC1-Ang I and TOAC3-Ang I are cleaved by ACE. TOAC8-Ang I and TOAC9-Ang I are not cleaved
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
-
angiotensin II is a vasoconstrictor that raises blood pressure and is formed from angiotensin I by the angiotensin I converting enzyme in the reninangiotensin system
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
-
i.e. DRVYIHPFHL
i.e. DRVYIHPF
-
?
angiotensin I + H2O
angiotensin II + His-Leu
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
-
i.e. DRVYIHPFHL
i.e. DRVYIHPF
-
?
angiotensin I + H2O
angiotensin II + His-Leu
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
-
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
-
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
-
enzyme plays a major role in blood pressure regulation
-
?
angiotensin I + H2O
angiotensin II + His-Leu
-
-
-
-
?
angiotensin I + H2O
angiotensin II + L-His-L-Leu
-
-
-
?
angiotensin I + H2O
angiotensin II + L-His-L-Leu
-
-
-
-
?
angiotensin I + H2O
angiotensin II + L-His-L-Leu
-
-
-
-
?
angiotensin I + H2O
angiotensin II + L-His-L-Leu
-
-
-
-
?
angiotensin I + H2O
angiotensin II + L-His-L-Leu
-
-
-
?
angiotensin I + H2O
angiotensin II + L-His-L-Leu
-
-
-
-
?
angiotensin I + H2O
angiotensin II + L-His-L-Leu
-
-
-
?
angiotensin I + H2O
angiotensin II + L-His-L-Leu
-
-
-
-
?
angiotensin I + H2O
angiotensin II + L-His-L-Leu
-
-
-
?
angiotensin I + H2O
angiotensin II + L-His-L-Leu
-
-
695571, 695798, 697524, 698406, 698416, 698423, 698425, 698426, 698430, 700690, 701430 -
-
?
angiotensin I + H2O
angiotensin II + L-His-L-Leu
-
-
-
?
angiotensin I + H2O
angiotensin II + L-His-L-Leu
-
-
-
-
?
angiotensin I + H2O
angiotensin II + L-His-L-Leu
-
-
-
?
angiotensin I + H2O
angiotensin II + L-His-L-Leu
-
-
-
?
angiotensin I + H2O
angiotensin II + L-His-L-Leu
-
-
-
-
?
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met-NH2 + H2O
?
-
cleavage sites: Arg-Pro-/-Lys-Pro-/-Gln-Gln-/-Phe-Phe-/-Gly-Leu-Met-NH2
-
?
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met-NH2 + H2O
?
-
i.e. substance P, lung and brain ACE cleave substance P via two pathways. In one pathway ACE first releases Gly-Leu-Met-NH2 and then dipeptides sequentially from the carboxyl terminus. The other first produces Leu-Met-NH2 and then releases dipeptides to leave substance P(1-5)
-
-
?
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met-NH2 + H2O
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly + Leu-Met-NH2
-
-
-
-
?
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met-NH2 + H2O
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly + Leu-Met-NH2
-
-
-
-
?
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met-NH2 + H2O
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly + Leu-Met-NH2
-
i.e. substance P
-
?
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met-NH2 + H2O
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly + Leu-Met-NH2
-
lung and brain ACE cleave substance P via two pathways. In one pathway ACE first releases Gly-Leu-Met-NH2 and then dipeptides sequentially from the carboxyl terminus. The other first produces Leu-Met-NH2 and then releases dipeptides to leave substance P(1-5)
-
?
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met-NH2 + H2O
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly + Leu-Met-NH2
-
primary cleavage at the Phe8-Gly9 bond followed by succesive dipeptide cleavages from the newly formed C-terminus, cleavage of the Gly9-Leu10 bond is relatively minor
-
-
?
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met-NH2 + H2O
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly + Leu-Met-NH2
-
primary cleavage of Phe8-Gly9
-
-
?
benzoyl-Gly-Ala-Pro + H2O
benzoyl-Gly + Ala-Pro
-
-
-
?
benzoyl-Gly-Ala-Pro + H2O
benzoyl-Gly + Ala-Pro
-
-
-
-
?
benzoyl-Gly-Ala-Pro + H2O
benzoyl-Gly + Ala-Pro
-
-
-
?
benzoyl-Gly-Ala-Pro + H2O
benzoyl-Gly + Ala-Pro
-
-
-
-
?
benzoyl-Gly-Ala-Pro + H2O
benzoyl-Gly + Ala-Pro
-
-
-
-
?
benzoyl-Gly-Gly-Gly + H2O
benzoyl-Gly + Gly-Gly
-
-
-
-
?
benzoyl-Gly-Gly-Gly + H2O
benzoyl-Gly + Gly-Gly
-
-
-
-
?
benzoyl-Gly-His-Leu + H2O
benzoyl-Gly + His-Leu
-
-
-
?
benzoyl-Gly-His-Leu + H2O
benzoyl-Gly + His-Leu
-
-
-
-
?
benzoyl-Gly-His-Leu + H2O
benzoyl-Gly + His-Leu
-
-
-
?
benzoyl-Gly-His-Leu + H2O
benzoyl-Gly + His-Leu
-
-
-
-
?
benzoyl-Gly-His-Leu + H2O
benzoyl-Gly + His-Leu
-
-
-
-
?
benzoyl-Gly-His-Leu + H2O
benzoyl-Gly + His-Leu
-
-
-
-
?
benzoyl-Gly-His-Leu + H2O
benzoyl-Gly + His-Leu
-
-
-
-
?
benzoyl-Gly-His-Leu + H2O
benzoyl-Gly + His-Leu
-
-
-
-
?
benzoyl-Gly-Phe-Arg + H2O
benzoyl-Gly + Phe-Arg
-
-
-
-
?
benzoyl-Gly-Phe-Arg + H2O
benzoyl-Gly + Phe-Arg
-
-
-
-
?
benzyloxycarbonyl-(NO2)Phe-His-Leu + H2O
benzyloxycarbonyl-(NO2)Phe + His-Leu
-
-
-
-
?
benzyloxycarbonyl-(NO2)Phe-His-Leu + H2O
benzyloxycarbonyl-(NO2)Phe + His-Leu
-
-
-
-
?
benzyloxycarbonyl-Phe-His-Leu + H2O
?
-
-
-
?
benzyloxycarbonyl-Phe-His-Leu + H2O
?
-
-
-
?
benzyloxycarbonyl-Phe-His-Leu + H2O
?
-
-
-
?
benzyloxycarbonyl-Phe-His-Leu + H2O
benzyloxycarbonyl-Phe + His-Leu
-
-
-
-
?
benzyloxycarbonyl-Phe-His-Leu + H2O
benzyloxycarbonyl-Phe + His-Leu
-
-
-
-
?
benzyloxycarbonyl-Phe-His-Leu + H2O
benzyloxycarbonyl-Phe + His-Leu
-
-
-
?
bradykinin + H2O
?
-
-
-
?
bradykinin + H2O
?
-
-
-
-
?
bradykinin + H2O
?
-
degradation
-
-
?
bradykinin + H2O
?
-
-
-
-
?
bradykinin + H2O
?
-
inactivation
-
-
?
bradykinin + H2O
?
-
-
-
-
?
bradykinin + H2O
?
-
bradykinin is a nonapeptide released from high molecular weight kininogen, it exerts its vasodilatory effect mainly by stimulation of B2 receptors
-
-
?
bradykinin + H2O
?
-
-
-
-
?
bradykinin + H2O
Phe-Arg + Ser-Pro + Arg-Pro-Pro-Gly-Phe
-
-
-
?
bradykinin + H2O
Phe-Arg + Ser-Pro + Arg-Pro-Pro-Gly-Phe
-
-
Arg-Pro-Pro + Gly-Phe + Ser-Pro + Phe-Arg
?
bradykinin + H2O
Phe-Arg + Ser-Pro + Arg-Pro-Pro-Gly-Phe
-
-
Arg-Pro-Pro + Gly-Phe + Ser-Pro + Phe-Arg
?
bradykinin + H2O
Phe-Arg + Ser-Pro + Arg-Pro-Pro-Gly-Phe
-
-
-
-
?
bradykinin + H2O
Phe-Arg + Ser-Pro + Arg-Pro-Pro-Gly-Phe
-
-
-
-
?
bradykinin + H2O
Phe-Arg + Ser-Pro + Arg-Pro-Pro-Gly-Phe
-
-
-
-
?
bradykinin + H2O
Phe-Arg + Ser-Pro + Arg-Pro-Pro-Gly-Phe
-
-
-
-
?
bradykinin + H2O
Phe-Arg + Ser-Pro + Arg-Pro-Pro-Gly-Phe
-
-
-
-
?
bradykinin + H2O
Phe-Arg + Ser-Pro + Arg-Pro-Pro-Gly-Phe
-
-
-
?
bradykinin + H2O
Phe-Arg + Ser-Pro + Arg-Pro-Pro-Gly-Phe
-
-
Phe-Arg + Ser-Pro -Arg-Pro-Pro-Gly-Phe
?
bradykinin + H2O
Phe-Arg + Ser-Pro + Arg-Pro-Pro-Gly-Phe
-
about 3.5% of the activity with hippury-Lys-Leu
-
?
bradykinin + H2O
Phe-Arg + Ser-Pro + Arg-Pro-Pro-Gly-Phe
-
-
hydrolyzes Phe-Arg + Ser-Pro from the C-terminus of bradykinin
?
bradykinin + H2O
Phe-Arg + Ser-Pro + Arg-Pro-Pro-Gly-Phe
-
-
hydrolyzes Phe-Arg + Ser-Pro from the C-terminus of bradykinin
?
bradykinin + H2O
Phe-Arg + Ser-Pro + Arg-Pro-Pro-Gly-Phe
-
-
-
-
?
bradykinin + H2O
Phe-Arg + Ser-Pro + Arg-Pro-Pro-Gly-Phe
-
-
-
?
bradykinin + H2O
Phe-Arg + Ser-Pro + Arg-Pro-Pro-Gly-Phe
-
-
-
-
?
furanacryloyl-L-Phe-Gly-Gly + H2O
furanacryloyl-L-Phe + Gly-Gly
-
-
-
-
?
furanacryloyl-L-Phe-Gly-Gly + H2O
furanacryloyl-L-Phe + Gly-Gly
-
-
-
-
?
Hip-His-Leu + H2O
?
-
-
-
?
Hip-His-Leu + H2O
?
-
-
-
-
?
hippuryl-Gly-Gly + H2O
hippuric acid + Gly-Gly
-
-
-
-
?
hippuryl-Gly-Gly + H2O
hippuric acid + Gly-Gly
-
-
-
-
?
hippuryl-Gly-Gly + H2O
hippuric acid + Gly-Gly
-
-
-
-
?
hippuryl-His-Leu + H2O
hippuric acid + His-Leu
-
-
-
?
hippuryl-His-Leu + H2O
hippuric acid + His-Leu
-
-
-
-
?
hippuryl-His-Leu + H2O
hippuric acid + His-Leu
-
-
-
-
?
hippuryl-His-Leu + H2O
hippuric acid + His-Leu
-
-
-
-
?
hippuryl-His-Leu + H2O
hippuric acid + His-Leu
-
-
-
-
?
hippuryl-His-Leu + H2O
hippuric acid + His-Leu
-
-
-
?
hippuryl-His-Leu + H2O
hippuric acid + His-Leu
-
-
-
?
hippuryl-His-Leu + H2O
hippuric acid + His-Leu
-
-
-
-
?
hippuryl-His-Leu + H2O
hippuric acid + His-Leu
-
-
81211, 81212, 81225, 81231, 81234, 81236, 81238, 81239, 81240, 81241, 81242, 81245, 81246, 81247, 81248, 81277, 81282, 81288 -
-
?
hippuryl-His-Leu + H2O
hippuric acid + His-Leu
-
-
-
?
hippuryl-His-Leu + H2O
hippuric acid + His-Leu
-
-
-
-
?
hippuryl-His-Leu + H2O
hippuric acid + His-Leu
-
-
-
?
hippuryl-His-Leu + H2O
hippuric acid + His-Leu
-
colorimetric assay method
-
-
?
hippuryl-His-Leu + H2O
hippuric acid + His-Leu
-
-
-
?
hippuryl-His-Leu + H2O
hippuric acid + His-Leu
-
-
-
-
?
hippuryl-His-Leu + H2O
hippuric acid + His-Leu
-
-
-
-
?
hippuryl-His-Leu + H2O
hippuric acid + His-Leu
-
-
-
?
hippuryl-His-Leu + H2O
hippuric acid + His-Leu
-
-
668985, 669020, 669023, 669026, 669033, 678863, 680284, 680316, 680317, 681160, 681163, 681562, 682248, 707653, 707763, 707764, 708537, 708837, 708857, 710252 -
-
?
hippuryl-His-Leu + H2O
hippuric acid + His-Leu
-
-
-
-
?
hippuryl-His-Leu + H2O
hippuric acid + His-Leu
-
-
81211, 81219, 81220, 81241, 81244, 81252, 81254, 81283, 667885, 680293, 681562, 707783, 710160, 731569, 732968 -
-
?
hippuryl-His-Leu + H2O
hippuric acid + His-Leu
-
-
-
?
hippuryl-His-Leu + H2O
hippuric acid + His-Leu
-
-
-
-
?
hippuryl-His-Leu + H2O
hippuric acid + His-Leu
-
colorimetric assay method
-
-
?
hippuryl-His-Leu + H2O
hippuric acid + His-Leu
-
colorimetric quantification of released hippuric acid, using pyridine and benzene sulfonyl chloride, assay method evaluation, overview
-
-
?
hippuryl-His-Leu + H2O
hippuric acid + His-Leu
-
-
-
-
?
hippuryl-L-His-L-Leu + H2O
hippuric acid + L-His-L-Leu
-
-
-
-
?
hippuryl-L-His-L-Leu + H2O
hippuric acid + L-His-L-Leu
-
-
-
-
?
hippuryl-L-His-L-Leu + H2O
hippuric acid + L-His-L-Leu
-
-
-
?
hippuryl-L-His-L-Leu + H2O
hippuric acid + L-His-L-Leu
-
-
-
-
?
hippuryl-L-His-L-Leu + H2O
hippuric acid + L-His-L-Leu
-
-
-
-
?
hippuryl-L-His-L-Leu + H2O
hippuric acid + L-His-L-Leu
-
-
-
-
?
hippuryl-Phe-Arg + H2O
hippuric acid + Phe-Arg
-
-
-
-
?
hippuryl-Phe-Arg + H2O
hippuric acid + Phe-Arg
-
-
-
-
?
LEQIYHL + H2O
?
-
-
-
?
Leu5-enkephalin + H2O
Tyr-Gly-Gly + Phe-Leu
-
-
-
-
?
Leu5-enkephalin + H2O
Tyr-Gly-Gly + Phe-Leu
-
-
-
-
?
MCA-Ala-Ser-Asp-Lys-Dap(DNP)-OH + H2O
?
angiotensin-converting enzyme
-
-
?
MCA-Ala-Ser-Asp-Lys-Dap(DNP)-OH + H2O
?
angiotensin-converting enzyme
-
-
?
MCA-Tyr-Val-Ala-Asp-Ala-Pro-Lys(DNP)-OH + H2O
?
angiotensin-converting enzyme 2
-
-
?
MCA-Tyr-Val-Ala-Asp-Ala-Pro-Lys(DNP)-OH + H2O
?
angiotensin-converting enzyme 2
-
-
?
Met5-enkephalin + H2O
Tyr-Gly-Gly + Phe-Met
-
-
-
-
?
Met5-enkephalin + H2O
Tyr-Gly-Gly + Phe-Met
-
-
-
-
?
Met5-enkephalin + H2O
Tyr-Gly-Gly + Phe-Met
-
-
-
-
?
N-benzyloxycarbonyl-L-Phe-L-His-L-Leu + H2O
N-benzyloxycarbonyl-L-Phe + L-His-L-Leu
-
-
-
-
?
N-benzyloxycarbonyl-L-Phe-L-His-L-Leu + H2O
N-benzyloxycarbonyl-L-Phe + L-His-L-Leu
-
-
-
-
?
N-hippuryl-His-Leu + H2O
hippuric acid + His-Leu
-
-
-
?
N-hippuryl-His-Leu + H2O
hippuric acid + His-Leu
-
-
-
?
N-hippuryl-His-Leu + H2O
hippuric acid + His-Leu
-
-
-
?
N-[3-(2-furyl)acryloyl]-L-phenylalanyl-glycyl-glycine + H2O
N-[3-(2-furyl)acryloyl]-L-phenylalanine + glycyl-glycine
-
-
-
-
?
N-[3-(2-furyl)acryloyl]-L-phenylalanyl-glycyl-glycine + H2O
N-[3-(2-furyl)acryloyl]-L-phenylalanine + glycyl-glycine
-
-
-
-
?
N-[3-(2-furyl)acryloyl]-L-phenylalanylglycylglycine + H2O
?
-
-
-
?
N-[3-(2-furyl)acryloyl]-L-phenylalanylglycylglycine + H2O
?
-
-
-
?
neurotensin + H2O
pGlu-Leu-Tyr-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Tyr + Ile-Leu
-
-
-
-
?
neurotensin + H2O
pGlu-Leu-Tyr-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Tyr + Ile-Leu
-
-
-
-
?
NKLKPSQ + H2O
?
-
-
-
?
NKLKPSQWI + H2O
?
-
-
-
?
NKLKPSQWI + H2O
?
-
-
-
?
NKLKPSQWISL + H2O
?
-
-
-
?
NKLKPSQWISL + H2O
?
-
-
-
?
NKLKPSQWISLSD + H2O
?
-
-
-
?
NKLKPSQWISLSD + H2O
?
-
-
-
?
SLKPSNWLTPSE + H2O
?
-
-
-
?
SLKPSNWLTPSE + H2O
?
-
-
-
?
additional information
?
-
-
no cleavage of imido-bonds. No hydrolysis of angiotensin II and angiotensin III
-
?
additional information
?
-
ACE is a key regulator of blood pressure homeostasis
-
-
?
additional information
?
-
-
ACE is a key regulator of blood pressure homeostasis
-
-
?
additional information
?
-
-
the enzyme may play a role not only in the angiotensin-bradykinin system but also in the metabolism of circulating enkephalins and other bioactive peptides
-
-
?
additional information
?
-
AnCE is a single domain protein with ACE activity, an ACE homologue
-
-
?
additional information
?
-
-
AnCE is a single domain protein with ACE activity, an ACE homologue
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
may contribute to elevated blood pressure in hypertensive disease via conversion of angiotensin I to angiotensin II or inactivation of bradykinin
-
-
?
additional information
?
-
-
plays a role in blood pressure regulation
-
-
?
additional information
?
-
-
angiotensin-converting enzyme-2 is a regulatory protein of the renin-angiotensin system. ACE2 interacts with calmodulin and this association down-regulates shedding of the ACE2 ectodomain
-
-
?
additional information
?
-
-
neutral endopeptidase and angiotensin converting enzyme do not have additive effects regarding neuropeptide degradation
-
-
?
additional information
?
-
somatic angiotensin I-converting enzyme plays a central role in blood pressure regulation
-
-
?
additional information
?
-
-
ACE may play a role in human epidermis morphogenesis during fetal life and serve as an unrecognized marker for keratinocyte progenitor cells
-
-
?
additional information
?
-
-
complex formation witht e bradykinin B2 receptor
-
-
?
additional information
?
-
ACE comprises two homologous domains, that differ in their substrate preferences, overview
-
-
?
additional information
?
-
-
ACE comprises two homologous domains, that differ in their substrate preferences, overview
-
-
?
additional information
?
-
-
ACE is a dipeptidyl carboxypeptidase
-
-
?
additional information
?
-
-
the enzyme enhances presentation of certain endogenously synthesized peptides to major histocompatibility complex class-I-restricted cytotoxic T-lymphocytes
-
-
?
additional information
?
-
-
primary enzyme that is involved in the degradation of Tyr-Gly-Gly-Phe-Met-Arg-Gly-Leu in brain
-
-
?
additional information
?
-
-
ACE structure-activity relationship, overview
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
potential role of follicular enzyme in early stages of follicular maturation and atresia
-
-
?
additional information
?
-
-
ACE degrades bradykinin, other vasoactive peptides, and activates angiotensin
-
-
?
additional information
?
-
-
ACE is a dipeptidyl carboxypeptidase
-
-
?
additional information
?
-
ACE interacts with beta-arrestin1
-
-
?
additional information
?
-
-
ACE interacts with beta-arrestin1
-
-
?
additional information
?
-
ACE interacts with beta-arrestin1
-
-
?
additional information
?
-
-
ACE may influence trypsin biosynthesis in the larval gut by interacting with a trypsin-modulating oostatic factor
-
-
?
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(+)-catechin
-
IC50: about 1.6 mM
(-)-epicatechin
-
IC50: about 1.7 mM
(-)-epigallocatechin gallate
-
(2E)-3-(3-amino-4-methoxyphenyl)-1-(3,4,5-trimethoxyphenyl)prop-2-en-1-one
-
-
(2E)-3-(3-fluoro-4-methoxyphenyl)-1-(3,4,5-trimethoxyphenyl)prop-2-en-1-one
-
-
(2E)-3-(3-hydroxy-4-methoxyphenyl)-1-(3,4,5-trimethoxyphenyl)prop-2-en-1-one
-
-
(2E)-3-(3-hydroxy-4-nitrophenyl)-1-(3,4,5-trimethoxyphenyl)prop-2-en-1-one
-
-
(2E)-3-(3-methoxyphenyl)-1-(3,4,5-trimethoxyphenyl)prop-2-en-1-one
-
-
(2E)-3-(4-hydroxy-3-methoxyphenyl)-1-(3,4,5-trimethoxyphenyl)prop-2-en-1-one
-
-
(2E)-3-(4-methoxy-3-nitrophenyl)-1-(3,4,5-trimethoxyphenyl)prop-2-en-1-one
-
-
(2E)-3-(4-methoxyphenyl)-1-(3,4,5-trimethoxyphenyl)prop-2-en-1-one
-
-
(2E)-3-phenyl-1-(3,4,5-trimethoxyphenyl)prop-2-en-1-one
-
-
(2R)-2-((3-[hydroxyl (2-phenyl-(1R)-1-([(benzyloxy) carbonyl]-amino)ethyl)phosphinyl]-2-[(3-phenylisoxazol-5-yl)methyl]-1-oxopropyl)amino)-3-(4-hydroxy-phenyl) propanoic acid
(2S)-1-((3S)-3-amino-3-carboxypropyl)azetidine-2-carboxylic acid
-
IC50: 0.0033 mM
(2S)-2-((3-[hydroxyl (2-phenyl-(1R)-1-([(benzyloxy) carbonyl]-amino)ethyl)phosphinyl]-2-[(3-phenylisoxazol-5-yl)methyl]-1-oxopropyl)amino)-3-(4-hydroxy-phenyl) propanoic acid
(2S)-2-((3-[hydroxyl(2-phenyl-(1R)-1([(benzyloxy)carbonyl]amino)ethyl)phosphinyl]-(2R)-2-[(3-phenylisoxazol-5-yl)methyl]-1-oxopropyl)amino)-3-phenyl propanoic acid
-
-
(2S)-2-((3-[hydroxyl(2-phenyl-(1R)-1-([(benzyloxy)carbonyl]-amino)ethyl)phosphinyl]-(2R)-2-[(3-phenylisoxazol-5-yl)methyl]-1-oxopropyl)amino) 1H-Indole-3-propanoic acid
-
-
(2S)-2-((3-[hydroxyl(2-phenyl-(1R)-1-([(benzyloxy)carbonyl]-amino)ethyl)phosphinyl]-(2R)-2-[(3-phenylisoxazol-5-yl)methyl]-1-oxopropyl)amino)-3-(4-hydroxy-phenyl) propanoic acid
-
-
(2S)-2-((3-[hydroxyl(2-phenyl-(1R)-1-([(benzyloxy)carbonyl]-amino)ethyl)phosphinyl]-(2S)-2-[(3-phenylisoxazol-5-yl)methyl]-1-oxopropyl)amino) 1H-indole-3-propanoic acid
-
-
(2S)-2-((3-[hydroxyl(2-phenyl-(1R)-1-([(benzyloxy)carbonyl]-amino)ethyl)phosphinyl]-(2S)-2-[(3-phenylisoxazol-5-yl)methyl]-1-oxopropyl)amino)-3-(4-hydroxy-phenyl) propanoic acid
-
-
(2S)-2-([3-(1,1'-biphenyl)-2-([hydroxyl(2-phenyl-(1R)-1-([(benzyloxy)carbonyl]amino)ethyl)phosphinyl]methyl)-1-oxopropyl]-amino) 1H-indole-3-propanoic acid
-
-
(2S)-2-([3-(3'-[1,1'-biphenyl]-4''-yl-4',5'-dihydro-5'-isoxazolyl)-2-([hydroxyl(2-phenyl-(1R)-1-([(benzyloxy)carbonyl]amino)ethyl)-phosphinyl]methyl)-1-oxopropyl]amino) 1H-indole-3-propanoic acid
-
-
(2S)-2-[[(2S)-2-mercapto-3-methylpentanoyl]amino]-3-(1-naphthyl)propanoic acid
-
(2S)-2-[[(2S)-2-mercapto-3-methylpentanoyl]amino]-3-(2-naphthyl)propanoic acid
(2S)-2-[[(2S)-2-mercapto-3-methylpentanoyl]amino]-3-phenylpropanoic acid
-
(2S)-2-[[(2S)-2-mercapto-3-methylpentanoyl]amino]propanoic acid
-
(2S)-3-(4-hydroxyphenyl)-2-[[(2S)-2-mercapto-3-methylpentanoyl]amino]propanoic acid
-
(2S)-3-biphenyl-2-yl-2-[[(2S)-3-methyl-2-sulfanylpentanoyl]amino]propanoic acid
(2S)-3-biphenyl-3-yl-2-[[(2S)-3-methyl-2-sulfanylpentanoyl]amino]propanoic acid
(2S)-3-biphenyl-4-yl-2-[(2-mercapto-2-methylpropanoyl)amino]propanoic acid
-
(2S)-3-biphenyl-4-yl-2-[(mercaptoacetyl)amino]propanoic acid
-
(2S)-3-biphenyl-4-yl-2-[[(2S)-2-mercaptobutanoyl]amino]propanoic acid
-
(2S)-3-biphenyl-4-yl-2-[[(2S)-2-mercaptopropanoyl]amino]propanoic acid
-
(2S)-3-biphenyl-4-yl-2-[[(2S)-3-methyl-2-sulfanylpentanoyl]amino]propanoic acid
(5S)-5-[(N-benzoyl)-amino]-4-oxo-6-phenyl-hexanoyl-L-phenylalanine
phosphinic peptide inhibitor kAF
(5S)-5-[(N-benzoyl)amino]-4-oxo-6-phenylhexanoyl-L-phenylalanine
the inhibitor has a 30fold higher affinity for the C domain than for the N domain of ACE
(5S)-5-[(N-benzoyl)amino]-4-oxo-6-phenylhexanoyl-L-tryptophan
1-cyclohexyl-3-(2-morpholinoethyl)carbodiimide metho-p-toluene sulfonate
-
20 mM, 99.6% inhibition
1-Fluoro-2,4-dinitrobenzene
1-methyl-5-phenyl-3-(3,4,5-trimethoxyphenyl)-4,5-dihydro-1H-pyrazole
-
-
1-[(5S)-4-oxo-6-phenyl-5-[(phenylcarbonyl)amino]hexanoyl]-L-proline
-
1-[(5S)-5-[(tert-butoxycarbonyl)amino]-4-oxo-6-phenylhexanoyl]-L-proline
-
15B2
-
an inhibitor isolated from the culture broth of Actinomadura sp. No. 937ZE-1
2''-hydroxynicotianamide
-
angiotensin-I converting enzyme inhibitor from buckwheat (Fagopyrum esculentum Moench) flour, IC50: 0.00008 mM
2,3-butendione
-
10 mM, 97.4% inhibition
2,3-dimercapto-1-propanol
-
-
2-(benzyloxy)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-phenylalanine
2-hydroxyemodin 1-methylether
-
47.52% inhibition at 1.63 ng/ml
2-methoxy-4-[1-methyl-3-(3,4,5-trimethoxyphenyl)-4,5-dihydro-1H-pyrazol-5-yl]phenol
-
-
2-methoxy-5-[1-methyl-3-(3,4,5-trimethoxyphenyl)-4,5-dihydro-1H-pyrazol-5-yl]aniline
-
-
2-methoxy-5-[1-methyl-3-(3,4,5-trimethoxyphenyl)-4,5-dihydro-1H-pyrazol-5-yl]phenol
-
-
2-[([2-[(1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]cyclopentyl]carbonyl)amino]-3-(2,3-dihydro-1H-indol-3-yl)propanoate
-
3,6-Dihydroxy-1-phenazinecarboxylic acid
-
i.e. phenacein, competitive, reversed by Zn2+, isolated from a member of Streptomyces tanashiensis-zaomyceticus
3-(benzyloxy)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-phenylalanine
3-mercapto-2-D-methylpropanoyl-L-Pro
-
i.e. SQ-14,225
3-p-acetyl-aminophenylpropionate
-
-
3-p-aminophenylpropionate
-
-
5-(3,4,5-trihydroxyphenyl) 4-hydroxyvaleric acid
-
5-(3,4,5-trihydroxyphenyl)-gamma-valerolactone
the metabolite has a hypotensive effect in vivo
5-(3,5-dihydroxyphenyl) 4-hydroxyvaleric acid
-
5-(3,5-dihydroxyphenyl)-gamma-valerolactone
the metabolite has a hypotensive effect in vivo
5-(3-fluoro-4-methoxyphenyl)-1-methyl-3-(3,4,5-trimethoxyphenyl)-4,5-dihydro-1H-pyrazole
-
-
5-(3-methoxyphenyl)-1-methyl-3-(3,4,5-trimethoxyphenyl)-4,5-dihydro-1H-pyrazole
-
-
5-(4-methoxy-3-nitrophenyl)-1-methyl-3-(3,4,5-trimethoxyphenyl)-4,5-dihydro-1H-pyrazole
-
-
5-(4-methoxyphenyl)-1-methyl-3-(3,4,5-trimethoxyphenyl)-4,5-dihydro-1H-pyrazole
-
-
5-[1-methyl-3-(3,4,5-trimethoxyphenyl)-4,5-dihydro-1H-pyrazol-5-yl]-2-nitrophenol
-
-
9-[1-carboxy-3-(4-hydroxyphenyl)propylamino]octahydro-10-oxo-6H-pyridazo[1,2-a][1,2]diazepine-1-carboxylic acid
-
-
Ac-FKCRRWQWRMKKLGA-NH2
-
0.02 mM, 38% loss of activity with hippuryl-His-Leu, 41% loss of activity with angiotensin I
Ac-RKKPFW-NH2
-
0.02 mM, 24% loss of activity with hippuryl-His-Leu
Ac-RKWHFW-NH2
-
0.02 mM, 42% loss of activity with hippuryl-His-Leu, 55% loss of activity with angiotensin I; 0.02 mM, 48% loss of activity with hippuryl-His-Leu
Ac-RKWLFW-NH2
-
0.02 mM, 26% loss of activity with hippuryl-His-Leu, 71% loss of activity with angiotensin I; 0.02 mM, 32% loss of activity with hippuryl-His-Leu
Ac-RKWRFW-NH2
-
0.02 mM, 3% loss of activity with hippuryl-His-Leu
Ac-RRWQWR-NH2
-
0.02 mM, 29% loss of activity with hippuryl-His-Leu, 34% loss of activity with angiotensin I
Acetyl-Ala-Ala-Ala
-
hydrolysis of hippuryl-His-Leu
Acetyl-Ala-Ala-Ala-Ala
-
hydrolysis of hippuryl-His-Leu
acidic protease
-
about 80% ACE inhibitory
-
acteoside
-
a phenylpropanoid glycoside isolated from ethanolic extracts of seeds of Plantago asiatica, collected from Jiang Xi Province in China. The compound shows ACE inhibitory activity in vitro, structure analysis by NMR, UV, IR and MS
Ala-Ala-Ala
-
hydrolysis of hippuryl-His-Leu
Ala-Ala-Ala-Ala
-
hydrolysis of hippuryl-His-Leu
Ala-His-Ser-Tyr
-
a noncompetitive inhibitor, the peptide is resistant to further degenration by pepsin, trypsin, and chymotrypsin
Ala-Pro-Gly-Ala-Gly-Val-Tyr
-
-
alaternin
-
24.26% inhibition at 1.63 ng/ml
alcacepril
-
synthetic ACE inhibitor and antihypertensive drug
alcalase
-
about 20% ACE inhibitory
-
aliphatic monocarboxylates
-
degree of inhibition increases in proportion to their chain length up to C14
-
aminoethyl-chitin
-
with 10%, 50%, and 90% deacetylation
angiotensin converting enzyme inhibitor
-
ACE-I, inhibition is impacting both the renin-angiotensin cascade and the degradation metabolism of bradykinin, inhibition mechanism, overview. ACE-I is used as therapeutic agent in congestive heart failure, diabetic nephropathy, hypertension, and coronary artery disease. ACE-I medications can induce chronic cough, hypotension, hyperkalemia, bone marrow depression, angioedema, and rarely, hepatic failure. Angioedema involves a subcutaneous swelling reaction that evolves over several hours and is not associated with itching or pain, pathomechanism, detailed overview
-
angiotensin I converting enzyme inhibitory peptides
-
from wheat milling byproducts by proteolysis through aspartic proteases, optimally produced at pH 3.2. Milled whole grain, bran, shorts, and red dog acquire ACE inhibitory activity though water soaking treatment, preparation of shorts exhibits the strongest inhibitory activity with an IC50 value of 0.08 mg/ml, overview
-
angiotensin I-converting enzyme inhibitory peptides
-
i.e. ACE-Is, from enzymatic hydrolysates of cuttlefish, Sepia officinalis, muscle proteins, generated by the crude enzyme from Bacillus mojavensis A21, show 87.11% inhibition at 2 mg/ml, mass spectrometric analysis, overview
-
angiotensin IV
-
IC50: 0.07 mM
angiotensin-converting enzyme inhibitor
-
ACEi, induces angioedema, a non-allergic bradykinin-induced drug side-effect and clinical life-threatening problem, overview. ACE insertion/deletion and bradykinin B2 receptor polymorphisms are not involved in the development of ACEi-induced angio-oedema
-
angiotensin-I converting enzyme inhibitory peptides
-
activity of hydrolysates, using diverse proteases, from Avena sativa proteins by in silico and in vitro analyses, peptide sequencing, overview
-
antipain
-
0.1 mg/ml, 26% inhibition
Arg-Ala
-
hydrolysis of hippuryl-His-Leu
Arg-Met-Leu
-
IC50: 1.019 mM, competitive inhibition
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
-
hydrolysis of hippuryl-His-Leu
Asn-Trp-Gly-Pro-Leu-Val
-
-
Asp-Ala
-
hydrolysis of hippuryl-His-Leu
Asp-Asp-Thr-Gly-His-Asp-Phe-Glu-Asp-Thr-Gly-Glu-Ala-Met
-
an inhibitory peptide from the marine rotifer, Brachionus rotundiformis
Asp-Tyr-Gly-Leu-Tyr-Pro
-
-
aspergillomarasmine A
-
-
aspergillomarasmine B
-
-
benzoyl-NHCOCH2CH(COOH)-Ala-Pro-OH
-
-
benzoyl-NHCOCH2CH(COOH)-Trp-Pro-OH
-
-
benzyloxycarbonyl-PhePSI[PO2-CH]Ala-Ala
Drosophila sp. (in: flies)
-
-
benzyloxycarbonyl-PhePSI[PO2-CH]Ala-Trp
Drosophila sp. (in: flies)
-
-
Bothrops bradykinin potentiating peptides
-
-
-
bradykinin potentating factor nonapeptide
-
-
-
bradykinin potentiating peptide
i.e. BPP1 or pGlu-Trp-Pro-Arg-Pro-Gln-Ile-Pro-Pro
-
bradykinin potentiating peptide b
interaction with sACE in a Zn-dependent manner
-
bradykinin potentiator B
-
-
bradykinin-potentiating factor SQ 20881
-
-
bradykinin-potentiating peptide 9a
-
-
bradykinin-potentiator B
-
-
bradykinin-potentiator C
-
-
Ca2+
inhibitory at concentrations above 1 mM
catechin
-
IC50: 1.593 mM, competitive
chitooligosaccharide derivatives
-
chitosan trimer
-
effective in lowering blood pressure
chloramine-T
-
50 mM, 97.1% inhibition
Cl-
-
kcat increases with increasing KCl concentrations, reaches a maximum at about 300 mM KCl, and the begins to decrease. At relatively low concentrations chloride anions activate the C-domain of the enzyme, but at high concentrations chloride inhibits the enzyme activity. Presence of at least two chloride-binding sites in the C-domain of bovine enzyme: binding of chloride to one of the sites causes activation of the enzyme, whereas chloride binding to the second site results in inhibition of the enzymatic activity
cyanidin-3-O-beta-D-glucoside
-
isolated from flower buds of Rosa damascena. Metal ions might be involved in the inhibition
cyanidin-3-O-sambubioside
-
an anthocyanin isolated from Hibiscus sabdariffa calyces, competitive ACE inhibition reducing blood pressure in humans, IC50 is 0.0684 mg/ml
D-3-thio-2-methylpropanoyl-Pro
-
-
D-Cys-L-Pro
-
competitive to hippuryl-His-Leu
delphinidin-3-O-sambubioside
-
an anthocyanin isolated from Hibiscus sabdariffa calyces, competitive ACE inhibition reducing blood pressure in humans, IC50 is 0.0845 mg/ml
dexamethasone
-
markedly inhibits the plasma extravasion in the tracheal mucosa produced by substance P. The simultanous inhibition of neutral endopeptidase and angiotensin converting enzyme completely reverses the effect of dexamethasone on substance P-induced extravasion
diethyl dicarbonate
-
10 mM, 92.8% inhibition
emodin
-
45.79% inhibition at 1.63 ng/ml
epicatechin dimer
-
IC50: 0.267 mM, competitive
epicatechin hexamer
-
IC50: 0.01 mM, competitive
epicatechin pentamer
-
IC50: 0.025 mM, competitive
epicatechin tetramer
-
IC50: 0.012 mM, competitive
epicatechin trimer
-
IC50: 0.126 mM, competitive
epigallocatechin
-
IC50: about 0.3 mM
ESIINF
-
the inhibitor produces an acute blood-pressure-lowering effect in spontaneously hypertensive rats upon a single oral administration
ethyl caffeate
-
0.01 mg/ml, 32.4% inhibition
EtOAc extract of Rabdosia coetsa
-
angiotensin-converting enzyme inhibitory activity
-
flavanol
-
flavanols either isolated or present in foods can inhibit enzyme activity
flavourzyme
-
about 20% ACE inhibitory
-
genistein
-
0.003-0.3 mM genistein decreases the angiotensin-converting enzyme activity in blood plasma in a concentration-dependent manner; the isoflavone inhibits ACE in plasma and alters the vascular responses to angiotensin I and bradykinin, overview
Glu-Trp-Pro-Arg-Pro-Gln-Ile-Pro-Pro
-
-
gluco-aurantioobtusin
-
competitive inhibitor, 137.62% inhibition at 1.63 ng/ml
Gly-Gln
-
IC50: 5.63 mM, competitive inhibition
Gly-Gly-Val-Ile-Pro-Asn
-
-
Gly-L-Ala-Hyp-Gly-L-Leu-Hyp-Gly-L-Pro
Gly-L-Ala-Hyp-Gly-L-Pro-L-Ala-Gly-L-Pro-Gly-Gly-L-Ile-Hyp-Gly-L-Glu-L-Arg-Gly
Gly-L-Ile-Hyp-Gly-L-Glu-L-Arg-Gly-L-Pro-L-Val-Gly-L-Pro-L-Ser-Gly
Gly-L-Leu-Hyp-Gly-L-Ser-L-Arg-Gly-L-Glu-L-Arg-Gly-L-Leu-Hyp-Gly
Gly-Leu-Pro
-
IC50: 1.62 mM
Gly-Phe
-
IC50: 10.471 mM
Gly-Phe-Hyp-Gly-Thr-Hyp-Gly-Leu-Hyp-Gly-Phe
Gly-Pro
-
IC50: 252.63 mM
Gly-Pro-Ala
-
inhibits hydrolysis of Gly-Ala-Ala
Gly-Pro-Leu
-
IC50: 2.65 mM
glycinin hydrolysate
-
-
-
GQGGP
-
extraction and characterization of an ACE inhibitor from the fruiting body of Pholiota adiposa ASI 24012, which can be used as an antihypertensive drug
H2S
-
Zn2+ but not Cd2+, Ca2+ or Mg2+ could counteract the inhibitory effect
Hyp-Gly-Leu-Hyp-Gly-Phe
-
0.01 mM
Hyp-Gly-Phe
-
IC50: 0.433 mM
Hyp-Gly-Thr-Hyp-Gly-Leu-Hyp-Gly-Phe
-
0.019 mM
Ile-Ala-Tyr-Lys-Pro-Ala-Gly
-
-
Ile-Lys-Pro-Leu-Asn-Tyr
-
-
Ile-Pro-Pro-Gly-Val-Pro-Tyr
-
-
Ile-Pro-Pro-Gly-Val-Pro-Tyr-Trp-Thr
-
-
Ile-Val-Gly-Arg-Pro-Arg-His-Gln-Gly
-
-
inhibitory peptides from rice dreg hydrolysate
-
significant antihypertensive action and no other side effects by oral administration in spontaneous hypertension rats
-
isoacteoside
-
a phenylpropanoid glycoside isolated from ethanolic extracts of seeds of Plantago asiatica, collected from Jiang Xi Province in China. The compound shows ACE inhibitory activity in vitro, structure analysis by NMR, UV, IR and MS
isoquercitrin
-
IC50: 0.3 mM
isorhamnetin-3-beta-glucopyranoside
-
IC50: 0.4089 mM
kaempferol-3-alpha-arabinopyranoside
-
IC50: 0.3928 mM
kaempferol-3-O-alpha-L-arabinopyranoside
-
-
kaempferol-3-O-beta-D-galactopyranoside
-
-
KAPVA
-
a peptide derived from muscle titin
KRQKYDI
-
competitive inhibitor, the strongest inhibitor among reported troponin-originated peptides. The inhibhitor is slowly hydrolyzed by treatment with angiotensin I-converting enzyme. When KRQKYDI is administered orally to spontaneously hypertensive rats at a dose of 10 mg/kg, a temporary antihypertensive activity is observed at 3 and 6 h after administration
L-Glu-L-Arg-L-Tyr-L-Pro-L-Ile
-
-
L-Tyr-L-Thr-L-Ala-Gly-L-Val
-
-
Leu-Ala
-
hydrolysis of hippuryl-His-Leu
Leu-Ala-Ile-pro-Val-Asn-Lys-Pro
-
-
Leu-Arg-Ile-Pro-Val-Ala
-
-
Leu-Gly-Pro
-
IC50: 0.72 mM
Leu-Ile-Tyr
-
i.e. acein-2, isolated from tryptic hydrolysate of human plasma, non-competitive inhibitor, IC50: 0.00082 mM.
Leu-Lys-Tyr
-
competitive
Leu-Pro-Gly
-
IC50: 5.73 mM
Leu-Trp
-
IC50: 0.0174 mM, non-competitive
Leu-Val-Tyr
-
competitive
leupeptin
-
0.1 mg/ml, 18% inhibition
luteolin-7-O-beta-D-glucopyranoside
-
-
Lys-Ala
-
hydrolysis of hippuryl-His-Leu
Lys-Ala-Phe-Arg
-
ACE inhibitory peptide derived from Arachis hypogaea protein hydrolysate using digestion by Alcalase, mass spectrometric sequence determination, overview. IC50 value is 0.085 mg/ml
Lys-Leu-Pro-Arg-Gly-Thr-Leu-Phe
-
-
melanoidin
-
melanoidins obtained from coffee (three roasting degrees), beer, and sweet-wine show in-vitro angiotensin-converting enzyme-inhibitory activity. The activity in coffee melanoidinsis significantly higher at more severe heating conditions
-
Met-Trp
-
IC50: 0.0098 mM, non-competitive
methyl rosmarinate
-
0.01 mg/ml, 39.5% inhibition
Mg2+
inhibitory at concentrations above 1 mM
MLN-4760
-
conversion of Ang II to Ang(1-7) is blocked by MLN-4760 but not by DX600
Monascus-fermented soybean extract
-
butanol, ethyl acetate, 50% ethanol-soluble extract and water-soluble extract
-
mugineic acid
-
IC50: 0.00028 mM
N-(3-{[(1R)-1-{[(benzyloxy)carbonyl]amino}-2-phenylethyl](hydroxy)phosphoryl}-2-{[3-(biphenyl-4-yl)-4,5-dihydro-1,2-oxazol-5-yl]methyl}propanoyl)-L-tryptophan
-
-
N-alpha-[1-(S)-carboxy-3-phenylpropyl]-L-Lys-L-Pro
-
-
N-bromosuccinimide
-
2 mM, 99.8% inhibition
N-[(1S)-1-(ethoxycarbonyl)-3-phenylpropyl]-L-alanyl-L-proline
N-[(2S)-3-methyl-2-sulfanylpentanoyl]-2-phenoxy-L-phenylalanine
N-[(2S)-3-methyl-2-sulfanylpentanoyl]-3-phenoxy-L-phenylalanine
N-[(2S)-3-methyl-2-sulfanylpentanoyl]-O-phenyl-L-tyrosine
N-[(2S)-3-methyl-2-sulfanylpentanoyl]-O-[4-(trifluoromethyl)benzyl]-L-tyrosine
N-[(5S)-4-oxo-6-phenyl-5-[(phenylcarbonyl)amino]hexanoyl]-L-phenylalanine
-
N-[(5S)-4-oxo-6-phenyl-5-[(phenylcarbonyl)amino]hexanoyl]-L-tryptophan
-
N-[(5S)-5-[(tert-butoxycarbonyl)amino]-4-oxo-6-phenylhexanoyl]-L-phenylalanine
-
N-[(5S)-5-[(tert-butoxycarbonyl)amino]-4-oxo-6-phenylhexanoyl]-L-tryptophan
-
N-[(S)-1-(ethoxycarbonyl)-3-phenylpropyl]-L-alanyl-L-proline
-
i.e. MK 421. Effect of the inhibitor on the components of the renin system in healthy subjects : the drug has a prolonged duration of action and effectively reduces plasma converting enzyme activity, angiotensin II and aldosterone levels and thereby increases sodium diuresis
N-[(S)-1-Carboxy-3-phenylpropyl]-L-Ala-L-Pro
N-[1(S)-carboxy-5-aminopentyl]glycylglycine
-
weak competitive
N-[3-{[(1R)-1-{[(benzyloxy)carbonyl]amino}-2-phenylethyl](hydroxy)phosphoryl}-2-(biphenyl-4-ylmethyl)propanoyl]-L-tryptophan
-
-
N-{(2R)-3-{[(1R)-1-{[(benzyloxy)carbonyl]amino}-2-phenylethyl](hydroxy)phosphoryl}-2-[(3-phenyl-1,2-oxazol-5-yl)methyl]propanoyl}-L-tyrosine
-
-
N-{(2S)-3-{[(1R)-1-{[(benzyloxy)carbonyl]amino}-2-phenylethyl](hydroxy)phosphoryl}-2-[(3-phenyl-1,2-oxazol-5-yl)methyl]propanoyl}-L-tryptophan
-
-
N2-[(S)-1-carboxy-3-phenylpropyl]-L-lysyl-L-proline
-
effect of the inhibitor on the components of the renin system in healthy subjects : the drug has a prolonged duration of action and effectively reduces plasma converting enzyme activity, angiotensin II and aldosterone levels and thereby increases sodium diuresis
neutrase
-
about 70% ACE inhibitory
-
O-(2,4-difluorobenzyl)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-tyrosine
O-(3,4-difluorobenzyl)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-tyrosine
O-(4-fluorobenzyl)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-tyrosine
O-benzyl-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-tyrosine
o-phenanthroline
complete inhibition at 0.35 mM
O-[3,5-bis(trifluoromethyl)benzyl]-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-tyrosine
-
oenothein B
-
IC50: 0.25 mM
omega-phenylalkylcarboxylates
-
-
-
peptide
-
more angiotensin I converting enzyme-inhibitory peptides are present in hydrolyzed wet-milled corn germ compared to hydrolyzed dry-milled germ
pGlu-Asn-Trp-Pro-His-Pro-Gln-Ile-Pro-Pro
-
-
pGlu-Gly-Leu-Pro-Pro-Arg-Pro-Lys-Ile-Pro-Pro
-
-
pGlu-Gly-Leu-Pro-Pro-Gly-Pro-Pro-Ile-Pro-Pro
-
-
pGlu-Trp-Pro-Arg-Pro-Gln-Ile-Pro-Pro
-
-
Phe-Arg
-
hydrolysis of hippuryl-His-Leu
Phe-Gly-Ala-Ser-Thr-Arg-Gly-Ala
-
IC50: 0.0147 mM, noncompetitive
Phe-Gly-Gly-Phe
-
inhibits hydrolysis of Gly-Ala-Ala
Phe-His-Leu
-
inhibits hydrolysis of Gly-Ala-Ala
Phe-Hyp-Gly
-
IC50: 0.171 mM
Phe-Hyp-Gly-Thr-Hyp-Gly
-
0.406 mM
Phe-Hyp-Gly-Thr-Hyp-Gly-Leu-Hyp-Gly
-
25 mM
Phe-Leu
-
IC50: 0.0136 mM, non-competitive
Phe-Val-Asn-Pro-Gln-Ala-Gly-Ser
plant extract
-
of Brazilian plants: Calophyllum brasiliense, Combretum fruticosum, Leea rubra, Phoenix roebelinii and Terminalia catappa
-
plantainoside D
-
a phenylpropanoid glycoside isolated from ethanolic extracts of seeds of Plantago asiatica, collected from Jiang Xi Province in China. The compound shows ACE inhibitory activity in vitro, structure analysis by NMR, UV, IR and MS
plantamajoside
-
a phenylpropanoid glycoside isolated from ethanolic extracts of seeds of Plantago asiatica, collected from Jiang Xi Province in China. The compound shows ACE inhibitory activity in vitro, structure analysis by NMR, UV, IR and MS
Pro-Arg-Tyr
a potato patatin-derived peptide, competitive inhibition
Pro-Asn-Asn-Lys-Pro-Phe-Gln
-
-
Pro-Gly-Leu
-
IC50: 13.93 mM
Pro-Leu
-
IC50: 337.32 mM
Pro-Leu-Gly
-
IC50: 4.74 mM
Pro-Thr-His-Ile-Lys-Trp-Gly-Asp
PTHIKWGD
-
IC50: about 0.008 mM. Production kinetics of angiotensin-I converting enzyme inhibitory peptides from bonito meat in artificial gastric juice
PTPVP
-
a peptide derived from muscle titin
puqiedine
-
an ACE inhibitory steroidal alkaloid from Fritillaria puqiensis, 6.1% inhibition at 0.2 mM
puqienine A
-
an ACE inhibitory steroidal alkaloid from Fritillaria puqiensis, 20.4% inhibition at 0.2 mM
puqienine B
-
an ACE inhibitory steroidal alkaloid from Fritillaria puqiensis, 24.7% inhibition at 0.2 mM
puqienine C
-
an ACE inhibitory steroidal alkaloid from Fritillaria puqiensis, 19.8% inhibition at 0.2 mM
puqienine D
-
an ACE inhibitory steroidal alkaloid from Fritillaria puqiensis, 16.5% inhibition at 0.2 mM
puqienine E
-
an ACE inhibitory steroidal alkaloid from Fritillaria puqiensis, 72% inhibition at 0.2 mM
puqietinone
-
an ACE inhibitory steroidal alkaloid from Fritillaria puqiensis, 9.3% inhibition at 0.2 mM
Pyr-Asn-Trp-Pro-Arg-Pro-Gln-Ile-Pro-Pro
-
hydrolysis of hippuryl-His-Leu
Pyr-Asn-Trp-Pro-His-Pro-Gln-Ile-Pro-Pro
-
hydrolysis of hippuryl-His-Leu
Pyr-Gly-Gly-Trp-Pro-Arg-Pro-Gly-Pro-Glu-Ile-Pro-Pro
-
hydrolysis of hippuryl-His-Leu
Pyr-Gly-Leu-Pro-Pro-Arg-Pro-Lys-Ile-Pro-Pro
-
hydrolysis of hippuryl-His-Leu
Pyr-Gly-Leu-Pro-Pro-Gly-Pro-Pro-Ile-Pro-Pro
-
hydrolysis of hippuryl-His-Leu
Pyr-Ser-Trp-Pro-Asn-Ile-Pro-Pro
-
hydrolysis of hippuryl-His-Leu
Pyr-Trp-Pro-Arg-Pro-Gln-Ile-Pro
Pyr-Trp-Pro-Arg-Pro-Gln-Ile-Pro-Pro
Pyr-Trp-Pro-Arg-Pro-Thr-Pro-Gln-Ile-Pro-Pro
-
hydrolysis of hippuryl-His-Leu
pyrrolidone-Lys-Trp-Ala-Pro
-
-
quercetin 3-O-(6''-galloyl)-galactoside
-
IC50: 0.16 mM
quercetin 3-O-alpha-(6''-p-coumaroylglucosyl-beta -1,2-rhamnoside)
-
IC50: 0.351 mM
quercetin-3-beta-glucopyranoside
-
IC50: 0.7088 mM
quercetin-3-O-alpha-(6''-caffeoylglucosyl-beta-1,2-rhamnoside)
-
IC50: 0.1589 mM
quercetin-3-O-alpha-L-arabinopyranoside
-
-
quercitrin
-
IC50: 0.25 mM
quercitrin glucuronide
-
IC50: 0.2 mM
RMLGQ
-
IC50: 0.358 mM, competitive inhibition
RMLGQTP
-
IC50: 0.503 mM, mixed-type inhibition
RMLGQTPTK
-
IC50: 0.034 mM, noncompetitive inhibition
rosmarinic acid
-
0.01 mg/ml, 55.2% inhibition
sardine peptide
-
a protein hydrolysate derived from muscles of sardines, inhibits in vivo and reduces the blood glucose level, but not the plasma insulin level
-
Ser-Pro
-
hydrolysis of hippuryl-His-Leu
SFTAGARTFNFDENPCDYFQGGKIKAT
-
-
soymilk protein proteolytic peptides
-
generated by proteolytic action of Lactobacilli and Bifidobacterium, which is increased in presence of fructooligosaccharides. The peptides show inhibitory activity to ACE, with IC50 values of 0.02 to 0.17 mg/ml, and antihypertensive effect in vivo, overview
-
SPB1
Bacillus subtilis crude lipopeptide biosurfactant, the biosurfactant displays a potent inhibition of ACE activity in vitro, IC50 is 1.37 mg/ml
-
temocapril
-
chronic treatment with temocapril improves the carotid arterial stiffness in healthy, normotensive elderly, and hence may reduce their risk for cardiovascular disease
Tetranitromethane
-
5 mM, 99.1% inhibition
Thermolysin
-
extract of dried bonito
-
thiorphan
-
weak, IC50: 0.0001 mM
Thr-Lys
-
IC50: 1.634 mM, mixed-type inhibition
Thr-Pro
-
IC50: 2.071 mM, competitive inhibition
trifluoroethanol
TFE, stabilizes ACE at low concentrations, while acts as a denaturant at higher concentration (20%). Secondary and tertiary structure and activity of ACE in the absence and presence of TFE are investigated using circular dichroism, fluorescence quenching, and UV-visible spectroscopy, respectively
Triton X-100
activates at 0.01%, inhibits at 1.0-10.0%
Trp-Ala
-
IC50: 0.2773 mM, competitive
Trp-Gly
a potato patatin-derived peptide, mixed-type inhibition
Trp-Met
-
IC50: 0.0986 mM, competitive
Trp-Pro-Glu-Ala-Ala-Glu-Leu-Met-Met-Glu-Val-Asp-Pro
Trp-Tyr-Thr
a peptide from hempseed, mixed-type inhibition
Trp-Val
-
IC50: 0.5005 mM, competitive
Trp-Val-Pro-Ser-Val-Tyr
-
-
Trp-Val-Tyr-Tyr
a peptide from hempseed, mixed-type inhibition
Tyr-Ala
-
hydrolysis of hippuryl-His-Leu
Tyr-Ala-Leu-Pro-His-Ala
-
-
Tyr-Leu-Ala-Gly-Asn-Gln
-
-
Tyr-Tyr-Ala-Pro-Phe-Asp-Gly-Ile-Leu
-
-
Val-Ile-Glu-Lys-Tyr-Pro
-
-
Val-Lys-Lys-Val-Leu-Gly-Asn-Pro
-
the angiotensin-I converting enzyme inhibitory peptide derived from porcine skeletal muscle myosin is a noncompetitive inhibitor that is slowly hydrolyzed by angiotensin-I converting enzyme. At the dose of 10 mg/kg, this peptide shows antihypertensive activity after a maximum of 3 h of administration
Val-Met-Asp-Lys-Pro-Gln-Gly
-
-
Val-Thr-Pro-Ala-Leu-Arg
-
-
Val-Thr-Val-Asn-Pro-Tyr-Lys-Trp-Leu-Pro
-
-
verticine
-
IC50: 0.3128 mM
verticinone
-
IC50: 0.165 mM
YRGGLEPINF
-
the inhibitor produces an acute blood-pressure-lowering effect in spontaneously hypertensive rats upon a single oral administration
Zn2+
inhibitory at concentrations above 1 mM
ZnCl2
-
1.0 mM, 98% inhibition
[CB-TE2A]1--lisinopril
-
-
-
[Co-DOTA]1--lisinopril
-
-
-
[Co-EDTA]1--lisinopril
-
-
-
[Cu-CB-TE2A]1+-lisinopril
-
-
-
[Cu-DOTA]1--lisinopril
-
-
-
[Cu-EDTA]1--lisinopril
-
-
-
[DOTA]1--lisinopril
-
-
-
[Fe-CB-TE2A]2+-lisinopril
-
-
-
[Fe-DOTA]0-lisinopril
-
-
-
[Fe-EDTA]0-lisinopril
-
-
-
[Fe-NTA]1+-lisinopril
-
-
[Ni-CB-TE2A]1+-lisinopril
-
-
-
[Ni-DOTA]1--lisinopril
-
-
-
[Ni-EDTA]1--lisinopril
-
-
-
[[(2S)-2-mercapto-3-methylpentanoyl]amino]acetic acid
(2R)-2-((3-[hydroxyl (2-phenyl-(1R)-1-([(benzyloxy) carbonyl]-amino)ethyl)phosphinyl]-2-[(3-phenylisoxazol-5-yl)methyl]-1-oxopropyl)amino)-3-(4-hydroxy-phenyl) propanoic acid
-
(2R)-2-((3-[hydroxyl (2-phenyl-(1R)-1-([(benzyloxy) carbonyl]-amino)ethyl)phosphinyl]-2-[(3-phenylisoxazol-5-yl)methyl]-1-oxopropyl)amino)-3-(4-hydroxy-phenyl) propanoic acid
-
(2S)-2-((3-[hydroxyl (2-phenyl-(1R)-1-([(benzyloxy) carbonyl]-amino)ethyl)phosphinyl]-2-[(3-phenylisoxazol-5-yl)methyl]-1-oxopropyl)amino)-3-(4-hydroxy-phenyl) propanoic acid
-
(2S)-2-((3-[hydroxyl (2-phenyl-(1R)-1-([(benzyloxy) carbonyl]-amino)ethyl)phosphinyl]-2-[(3-phenylisoxazol-5-yl)methyl]-1-oxopropyl)amino)-3-(4-hydroxy-phenyl) propanoic acid
-
(2S)-2-[[(2S)-2-mercapto-3-methylpentanoyl]amino]-3-(2-naphthyl)propanoic acid
-
(2S)-2-[[(2S)-2-mercapto-3-methylpentanoyl]amino]-3-(2-naphthyl)propanoic acid
-
(2S)-3-biphenyl-2-yl-2-[[(2S)-3-methyl-2-sulfanylpentanoyl]amino]propanoic acid
-
(2S)-3-biphenyl-2-yl-2-[[(2S)-3-methyl-2-sulfanylpentanoyl]amino]propanoic acid
-
(2S)-3-biphenyl-3-yl-2-[[(2S)-3-methyl-2-sulfanylpentanoyl]amino]propanoic acid
-
(2S)-3-biphenyl-3-yl-2-[[(2S)-3-methyl-2-sulfanylpentanoyl]amino]propanoic acid
-
(2S)-3-biphenyl-4-yl-2-[[(2S)-3-methyl-2-sulfanylpentanoyl]amino]propanoic acid
-
(2S)-3-biphenyl-4-yl-2-[[(2S)-3-methyl-2-sulfanylpentanoyl]amino]propanoic acid
-
(5S)-5-[(N-benzoyl)amino]-4-oxo-6-phenylhexanoyl-L-tryptophan
the inhibitor shows strong C domain selectivity, having almost 1300-fold greater affinity for the C domain than for the N domain of ACE
(5S)-5-[(N-benzoyl)amino]-4-oxo-6-phenylhexanoyl-L-tryptophan
phosphinic peptide inhibitor kAW
1,10-phenanthroline
-
5.0 mM, complete inhibition
1-Fluoro-2,4-dinitrobenzene
-
1 mM, 96% inhibition of N-domain ACE
1-Fluoro-2,4-dinitrobenzene
-
1 mM, 31% inhibition
2-(benzyloxy)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-phenylalanine
-
2-(benzyloxy)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-phenylalanine
-
2-mercaptoethanol
-
-
3-(benzyloxy)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-phenylalanine
-
3-(benzyloxy)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-phenylalanine
-
4-coumaric acid
-
-
4-hydroxybenzoic acid
-
-
4-hydroxybenzoic acid
-
-
Ala-Ala
-
hydrolysis of hippuryl-His-Leu
Ala-Ala
-
inhibits hydrolysis of Gly-Ala-Ala
Ala-Leu-Pro-His-Ala
-
-
Ala-Phe
-
-
Ala-Trp
-
IC50: 0.0064 mM, non-competitive
Ala-Tyr
-
-
angiotensin I
-
-
angiotensin II
-
-
angiotensin II
angiotensin II shows selective competitive inhibition of the carboxy-terminal domain of human somatic ACE
angiotensin II
-
hydrolysis of hippuryl-His-Leu
angiotensin II
-
inhibits hydrolysis of angiotensin I and Gly-Ala-Ala
apigenin
-
-
Arg-Pro-Pro
-
inhibition of enzyme form I and II, enzyme form III is not inhibited
Arg-Pro-Pro
-
hydrolysis of hippuryl-His-Leu
Arg-Pro-Pro
-
more inhibitory at pH 8 than at pH 6
benazepril
-
induces isolated visceral angioedema: a rare and under diagnosed adverse effect of angiotensin converting enzyme inhibitors
benazepril
-
treatment with angiotensin-converting enzyme inhibitors is of benefit in reducing the progression of renal damage in young patients with moderately proteinuric IgA nephropathy
benazeprilat
-
-
benzoic acid
-
-
bradykinin
-
-
bradykinin potentiator C
-
-
bradykinin potentiator C
-
inhibition of enzyme form I and II, enzyme form III is not inhibited
caffeic acid
-
-
caffeic acid
-
IC50: about 1.7 mM
captopril
-
0.1 mM, complete inhibition
captopril
-
reduces the percentage of sperm with progressive motility and acrosome reactions after capacitation in vitro
captopril
the relative potency of the inhibitors in the order of decreasing efficieny is: enalaprilat, lisinopril, captopril. The thermodynamic behaviour of the binding process is analyzed
captopril
-
synthetic ACE inhibitor and antihypertensive drug
captopril
-
the ACE inhibitor shows best renoprotective effect in patients with renal disease
captopril
-
competitive, of great value for use in chronic therapy of human hypertensive disease
captopril
-
i.e. D-(3-mercapto-2-methylpropanoyl)-L-Pro
captopril
-
i.e. SQ 14225
captopril
binding mode, molecular docking, detailed overview
captopril
-
i.e. D-(3-mercapto-2-methylpropanoyl)-L-Pro
captopril
-
the angiotensin-converting enzyme inhibitor, promotes growth of immunogenic tumors in mice
captopril
-
hyperalgesic effect
captopril
-
it is likely that prevention of angiotensin II receptor stimulation is a major mechanism underlying the inhibition of myosin-induced myocarditis by captopril
captopril
-
angiotensin-converting enzyme inhibition confers renoprotection in adriamycin nephropathy by reducing intrarenal angiotensin II and augmenting expression of N-acetylseryl-aspartyl-lysyl-proline that together attenuate signaling of mitogen-activated protein kinase and its downstream proinflammatory and fibrinogenic properties
captopril
-
microarray gene expression profiling of the aorta during atherosclerosis prevention with the ACE inhibitor, overview. Captopril treatment for 7 months strongly decreases the recruitment of proatherogenic immune cells into the aorta. Captopril-mediated inhibition of plaque infiltrating immune cells involves downregulation of the C-C chemokine receptor 9, CCR9, phenotype and physiological mechanism, overview
captopril
ACE competitive inhibitor, inhibits somatic ACE activity. Captopril significantly lowers the percentage of cells in the S phase and significantly increases the percentage of cells in the G0/G1 phase compared with the negative control, whereas the percentage of cells in each cell cycle phase nearly recovers following captopril withdrawal
captopril
-
inhibition study by capillary electrophoresis
captopril
-
87.87% inhibition at 1.63 ng/ml
captopril
-
98.5% inhibition at 0.2 mM
captopril
-
lipophilic ACE inhibitors quinapril, enalapril, and captopril increase the survival and lifetime of rats with experimental chronic heart failure
captopril
-
plasma angiotensin converting enzyme inhibitors
captopril
-
the anngiotensin converting enzyme inhibitor captopril modifies conditioned place preference induced by morphine and morphine withdrawal signs in rats
captopril
-
inhibits in vivo and reduces the blood glucose level, but not the plasma insulin level
captopril
-
ACE inhibition during pregnancy and lactation in adult offspring rats induces behavioural changes, e.g. in the open field test, overview
captopril
-
synthetic ACE inhibitor and antihypertensive drug
captopril
-
i.e. SQ 14225
captopril
-
i.e. D-3-mercapto-2-methyl-propionyl-L-proline, 80.5% inhibition at 0.005 mg/mg in L6 larvae
catechol
-
-
chitooligosaccharide derivatives
-
i.e. COS, chitosan derivatives, polycationic polymers comprised principally of glucosamine units, generated via either chemical or enzymatic hydrolysis of chitosan. ACE inhibitory activity of hetero-COS, derived from crab chitin, is dependent on the degree of deacetylation of chitosan
-
chitooligosaccharide derivatives
-
i.e. COS, chitosan derivatives, polycationic polymers comprised principally of glucosamine units, generated via either chemical or enzymatic hydrolysis of chitosan. ACE inhibitory activity of hetero-COS, derived from crab chitin, is dependent on the degree of deacetylation of chitosan
-
chlorogenic acid
-
IC50: about 1.8 mM
Co2+
-
-
Co2+
-
testicular enzyme is inhibited, lung enzyme not
Co2+
inhibitory at concentrations above 1 mM
CuCl2
-
73% inhibition at 0.1 mM, 99% inhibition at 1.0 mM
D-mannitol
-
IC50: 3 mg/ml
D-mannitol
-
antihypertensive effect in spontaneously hypertensive rats by oral administration
dieckol
-
deribed from Ecklonia stolonifera
dieckol
-
deribed from Ecklonia stolonifera
eckol
-
derived from Ecklonia stolonifera
eckol
-
derived from Ecklonia stolonifera
EDTA
-
1.0 mM, complete inhibition
EDTA
-
10 mM, complete inhibition of hydrolysis of o-aminobenzoyl-SDK-(dinitrophenyl)-P-OH and o-aminobenzoyl-FRK-(dinitrophenyl)-P-OH of wild-type enzyme, N-domain and C-domain
EDTA
-
recombinant enzyme, restored by ZnSO4
EDTA
complete inhibition at 0.01 mM
EDTA
-
somewhat more effective at pH 6 than at pH 8
ellagic acid
-
-
ellagic acid
-
IC50: 0.4 mM
enalapril
-
-
enalapril
-
angioedema is a rare but potentially life-threatening adverse effect of angiotensin-converting enzyme inhibitors. Angioedema due to angiotensin-converting enzyme inhibitors usually appears during the first weeks of treatment. Late-onset anioedema is often unrecognized
enalapril
-
the angiotensin-converting enzyme inhibitor has no effect on the rate of endothelial apoptosis in vitro in HUVEC cells
enalapril
-
standing and supine blood pressure decreases significantly in both autosomal-dominant polycystic kidney disease patients and controls after the administration of enalapril on low and high-sodium intakes, with no differences between the two groups
enalapril
-
synthetic ACE inhibitor and antihypertensive drug
enalapril
-
i.e. (2S)-1-[(2S)-2-[(2S)-1-ethoxy-1-oxo-4-phenylbutan-2-yl]aminopropanoyl]pyrrolidine-2-carboxylic acid
enalapril
-
treatment of mdx mice (murine model of duchenne muscular dystrophy) with the ACE inhibitor enalapril significantly increases the net force and tetanic isometric force of the gastrocnemius muscle in sedentary and exercised dystrophic mice. Enalapril decreases the necrotic areas in the gastrocnemius muscles in both conditions of mdx mice. ACE inhibition treatment also leads to a decrease in fibrosis, as manifested by a reduction in ECM protein levels and collagen amount
enalapril
-
inhibits corneal angiogenesis in vivo, enalapril treatment causes a notable decrease in corneal neovascularization, and enalapril-treated rabbit corneas showing a lesser degree of blood vessel staining for collagen type IV and lectin, overview
enalapril
-
acute angiotensin-converting enzyme inhibition evokes bradykinin-induced sympathetic activation in diabetic rats
enalapril
-
lipophilic ACE inhibitors quinapril, enalapril, and captopril increase the survival and lifetime of rats with experimental chronic heart failure
enalapril
-
the angiotensin-converting enzyme inhibitor has no significant effect on apoptosis induced via endotoxic shock with Escherichia coli lipopolysaccharides
enalapril
-
reduces the liver tissue transforming growth factor beta-1 and has an ameliorating effect on the fibrosis markers transforming growth factor beta-1 and matrix metalloproteinase-2. Enalapril does not affect the process of liver fibrosis at all (induced in rats by bile-duct ligation)
enalapril
-
plasma angiotensin converting enzyme inhibitors
enalapril
-
i.e. ((S)-1-ethoxycarbonyl-3-phenylpropyl)-L-alanyl-L-proline, 74.9% inhibition at 0.005 mg/mg in L6 larvae
enalapril
-
i.e. (2S)-1-[(2S)-2-[(2S)-1-ethoxy-1-oxo-4-phenylbutan-2-yl]aminopropanoyl]pyrrolidine-2-carboxylic acid
enalaprilat
-
-
enalaprilat
the relative potency of the inhibitors in the order of decreasing efficieny is: enalaprilat, lisinopril, captopril. The thermodynamic behaviour of the binding process is analyzed
enalaprilat
-
inhibits ACE and the bradykinin degradation in vivo, which is reversed by insulin
enalaprilate
-
-
enalaprilate
-
no inhibition
enalaprilate
-
bradykinin receptor 2 (BDKRB2) BE1 polymorphism influences bradykinin type 2 receptor mediated vasodilation during angiotensin-converting enzyme inhibition
enapril
-
-
enaprilat
-
-
enaprilat
-
i.e. N-[(S)-1-carboxy-3-phenylpropyl]-Ala-Pro
epicatechin
-
-
epicatechin
-
IC50: 1.781 mM, competitive
ferulic acid
-
-
fosinopril
-
-
fosinopril
-
administered as a prodrug and then rapidly converted by the liver and the gastrointestinal mucosa to the active form fosinoprilat
fosinopril
-
causes a significant decrease in plasminogen activator inhibitor 1, PAI-1, levels, probably by aldosterone escape
gallic acid
-
-
gallic acid
-
IC50 : about 1.7 mM
Gly-L-Ala-Hyp-Gly-L-Leu-Hyp-Gly-L-Pro
-
highest ACE-inhibitory activity
Gly-L-Ala-Hyp-Gly-L-Leu-Hyp-Gly-L-Pro
-
highest ACE-inhibitory activity
Gly-L-Ala-Hyp-Gly-L-Pro-L-Ala-Gly-L-Pro-Gly-Gly-L-Ile-Hyp-Gly-L-Glu-L-Arg-Gly
-
-
Gly-L-Ala-Hyp-Gly-L-Pro-L-Ala-Gly-L-Pro-Gly-Gly-L-Ile-Hyp-Gly-L-Glu-L-Arg-Gly
-
-
Gly-L-Ile-Hyp-Gly-L-Glu-L-Arg-Gly-L-Pro-L-Val-Gly-L-Pro-L-Ser-Gly
-
-
Gly-L-Ile-Hyp-Gly-L-Glu-L-Arg-Gly-L-Pro-L-Val-Gly-L-Pro-L-Ser-Gly
-
-
Gly-L-Leu-Hyp-Gly-L-Ser-L-Arg-Gly-L-Glu-L-Arg-Gly-L-Leu-Hyp-Gly
-
-
Gly-L-Leu-Hyp-Gly-L-Ser-L-Arg-Gly-L-Glu-L-Arg-Gly-L-Leu-Hyp-Gly
-
-
Gly-Phe-Hyp-Gly-Thr-Hyp-Gly-Leu-Hyp-Gly-Phe
-
IC50: 0.026 mM. Inhibitory peptide derived from chicken breast muscle
Gly-Phe-Hyp-Gly-Thr-Hyp-Gly-Leu-Hyp-Gly-Phe
-
inhibitory peptide derived from chicken breast muscle possesses hypotensive activity for spontaneously hypertensive rats
Gly-Trp
-
IC50: 20.417 mM
Gly-Tyr
-
IC50: 5.495 mM
HERDPTHIKWGD
-
IC50: about 0.008 mM. Production kinetics of angiotensin-I converting enzyme inhibitory peptides from bonito meat in artificial gastric juice
HERDPTHIKWGD
-
ACE inhibitor peptide B derived from water extracts of bonito protein, glyceraldehyde-3-phosphate dehydrogenase, hydrolysates, tandem multimer expression in and purification from Escherichia coli strain XL1-Blue and BL21(DE3), detailed overview
His-Leu
-
-
His-Leu
-
hydrolysis of hippuryl-His-Leu
His-Leu
-
inhibits hydrolysis of Gly-Ala-Ala
Ile-Glu-Pro
-
molecular docking analysis at the active site of testis ACE, overview
Ile-Glu-Trp
-
-
Ile-Glu-Tyr
-
molecular docking analysis at the active site of testis ACE, overview
Ile-Lys-Pro
-
a potent competitive inhibitor, molecular docking analysis at the active site of testis ACE, overview
Ile-Lys-Trp
-
molecular docking analysis at the active site of testis ACE, overview
Ile-Lys-Tyr
-
molecular docking analysis at the active site of testis ACE, overview
Ile-Pro-Pro
-
-
Ile-Pro-Pro
-
casein hydrolysate containing VPP and IPP improves the vascular endothelial dysfunction in subjects with mild hypertension. The continuous intake of VPP and IPP could help to prevent cardiovascular diseases in hypertensive subjects
Ile-Trp
-
-
Ile-Trp
-
IC50: 0.0047 mM, non-competitive
Ile-Trp-His-His-Thr
-
-
Ile-Tyr
-
-
kaempferol
-
-
kaempferol
-
IC50: about 1.2 mM
kaempferol
-
dose-dependent inhibition, 46% inhibition at 0.1 mM
L-681,176
-
-
L-681,176
-
purification of the inhibitor found in the culture filtrate of Streptomyces sp. MA 5143
L-Ala-L-Trp
-
-
L-Val-L-Phe
-
-
L-Val-L-Tyr
-
-
Leu-Gln-Pro
-
-
Leu-Gln-Pro
-
competitive
Leu-Phe
-
-
Leu-Phe
-
IC50: 0.3832 mM, competitive
lisinopril
-
-
lisinopril
-
no inhibition
lisinopril
-
the inhibitor binds in a highly ordered, extended conformation, with the phenyl group extended in an N-terminal direction and a lysine side chain parallel to the alpha13 helix containing the HEXXH zinc binding motif
lisinopril
the relative potency of the inhibitors in the order of decreasing efficieny is: enalaprilat, lisinopril, captopril. The thermodynamic behaviour of the binding process is analyzed
lisinopril
the compound shows a 4fold domain-selectivity for the C-domain compared to the N-domain. Active site binding structure, overview
lisinopril
-
synthetic ACE inhibitor and antihypertensive drug
lisinopril
-
i.e. N2-[(1S)-1-carboxy-3-phenylpropyl]-L-lysyl-L-proline, molecular docking analysis at the active site of testis ACE, PDB ID 1086, overview
lisinopril
-
i.e. N-[(S)-1-carboxy-3-phenylpropyl]-L-Lys-L-Pro
lisinopril
-
tumor growth is significantly inhibited as measured by tumor weight
lisinopril
-
angiotensin-converting enzyme inhibitor enhances the liver regeneration in rats after partial hepatectomy. Angiotensin-converting enzyme enhanced the hepatic regenerative response to PH by two independent mechanisms: an activation of B2 receptors and inhibition of angiotensin II production, both of which may stimulate production of hepatocyte growth factor, resulting in enhancement of the hepatic regeneration
lisinopril
-
therapeutic resistance to angiotensin converting enzyme inhibition is related to a difference in the combination of renal pharmacodynamic and pharmacokinetic characteristics in non-responders, primarily consisting of increased renal expression of angiotensin converting enzyme and higher angiotensin converting enzyme inhibitor clearance
lisinopril
-
treatment with 75 mg/l lisinopril significantly reduces renal ACE activity without affecting renal ACE2 activity
lisinopril
-
i.e. [(S)-1-carboxy-3-phenylpropyl]-L-lysyl-L-proline
lisinopril
-
i.e. N2-[(1S)-1-carboxy-3-phenylpropyl]-L-lysyl-L-proline
lisW-S
lisinopril-tryptophan S-enantiomer, a C-domain human sACE specific inhibitor and antihypertensive drug
lisW-S
a C-domain-selective derivative of the drug lisinopril. The compound shows a 258fold domain-selectivity for the C-domain compared to the N-domain, that is largely due to the co-operative effect of C-domain-specific residues in the S2' subsite. Interactions in the active site: comparison between N- and C-domain residues, overview
Mn2+
-
-
muracein A
-
-
muracein A
-
and SQ 28,370, the reduction product of muracein A
muracein B
-
-
muracein B
-
less potent inhibitor
muracein C
-
-
muracein C
-
less potent inhibitor
N-[(1S)-1-(ethoxycarbonyl)-3-phenylpropyl]-L-alanyl-L-proline
-
accelerated nitrotyrosine content in the renal cortex during high-glucose conditions is prevented by treatment with the angiotensin-converting enzyme inhibitor treatment. The suppressed degradation of nitrotyrosine in the renal cortex by the angiotensin-converting enzyme inhibitor enhances both superoxide anion degradation per se and antioxidative effects including activation of superoxide dismutase
N-[(1S)-1-(ethoxycarbonyl)-3-phenylpropyl]-L-alanyl-L-proline
-
independent of diet enalapril treatment decreases food intake, energetic gain and body weight in normotensive young rats, followed by reduced body fat mass and serum leptin
N-[(2S)-3-methyl-2-sulfanylpentanoyl]-2-phenoxy-L-phenylalanine
-
N-[(2S)-3-methyl-2-sulfanylpentanoyl]-2-phenoxy-L-phenylalanine
-
N-[(2S)-3-methyl-2-sulfanylpentanoyl]-3-phenoxy-L-phenylalanine
-
N-[(2S)-3-methyl-2-sulfanylpentanoyl]-3-phenoxy-L-phenylalanine
-
N-[(2S)-3-methyl-2-sulfanylpentanoyl]-O-phenyl-L-tyrosine
-
N-[(2S)-3-methyl-2-sulfanylpentanoyl]-O-phenyl-L-tyrosine
-
N-[(2S)-3-methyl-2-sulfanylpentanoyl]-O-[4-(trifluoromethyl)benzyl]-L-tyrosine
-
N-[(2S)-3-methyl-2-sulfanylpentanoyl]-O-[4-(trifluoromethyl)benzyl]-L-tyrosine
-
N-[(S)-1-Carboxy-3-phenylpropyl]-L-Ala-L-Pro
-
-
N-[(S)-1-Carboxy-3-phenylpropyl]-L-Ala-L-Pro
-
-
N-[(S)-1-Carboxy-3-phenylpropyl]-L-Ala-L-Pro
-
-
NaCl
Drosophila sp. (in: flies)
-
at pH 7 increasing concentrations of NaCl result in a faster rate of conversion which reaches a plateau at 150-200 mM NaCl. The activation by NaCl at pH 7 is the result of a 330% increase in kcat/Km which is solely attributable to a lowering of the Km. At pH 8, maximal activity is achieved in absence of NaCl, weak inhibitory effect on hydrolysis of angiotensin I as salt concentrations increase from 0 to 200 mM
NaCl
-
500 mM, 50% inhibition
NaCl
-
concentration dependent inhibition of hippuryl-His-Leu between 0 and 100 mM
nicotianamine
-
IC50: 0.000085 mM
nicotianamine
-
mixed inhibition. The preferential inhibition of circulating and tissue angiotensin I-converting enzyme by nicotianamine can contribute to the suppression of hypertension
nicotianamine
-
mixed inhibition. The preferential inhibition of circulating and tissue angiotensin I-converting enzyme by nicotianamine can contribute to the suppression of hypertension
O-(2,4-difluorobenzyl)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-tyrosine
-
O-(2,4-difluorobenzyl)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-tyrosine
-
O-(3,4-difluorobenzyl)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-tyrosine
-
O-(3,4-difluorobenzyl)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-tyrosine
-
O-(4-fluorobenzyl)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-tyrosine
-
O-(4-fluorobenzyl)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-tyrosine
-
O-benzyl-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-tyrosine
-
O-benzyl-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-tyrosine
-
PCMB
-
1.0 mM, 42% inhibition
peimisine
-
an ACE inhibitory steroidal alkaloid from Fritillaria puqiensis, 20.2% inhibition at 0.2 mM
peimisine
-
IC50: 0.5265 mM
Pepsin
-
-
-
Pepsin
-
about 60% ACE inhibitory
-
peptides
-
purified from sunflower hydrolysate
peptides
-
purified from sunflower hydrolysate or rapeseed hydrolysate
perindopril
-
the angiotensin-converting enzyme inhibitor has no effect on the rate of endothelial apoptosis in vitro in HUVEC cells
perindopril
-
shows beneficial effects, independent of the presence of cardiovascular risk factors at baseline in all study groups, in patients after myocardial infarction and revascularization, detailed overview
perindopril
-
in a murine hepatocellular carcinoma xenograft model perindopril suppresses hepatocellular carcinoma development and inhibits neovascularization
perindopril
-
chronic in vivo administration of the angiotensin-converting enzyme inhibitor reduces apoptosis induced via endotoxic shock with Escherichia coli lipopolysaccharides
perindopril
-
itssue angiotensin converting enzyme inhibitors
perindopril
-
in growing spontaneously hypertensive rats, chronic treatment with perindopril enhances untrained exercise capacity, while it does no affect acquired exercise capacity as a result of exercise training. Perindopril promotes adaptive changes of skeletal muscle in response to exercise such as increases in capillary density and percentage of type I fibre
perindopril
-
chronic administration of perindopril results in a decrease in body adiposity
perindopril
-
decreases food intake and circulating insulin in both diet groups, and hepatic ACE activity in high fat fed animals only, while decreased plasma leptin concentration with ACE inhibition is only evident in chow fed animals
perindoprilat
-
perindoprilat
-
strong inhibitor
Phe-Val-Asn-Pro-Gln-Ala-Gly-Ser
-
-
Phe-Val-Asn-Pro-Gln-Ala-Gly-Ser
-
the peptide corresponds to a fragment of helianthinin, the 11S globulin from sunflower seeds, which is the main storage protein in sunflower. Sunflower seed proteins are a potential source of angiotensin-converting enzyme inhibitory peptides when hydrolyzed with pepsin and pancreatin
phloretin
-
-
phlorofucofuroeckol A
-
derived from Ecklonia stolonifera
phlorofucofuroeckol A
-
derived from Ecklonia stolonifera
phlorotannins
-
e.g. from Ahnfeltiopsis flabelliformis, Ecklonia cava, Ecklonia stolonifera, Pelvetia siliqousa, and Undaria pinnatifida, phenolic compounds formed by the polymerization of phloroglucinol or defined as 1,3,5-trihydroxybenzene monomer units and biosynthesized through the acetate-malonate pathway. They are highly hydrophilic components with a wide range of molecular sizes ranging between 126-650 kDa. A closed ring dibenzo-1,4-dioxin moiety may be crucial for ACE inhibitory effects
-
phlorotannins
-
e.g. from Ahnfeltiopsis flabelliformis, Ecklonia cava, Ecklonia stolonifera, Pelvetia siliqousa, and Undaria pinnatifida, phenolic compounds formed by the polymerization of phloroglucinol or defined as 1,3,5-trihydroxybenzene monomer units and biosynthesized through the acetate-malonate pathway. They are highly hydrophilic components with a wide range of molecular sizes ranging between 126-650 kDa. A closed ring dibenzo-1,4-dioxin moiety may be crucial for ACE inhibitory effects
-
phosphoramidon
-
weak, IC50: 0.001 mM
PO43-
-
100 mM, 50% inhibition
Pro-Thr-His-Ile-Lys-Trp-Gly-Asp
-
inhibitor is isolated from tuna muscle
Pro-Thr-His-Ile-Lys-Trp-Gly-Asp
-
inhibitor is isolated from tuna muscle
protocatechuic acid
-
-
Pyr-Lys-Trp-Ala-Pro
-
i.e. venom bradykinin-potentiating peptide V-3A, hydrolysis of hippuryl-His-Leu
Pyr-Lys-Trp-Ala-Pro
-
mixed type inhibition
Pyr-Trp-Pro-Arg-Pro-Gln-Ile-Pro
-
therapeutical useful
Pyr-Trp-Pro-Arg-Pro-Gln-Ile-Pro
-
i.e. SQ20881, competitive with angiotensin I and hippuryl-L-His-L-Leu
Pyr-Trp-Pro-Arg-Pro-Gln-Ile-Pro-Pro
-
hydrolysis of hippuryl-His-Leu
Pyr-Trp-Pro-Arg-Pro-Gln-Ile-Pro-Pro
-
i.e. SQ20858, competitive with angiotensin I and hippuryl-L-His-L-Leu
pyrogallol
-
-
quercetin
-
-
quercetin
-
IC50: about 2.0 mM
quinapril
-
the angiotensin-converting enzyme inhibitor has no effect on the rate of endothelial apoptosis in vitro in HUVEC cells
quinapril
-
lipophilic ACE inhibitors quinapril, enalapril, and captopril increase the survival and lifetime of rats with experimental chronic heart failure
quinapril
-
the angiotensin-converting enzyme inhibitor has no significant effect on apoptosis induced via endotoxic shock with Escherichia coli lipopolysaccharides
quinapril
-
tissue angiotensin converting enzyme inhibitors
quinapril
-
18 mg/kg quinapril per day feeding for 3 days significantly reduces blood plasma ACE activity by 80%, quinapril administration for 16 days greatly decreases blood plasma ACE activity by 88% with 18 mg/kg per day, ACE activities in the heart, lung, and skeletal muscles of the 16-day ACE-inhibition with 18 mg/kg per day are 9%, 16%, and 22% of the controls, respectively
quinaprilat
-
-
ramipril
-
plasma-ACE activity is almost completely abolished 0.5-2.0 h after treatment with ramipril (0.125, 0.25, 0.5, and 1.0 mg/kg), irrespective of the dose rate, significant inhibition of ACE activity of 54.7 to 82.6% (depending on the dosage) is still present 24 h after treatment, ramipril at a dose rate of 0.125 mg/kg once daily produces significant and long-lasting inhibition of ACE activity in healthy cats
ramipril
-
human physiologically based pharmacokinetic model for the inhibitor
ramipril
-
the angiotensin-converting enzyme inhibitor has no effect on the rate of endothelial apoptosis in vitro in HUVEC cells
ramipril
-
short-term ramipril treatment adequately reduces angiotensin-converting enzyme activity and blood pressure, but has no significant effects on insulin sensitivity, forearm blood flow, substrate fluxes across the forearm, whole-body substrate oxidation and intramuscular triacylglycerol content in obese insulinresistant subjects
ramipril
-
ACE-specific inhibitor
ramipril
-
the ACE inhibitor is associated with a major reduction of proteinuria, slower GFR decline and risk of doubling serum creatinine or progression to end-stage renal disease in patients with nondiabetic kidney disease
ramipril
-
diabetic nephropathy can be delayed by the use of angiotensin-converting enzyme inhibitors. Critical role of bradykinin B2 receptor activation in the mediation of angiotensin-converting enzyme inhibitors renal protection against diabetic nephropathy
ramipril
-
in the early phase of diabetes, the angiotensin-converting enzyme inhibitor reverses glomerular overexpression and activation of some critical growth factor pathways and increases protection against oxidative stress. These effects involve B2-kinin receptor activation
ramipril
-
the angiotensin-converting enzyme inhibitor has no significant effect on apoptosis induced via endotoxic shock with Escherichia coli lipopolysaccharides
ramiprilat
-
-
ramiprilat
-
human physiologically based pharmacokinetic model for the inhibitor
ramiprilat
the ACE inhibitor-induced dimerization of angiotensin-converting enzyme, via the C domain of the enzyme, represents the initial step in the angiotensin-converting enzyme signaling pathway that involves the activation of the JNK/c-Jun pathway and leads to changes in endothelial cell gene expression
resveratrol
-
-
resveratrol
-
IC50: about 1.6 mM
rutin
-
-
RXP407
i.e. Ac-Asp-L-Phe(PO2CH2)-L-Ala-Ala-NH2, a human sACE domain-specific phosphinic peptidyl inhibitor and antihypertensive drug
RXPA380
i.e. (2S)-2-[([2-[(1R)-1-[((benzyloxy)carbonyl)amino]-2-(phenylethyl)(hydroxyl)-phosphinyl]cyclopentyl]carbonyl)amino]-3-(1H-indo-3-yl)-propionic acid (Cbz-PhePSI[P(O)(OH)CH]Pro-Trp-OH), a human sACE domain-specific phosphinic peptidyl inhibitor and antihypertensive drug
RXPA380
C domain-specific inhibitor
SDS
-
-
Ser-Tyr
-
-
snake venom peptide
-
-
-
snake venom peptide
-
of Bothrops jararaca
-
syringic acid
-
-
Tannic acid
-
-
Teprotide
-
from snake venom peptides
Teprotide
-
i.e. SQ 20881
trandolapril
-
the angiotensin-converting enzyme inhibitor has no effect on the rate of endothelial apoptosis in vitro in HUVEC cells
trandolapril
-
the angiotensin-converting enzyme inhibitor has no significant effect on apoptosis induced via endotoxic shock with Escherichia coli lipopolysaccharides
trandolaprilat
-
trans-cinnamic acid
-
-
Trp-Leu
-
-
Trp-Leu
-
IC50: 0.0341 mM, non-competitive
Trp-Pro-Glu-Ala-Ala-Glu-Leu-Met-Met-Glu-Val-Asp-Pro
-
noncompetitive inhibitor
Trp-Pro-Glu-Ala-Ala-Glu-Leu-Met-Met-Glu-Val-Asp-Pro
-
noncompetitive inhibitor.The peptide has an antihypertensive effect according to the time-course measurement after oral administration to spontaneously hypertensive rats. Maximal reduction is detected 3 h after oral administration at a dose of 10 mg/kg of body weight
Trypsin
-
-
-
Trypsin
-
about 10% ACE inhibitory
-
Val-Leu-Ile-Val-Pro
-
-
Val-Leu-Ile-Val-Pro
-
IC50: 0.00169 mM. The peptide is resistant to digestion by proteases of the gastrointestinal tract. The antihypertensive property of this peptide derived from glycinin might find importance in the development of therapeutic functional foods
Val-Pro-Pro
-
-
Val-Pro-Pro
-
casein hydrolysate containing VPP and IPP improves the vascular endothelial dysfunction in subjects with mild hypertension. The continuous intake of VPP and IPP could help to prevent cardiovascular diseases in hypertensive subjects
Val-Trp
-
IC50: 3.311 mM
Val-Trp
-
IC50: 0.0025 mM, uncompetitive
Val-Tyr
-
IC50: 0.263 mM
vanillic acid
-
-
[[(2S)-2-mercapto-3-methylpentanoyl]amino]acetic acid
-
[[(2S)-2-mercapto-3-methylpentanoyl]amino]acetic acid
-
additional information
-
enzyme is not affected by addition of 0.1-1.0 mM CaCl2, Mn2Cl2, MgCl2 or 0.1 mM ZnCl2
-
additional information
-
hot water extract of Tamogi-take mushroom, IC50: 6 mg/ml
-
additional information
-
design and properties of N-carboxyalkyldipeptide inhibitors
-
additional information
-
-
-
additional information
-
angiotensin-converting enzyme inhibitors are recommended in dogs and cats with chronic renal failure. They decrease the glomerular capillary pressure, have antiproteinuric effects, tend to delay the progression of chronic renal failure and to limit the extent of renal lesions
-
additional information
-
design and properties of N-carboxyalkyldipeptide inhibitors
-
additional information
-
-
-
additional information
-
-
-
additional information
-
angiotensin-converting enzyme inhibitors are recommended in dogs and cats with chronic renal failure. They decrease the glomerular capillary pressure, have antiproteinuric effects, tend to delay the progression of chronic renal failure and to limit the extent of renal lesions
-
additional information
-
synthetic peptides derived from human collagen XVIII hinge domain with sequences similar to bradykinin potentiating peptides from snake venom
-
additional information
-
inhibition by food extract solution from garlic, buckwheat, mushroom, soy sauce, Tokuho A, Tokuho B
-
additional information
-
inhibition of angiotensin converting enzyme seems to augment catabolism of calcitonin gene related peptide
-
additional information
-
plant methanol extracts from Amaranthus dubius, Amaranthus hybridus, Asystasia gangetica, Galinsoga parviflora, Justicia flava, Oxygonum sinuatum, Physalis viscosa, and Tulbaghia violacea show ACE inhibitory activities
-
additional information
-
angiotensin-converting enzyme inhibition does not significantly modify major biomarkers of inflammation, hemostasis, and endothelial function, e.g. C-reactive protein, interleukin 6, plasminogen activator inhibitor 1, vascular cell adhesion molecule 1, and endothelin 1, while angiotensin II levels are reduced, overview
-
additional information
-
the enzyme inhibition by angiotensin-converting enzyme inhibitors is inhibited by aspirin, which can cause therapeutic problems during application of both in treatment of heart failure patients. Angiotensin receptor blockers do not interfere with the bradykinin pathway, detailed overview
-
additional information
-
angiotensin-converting enzyme inhibitors, ACEIs, treatment of myocardial infarction patients bears is asscoiated with increased mortality, the risk is also existent for renal failure patients, effects of ACEIs on heart failure patients with other diseases or risk factors, overview
-
additional information
-
ACE inhibitors can induce angioedema, overview; ACE-inhibitors in vivo act in a competitive manner and their activity is dependent on their plasma concentration
-
additional information
-
angiotensin-converting enzyme inhibitors, ACE-I, protect against cardiac toxicity in patients receiving doxorubicin chemotherapy, overview
-
additional information
-
both angiotensin-converting enzyme inhibitors and angiotensin receptor blockers, e.g. losartan, can slow the progression of diabetic nephropathy, overview
-
additional information
-
angiotensin converting enzyme inhibitors inhibit angiotensin II formation and affect the bradykinin B1 and B2 receptor, B2R and B2R, signaling, overview. They indirectly potentiate the actions of bradykinin and enzyme-resistant analogues of bradykinin on receptor BR2R, leading to increased release of arachidonic acid and NO, and they increase B2R action as allosteric enhancers, via their C-domain, inducing a conformational change in the enzyme. The inhibitors are useful in therapy of cardiovascular diseases, overview. The bradykinin B1 receptor is directly activated by ACE inhibitors, even in absence of ACE
-
additional information
-
isoflavones from soymilk may have inhibitory potency to affect ACE
-
additional information
-
inhibition of angiotensin-converting enzyme, or angiotensin II receptor blockage, slows down the progression of renal disease and provide a renal-protective effect. Therefore, they are used in therapy of type 2 diabetes, the main cause of end-stage renal disease in Europe and the United States, antagonizing the diabetic nephropathy progresses, overview
-
additional information
-
mass spectrometric and structural analysis, and production and purification of plant food-derived ACE inhibitory peptides, bioactivities, overview
-
additional information
-
generation of angiotensin I-converting enzyme inhibitory, ACEI, peptides after gastrointestinal digestion of pork meat by the action of pepsin and pancreatin at simulated gut conditions, analysis by nanoLC-ESI-MS/MS and MALDI-TOF/TOF mass spectrometry, and peptide sequencing, overview
-
additional information
-
generation of ACE inhibitory peptides from flaxseed protein, molecular weights and inhibitory potencies of fractions, overview
-
additional information
-
quantitative retention-activity relationship models of ACE inhibitors using biopartitioning micellar chromatography, method evaluation, overview
-
additional information
-
treatment with ACE inhibitors can induce chronic cough in many patients
-
additional information
-
nutrient sources of ACE inhibitory peptides derived from marine organisms, enzymes used for hydrolysis, and IC50 values, overview. Tryptophan, tyrosine, proline or phenylalanine at the C-terminal and branched-chain aliphatic amino acids at the N-terminal is suitable for peptides to act as competitive inhibitors by binding with ACE, some peptides also show a non-competitive mechanism. Hydrophobicity of the N-terminus, which is one of the common features of ACE inhibitory peptides, may contribute to the inhibitory activity. The peptides exhibit antihypertensive activity in vivo rather than in vitro. Polyphenolic compounds inhibit ACE activity through sequestration of the enzyme metal factor, Zn2+ ion
-
additional information
-
antiproteinuric and renoprotective effects of ACE inhibitors, ACEi, overview
-
additional information
-
inhibitory potencies of tripeptides derived from arachin, the major storage globulin of peanut, Arachis hypogaea variety TMV-2, sequence analysis, overview. Active site biniding and the degree of inhibition by the peptides correlates with the coordination distance between the catalytic Zn2+ and the carbonyl oxygen of the peptide bond between the amino-terminal and middle residue
-
additional information
-
use of ACE inhibitor is associated with a significant decrease in long-term mortality and cardiovascular events in the patients with diastolic heart failure
-
additional information
monoclonal antibosies mAbs 9B9 and 3G8 prevent ACE dimerization in vitro in reverse micelles, and only mAb 3G8 inhibits ACE shedding from the cell surface
-
additional information
whole horse gram flour (HGH), from seeds of Macrotyloma uniflorum, has ACE inhibitory potency, 77% inhibition, the highest ACE inhibitory activity is demonstrated by DH40 hydrolysate, increase in inhibition capacity as degree of hydrolysis progresses
-
additional information
inhibition of ACE activity with anti-catalytic anti-ACE monoclonal antibodies, development and inhibition analysis with enzyme from different tissues, overview
-
additional information
-
inhibition of ACE activity with anti-catalytic anti-ACE monoclonal antibodies, development and inhibition analysis with enzyme from different tissues, overview
-
additional information
-
design and properties of N-carboxyalkyldipeptide inhibitors
-
additional information
-
-
-
additional information
-
inhibitors that occur naturally in body fluids
-
additional information
-
the two homologous domains of human angiotensin I-converting enzyme interact differently with competitive inhibitors
-
additional information
-
design and properties of N-carboxyalkyldipeptide inhibitors
-
additional information
-
inhibitory peptide from Alaska pollack (Theragra chalcogramma) frame protein hydrolysate
-
additional information
-
inhibitory peptides from in vitro pepsin-pancreatin digestion of soy protein
-
additional information
-
the purified mucilage of storage roots (Ipomoea batatas (L.) Lam. Tainong 57) exhibits dose-dependent ACE inhibitory activity in vitro. The mucilage acted as a mixed type inhibitor toward ACE with an IC50 of 0.3645 mg/ml
-
additional information
-
the immobilized enzyme is used to purify inhibitory peptides from sunflower
-
additional information
-
simultaneous determination of angiotensin I-converting enzyme inhibitory peptides in tryptic casein hydrolysate by high-performance liquid chromatography combined with a replicate heart-cut column-switching technique
-
additional information
-
inhibitory peptide is isolated from tuna dark muscle hydrolysate prepared by alcalase, neutrase, pepsin, papain, alpha-chymotrypsin, and trypsin, respectively. Among hydrolysates, the pepsin-derived hydrolysate exhibited the highest ACE I inhibitory activity versus those of other enzyme hydrolysates. The structure of the peptide is identified to be Trp-Pro-Glu-Ala-Ala-Glu-Leu-Met-Met-Glu-Val-Asp-Pro
-
additional information
-
yak milk casein could be a resource to generate antihypertensive peptides
-
additional information
-
trichloroacetic acid filtrates of lactic acid bacteria (Lactobacillus casei 2607, Lactobacillus casei 15286, Lactobacillus acidophilus 4461, Lactobacillus acidophilus 33200, Streptococcus thermophilus 1275, Streptococcus thermophilus 285, Lactobacillus delbrueckii ssp. bulgaricus 1092, Lactobacillus delbrueckii ssp. bulgaricus 1368, Bifidobacterium longum 5022) show inhibitory activity
-
additional information
-
isolation and characterization of angiotensin I-converting enzyme inhibitory peptides derived from porcine hemoglobin. IC50-vlue for pepsin is 1.19 mg/ml, IC50-value for trypsin is 8.79 mg/ml, IC50-value for papain is 2.21 mg/ml
-
additional information
-
pacific hake (Merluccius productus) fillet hydrolysate demonstrates in vitro ACE-inhibitory activity (IC50 0.165 mg/ml), which is enhanced by ultrafiltration through a 10 kDa molecular weight cutoff membrane (IC50 0.044 mg/ml), PeptACE peptides and the unfractionated pacific hake (Merluccius productus) fillet hydrolysate show significantly greater ACE inhibitory activity (i.e., significantly lower IC50 values) after simulated gastrointestinal digestion and may therefore be considered as prodrug type inhibitors
-
additional information
-
chicken collagen hydrolysates possess ACE-inhibitory activities, chicken collagen hydrolysates inhibit about 30% of the activity of ACE, whereas further enzymatic treatment doubles their activities
-
additional information
-
autolysis of protein isolates from vascular bundle and inner tuber tissues of potato (Solanum tuberosum) enhances the inhibition of the angiotensin converting enzyme I, the highest inhibitory activities (50% reduction in ACE activity achieved following autolysis at a protein concentration of 0.36 mg/ml) are measured in tubers after 5-6 months of storage prior to sprouting, the rate of ACE inhibition is positively correlated with protease activity in tuber tissues
-
additional information
-
soybean flour hydrolysate and soybean ACE inhibitory peptides have an inhibitory effect towards ACE, adding isoflavones into both soybean flour hydrolysate and soybean ACE inhibitory peptide samples to a concentration of as high as 31.5% (w/w) does not affect ACE inhibitory activity
-
additional information
-
ACE is not inhibited by gluco-obtusifolin, obtusifolin, aurantioobtusin, cassitoroside, toralactone gentiobioside, chrysophanol triglucoside, questin, and cassiaside; both of the methanol extracts from the raw and roasted Cassia tora seeds exhibit significant inhibitory properties against ACE, demonstrating more than 50% inhibition at a concentration of 0.16393 mg/ml
-
additional information
-
inhibitor structure-activity relationship, overview
-
additional information
-
ACE inhibitory peptides from the marine rotifer, Brachionus rotundiformis, overview. The hydrolysate is prepared by Alcalase, a-chymotrypsin, Neutrase, papain, and trypsin, inhibitory activities of the different preparateions, overview. Glutamic acid, aspartic acid, proline, glycine and alanine from ACE inhibitory activity peptide are all observed in many other ACE inhibitory peptides. Peptides derived from rotifers may be beneficial as anti-hypertension compounds in functional foods resource
-
additional information
-
ACE-inhibitory protein hydrolysates produced from canola meals, after hydrolysis by different enzymes, IC50 of molecular weight fractions, overview
-
additional information
-
no inhibition by flavonoid glycosides, isolated from flower buds of Rosa damascena, kaempferol-3-O-beta-D-glucopyranosyl-(1,4)-beta-D-xylopyranoside, i.e. roxyloside A, isoquercitrin, quercetin gentiobioside, and afzelin
-
additional information
-
screening of ACE inhibitors using the spectrocolorimetric assay method with synthetic substrate 3-hydroxybutyrylglycyl-glycyl-glycine, assay method development and optimization, detailed overview
-
additional information
enzyme inhibition kinetics and moelecular docking of patatin-derived peptides. The higher inhibitory potency of PRY might be attributed to formation of more hydrogen bonds with the enzyme's active site or non-active sites that distort the configuration necessary for catalysis
-
additional information
-
design and properties of N-carboxyalkyldipeptide inhibitors
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
the presence of verticione, verticine, peimisine may be responsible, at least in part, for the antihypertensive action of the bulbs of Fritillaria ussuriensis
-
additional information
-
isolation of angiotensin converting enzyme (ACE) inhibitory flavonoids from Sedum sarmentosum
-
additional information
-
hot water extract of Tamogi-take mushroom, antihypertensive effect in spontaneously hypertensive rats by oral administration
-
additional information
-
tissue angiotensin converting enzyme inhibitors exert more pronounced antithrombotic effect than plasma ACE-Is in experimental thrombosis
-
additional information
-
angiotensin I-converting enzyme inhibitory peptides from protein hydrolysates by a soybean protease D3
-
additional information
-
not inhibited by MLN4760, SCH39370, amastatin bestatin, chymostatin, and p-chloromercuribenzoate
-
additional information
-
chicken collagen hydrolysates possess ACE-inhibitory activities, chicken collagen hydrolysates inhibit about 30% of the activity of ACE, whereas further enzymatic treatment doubles their activities
-
additional information
-
not inhibited by resveratrol
-
additional information
-
2.7fold peptide-enriched soy sauce-like seasoning, termed Fermented Soybean Seasoning, FSS, shows ACE inhibitory activity with an IC50 of 0.454 mg/ml, fermentation method, overview. FSS shows antihypertensive effects, overview
-
additional information
-
ACE inhibitory peptides derived from marine organisms show a strong suppressive effect on systolic blood pressure of spontaneously hypertensive rats, and this antihypertensive activity is similar with captopril, a commercial antihypertensive drug. Hydrophobicity of the N-terminus is one of the common features of ACE inhibitory peptides, and may contribute to the inhibitory activity. No side effect observed on rats after administration of antihypertensive peptides. The peptides exhibit antihypertensive activity in vivo rather than in vitro. An antihypertensive peptide isolated from bonito fish hydrolysate product, is hydrolyzed by ACE to produce a smaller peptide than the initial one, which has 8fold increased ACE inhibitory activity compared with the initial peptide. Polyphenolic compounds inhibit ACE activity through sequestration of the enzyme metal factor, Zn2+ ion
-
additional information
-
metabolic effects of low dose angiotensin converting enzyme inhibitor in dietary obesity in the rat
-
additional information
effects of metabolites produced from (-)-epigallocatechin gallate by rat intestinal bacteria on angiotensin I-converting enzyme activity and blood pressure in spontaneously hypertensive rats. All of the metabolites show ACE inhibitory activities and the order of IC50 is hydroxyphenyl valeric acids > 5-(3,4,5-trihydroxyphenyl)-gamma-valerolactone > 5-(3,4,5-trihydroxyphenyl) 4-hydroxyvaleric acid >> 5-(3,5-dihydroxyphenyl) 4-hydroxyvaleric acid >> 5-(3,5-dihydroxyphenyl)-gamma-valerolactone. Among the catechins, galloylated catechins exhibit stronger ACE inhibitory activity than nongalloylated catechins. Measurement of systolic blood pressure (SBP) after oral administration
-
additional information
-
design and properties of N-carboxyalkyldipeptide inhibitors
-
additional information
-
-
-
additional information
-
endogenous inhibitor from rat heart may modulate the activity of the enzyme in the heart in response to alterations of the oxidation-reduction balance in the tissue, MW of the inhibitor is about 100000 Da
-
additional information
PMSF has no effect on the ACE activity
-
additional information
-
compounds from Epilobium angustifolium inhibit. Taking into account the role of these peptidase in prostate diseases, the results may partly support and explain the use of Epilobium extracts in folk medicine
-
additional information
-
the immobilized lung extract is used to purify inhibitory peptides from sunflower and rapeseed protein hydrolysates that has been obtained by treatment of protein isolates with alcalase
-
additional information
-
preparation ACE inhibitor peptides from the enzymatic hydrolysis of arachin, the major storage protein of Arachis hypogaea, overview
-
additional information
-
inhibitory potencies of tripeptides derived from arachin, the major storage globulin of peanut, Arachis hypogaea variety TMV-2, sequence analysis, overview. Active site biniding and the degree of inhibition by the peptides correlates with the coordination distance between the catalytic Zn2+ and the carbonyl oxygen of the peptide bond between the amino-terminal and middle residue. In vitro stability of the peptides to gastrointestinal proteases, overview
-
additional information
-
design and properties of N-carboxyalkyldipeptide inhibitors
-
additional information
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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0.08 - 0.174
2-furanacryloyl-Phe-Gly-Gly
0.23 - 0.25
2-furylacryloyl-Phe-Gly-Gly
28.54
3-hydroxybutyryl-Gly-Gly-Gly
-
37°C
0.0055
Abz-FRK(Dnp)P-OH
-
pH 9.5, 37°C
0.0065 - 0.012
Abz-LFK(Dnp)-OH
0.035
Abz-SDK(Dnp)P-OH
-
pH 7.4, 37°C
0.069
acetyl-His-Pro-(NO2)Phe-His-Leu
-
-
0.007
amyloid beta-protein 1-42
-
-
-
0.009 - 2.7
angiotensin I
0.002
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met
-
-
0.58
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Tyr-Arg
Drosophila sp. (in: flies)
-
35°C, pH 8.0
0.073
Arg-Pro-Pro-Gly-Phe-Thr-Pro-Phe-Arg
Drosophila sp. (in: flies)
-
35°C, pH 8.0
0.0097
Asn-Arg-Val-Tyr-Ile-His-Pro-(NO2)Phe-His-Leu
-
-
3.4
benzoyl-Gly-Ala-His-Leu
-
-
2.1
benzoyl-Gly-Ala-Leu
-
-
7.19
benzoyl-Gly-Ala-Pro
-
-
2.7
benzoyl-Gly-Arg-His-Leu
-
-
1.3
benzoyl-Gly-Arg-Leu
-
-
4.9
benzoyl-Gly-Glu-Leu
-
-
6.2
benzoyl-Gly-Gly-Gly
-
-
4.9
benzoyl-Gly-His-Ala
-
-
0.12
benzoyl-Gly-His-Arg
-
-
0.56 - 18.2
benzoyl-Gly-His-Leu
5.2
benzoyl-Gly-His-Phe
-
-
4.4
benzoyl-Gly-Ile-His-Leu
-
-
0.6
benzoyl-Gly-Phe-Arg
-
-
0.89
benzoyl-Gly-Phe-His-Leu
-
-
2.1
benzoyl-Gly-Phe-Leu
-
-
4.6
benzoyl-Gly-Pro-His-Leu
-
-
2.3
benzoyl-Gly-Ser-His-Leu
-
-
0.067
benzyloxycarbonyl-(NO2)Phe-His-Leu
-
-
0.13 - 2.8
benzyloxycarbonyl-Phe-His-Leu
0.047
Gly-Ile-His-Pro-(NO2)Phe-His-Leu
-
-
0.057
Gly-Pro-(NO2)Phe-His-Leu
-
-
0.9
hippuryl-Gly-Gly
-
pH 6, 0.1 M NaCl
0.0308 - 20
hippuryl-His-Leu
5
hippuryl-L-His-L-Leu
-
-
0.5 - 1.8
hippuryl-Phe-Arg
0.067
His-Pro-(NO2)Phe-His-Leu
-
-
0.3
Ile-Ser-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
Drosophila sp. (in: flies)
-
35°C, pH 8.0
0.0045
Mca-RPPGFSAFK(Dnp)-OH
-
pH 7.4, 37°C
0.37
MKRSRGPSPRR
Drosophila sp. (in: flies)
-
35°C, pH 8.0
0.05
N-(3-(2-furyl)acryloyl)-Phe-Ala-Ala
-
pH 7.5, 25°C, enzyme from testis
0.14 - 0.17
N-(3-(2-furyl)acryloyl)-Phe-Ala-Lys
0.005 - 0.008
N-(3-(2-furyl)acryloyl)-Phe-Ala-Pro
0.5 - 0.98
N-(3-(2-furyl)acryloyl)-Phe-Gly-Gly
0.05 - 0.12
N-(3-(2-furyl)acryloyl)-Phe-Phe-Arg
0.08
N-(3-[2-furyl]acryloyl)-L-phenylalanylglycylglycine
pH 7.5, 22°C
0.125 - 0.6
N-benzyloxycarbonyl-L-Phe-L-His-L-Leu
1.16 - 1.8
N-hippuryl-His-Leu
0.01472 - 0.5237
NKLKPSQWI
0.0027 - 0.1505
NKLKPSQWISL
0.1367 - 0.6738
NKLKPSQWISLSD
0.011 - 0.0248
o-aminobenzoyl-FDK-(dinitrophenyl)-P-OH
0.0027 - 0.004
o-aminobenzoyl-FRK-(dinitrophenyl)-P-OH
0.001 - 0.002
o-aminobenzoyl-GFSPFAQ-(N-2,4-dinitrophenyl)ethylenediamine
0.0016
o-aminobenzoyl-GFSPFEQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, wild-type enzyme
0.0024 - 0.0037
o-aminobenzoyl-GFSPFFQ-(N-2,4-dinitrophenyl)ethylenediamine
0.0021 - 0.0034
o-aminobenzoyl-GFSPFLQ-(N-2,4-dinitrophenyl)ethylenediamine
0.00006 - 0.0011
o-aminobenzoyl-GFSPFQQ-(N-2,4-dinitrophenyl)ethylenediamine
0.0013 - 0.0018
o-aminobenzoyl-GFSPFRA-(N-2,4-dinitrophenyl)ethylenediamine
0.0007 - 0.0014
o-aminobenzoyl-GFSPFRF-(N-2,4-dinitrophenyl)ethylenediamine
0.0014 - 0.0024
o-aminobenzoyl-GFSPFRI-(N-2,4-dinitrophenyl)ethylenediamine
0.0009 - 0.005
o-aminobenzoyl-GFSPFRN-(N-2,4-dinitrophenyl)ethylenediamine
0.0016 - 0.006
o-aminobenzoyl-GFSPFRQ-(N-2,4-dinitrophenyl)ethylenediamine
0.0009 - 0.0014
o-aminobenzoyl-GFSPFRR-(N-2,4-dinitrophenyl)ethylenediamine
0.0007 - 0.003
o-aminobenzoyl-GFSPFRS-(N-2,4-dinitrophenyl)ethylenediamine
0.0021 - 0.0025
o-aminobenzoyl-GFSPFSQ-(N-2,4-dinitrophenyl)ethylenediamine
0.017 - 0.032
o-aminobenzoyl-SDK-(dinitrophenyl)-P-OH
0.0144 - 0.0229
o-aminobenzoyl-SRK-(dinitrophenyl)-P-OH
0.0154 - 0.0609
o-aminobenzoyl-TDK-(dinitrophenyl)-P-OH
0.0031 - 0.0102
o-aminobenzoyl-TRK-(dinitrophenyl)-P-OH
0.0051 - 0.015
o-aminobenzoyl-YDK-(dinitrophenyl)-P-OH
0.0047 - 0.0051
o-aminobenzoyl-YRK-(dinitrophenyl)-P-OH
0.146
Pro-(NO2)Phe-His-Leu
-
-
0.108 - 0.3117
SLKPSNWLTPSE
0.0381
TOAC1-angiotensin I
-
-
0.0472
TOAC3-angiotensin I
-
-
0.023
Tyr-Ile-His-Pro-(NO2)Phe-His-Leu
-
-
0.044 - 0.22
[Arg10]angiotensin I
0.011 - 0.025
[Phe9,Arg10]angiotensin I
0.032 - 0.056
[Phe9]angiotensin I
additional information
additional information
-
0.08
2-furanacryloyl-Phe-Gly-Gly
-
pH 7.5, 20°C
0.136
2-furanacryloyl-Phe-Gly-Gly
-
wild-type enzyme
0.174
2-furanacryloyl-Phe-Gly-Gly
-
recombinant enzyme
0.23
2-furylacryloyl-Phe-Gly-Gly
-
pH 7.5, 25°C
0.25
2-furylacryloyl-Phe-Gly-Gly
-
pH 7.5, 25°C, cobalt-ACE
0.0065
Abz-LFK(Dnp)-OH
-
pH 9.5, 37°C
0.012
Abz-LFK(Dnp)-OH
-
pH 7.4, 37°C
0.009
angiotensin I
-
enzyme from lung and testis
0.016
angiotensin I
-
recombinant enzyme
0.04
angiotensin I
-
pH 7.5, 37°C, enzyme from brain, 200 mM NaCl
0.052
angiotensin I
-
37°C, pH 7.5, wild-type enzyme
0.062
angiotensin I
-
lung enzyme
0.065
angiotensin I
-
detergent-solubilized enzyme
0.067
angiotensin I
-
37°C
0.076
angiotensin I
-
kidney enzyme
0.076
angiotensin I
-
serum enzyme
0.078
angiotensin I
-
lung enzyme
0.078
angiotensin I
-
trypsin-extracted enzyme
0.09
angiotensin I
-
enzyme from testis and lung
0.1
angiotensin I
-
37°C, pH 7.5, mutant enzyme R1098Q
0.21
angiotensin I
-
pH 7.5, 0.2 mM NaCl
0.42
angiotensin I
-
pH 9.0, 0.5 mM NaCl
0.54
angiotensin I
-
pH 6.0, without NaCl
0.82
angiotensin I
Drosophila sp. (in: flies)
-
35°C, pH 7.0, 100 mM NaCl
1.04
angiotensin I
Drosophila sp. (in: flies)
-
35°C, pH 8.0, 100 mM NaCl
1.23
angiotensin I
Drosophila sp. (in: flies)
-
35°C, pH 8.0, 0 mM NaCl
2.7
angiotensin I
Drosophila sp. (in: flies)
-
35°C, pH 7.0, 0 mM NaCl
0.56
benzoyl-Gly-His-Leu
-
-
1.2
benzoyl-Gly-His-Leu
-
-
1.2
benzoyl-Gly-His-Leu
-
-
1.3
benzoyl-Gly-His-Leu
-
-
18.2
benzoyl-Gly-His-Leu
-
-
0.13
benzyloxycarbonyl-Phe-His-Leu
-
pH 7.5, 25°C, enzyme from testis
0.14
benzyloxycarbonyl-Phe-His-Leu
-
pH 7.5, 25°C
0.3
benzyloxycarbonyl-Phe-His-Leu
37°C, pH 8.3, chimeric enzyme C583-623Ndom-ACE
0.3
benzyloxycarbonyl-Phe-His-Leu
37°C, pH 8.3, N-domain of tACE
0.4
benzyloxycarbonyl-Phe-His-Leu
-
pH 7.5
0.4
benzyloxycarbonyl-Phe-His-Leu
37°C, pH 8.3, chimeric enzyme C1-163Ndom-ACE
1.2
benzyloxycarbonyl-Phe-His-Leu
37°C, pH 8.3, ACE
2.8
benzyloxycarbonyl-Phe-His-Leu
37°C, pH 8.3, chimeric enzyme C417579Ndom-ACE
0.0004
bradykinin
-
-
0.27
bradykinin
Drosophila sp. (in: flies)
-
35°C, pH 8.0
0.0308
hippuryl-His-Leu
-
-
0.32
hippuryl-His-Leu
-
detergent-solubilized enzyme
0.5
hippuryl-His-Leu
37°C, pH 8.3, N-domain of tACE
0.52
hippuryl-His-Leu
-
trypsin-extracted enzyme
0.6
hippuryl-His-Leu
-
100 mM borate/sodium carbonate buffer, pH 7.8
1
hippuryl-His-Leu
-
Tris-NaCl buffer
1.1
hippuryl-His-Leu
-
10 mM potassium phosphate buffer, pH 8.3, enzyme form I, II, and III
1.1
hippuryl-His-Leu
37°C, pH 8.3, chimeric enzyme C1-163Ndom-ACE
1.1
hippuryl-His-Leu
37°C, pH 8.3, chimeric enzyme C583623Ndom-ACE
1.1
hippuryl-His-Leu
37°C, pH 8.3, tACE
1.2
hippuryl-His-Leu
-
lung enzyme
1.468
hippuryl-His-Leu
pH 7.5, temperature not specified in the publication
1.54
hippuryl-His-Leu
-
recombinant enzyme
1.61
hippuryl-His-Leu
-
wild-type enzyme
1.7
hippuryl-His-Leu
-
enzyme from kidney
1.8
hippuryl-His-Leu
-
kidney enzyme
1.9
hippuryl-His-Leu
-
enzyme from lung
2.6
hippuryl-His-Leu
-
enzyme from lung and testis
2.7
hippuryl-His-Leu
37°C, pH 8.3, chimeric enzyme C417-579Ndom-ACE
2.9
hippuryl-His-Leu
-
serum enzyme
3
hippuryl-His-Leu
-
phosphosaline buffer
3.1
hippuryl-His-Leu
-
lung enzyme
4
hippuryl-His-Leu
-
heart enzyme
0.5
hippuryl-Phe-Arg
-
heart enzyme
0.7
hippuryl-Phe-Arg
-
lung enzyme
1.8
hippuryl-Phe-Arg
-
kidney enzyme
0.0157
LEQIYHL
-
pH 7.0, N-domain
0.0347
LEQIYHL
-
pH 7.0, somatic enzyme
0.1592
LEQIYHL
-
pH 7.0, C-domain
0.014
LVVYPWTQRY
-
pH 7.5, 37°C, enzyme from testis, 200 mM NaCl
0.015
LVVYPWTQRY
-
pH 7.5, 37°C, enzyme from brain, 200 mM NaCl
0.019
LVVYPWTQRY
-
pH 7.5, 37°C, enzyme from brain, 10 mM NaCl
0.033
LVVYPWTQRY
-
pH 7.5, 37°C, enzyme from testis, 10 mM NaCl
0.14
N-(3-(2-furyl)acryloyl)-Phe-Ala-Lys
-
pH 7.5, 25°C, N-domain from lung enzyme
0.15
N-(3-(2-furyl)acryloyl)-Phe-Ala-Lys
-
pH 7.5, 25°C, enzyme from lung
0.17
N-(3-(2-furyl)acryloyl)-Phe-Ala-Lys
-
pH 7.5, 25°C, enzyme from testis
0.005
N-(3-(2-furyl)acryloyl)-Phe-Ala-Pro
-
pH 7.5, 25°C, enzyme from testis
0.008
N-(3-(2-furyl)acryloyl)-Phe-Ala-Pro
-
pH 7.5, 25°C, enzyme from lung
0.008
N-(3-(2-furyl)acryloyl)-Phe-Ala-Pro
-
pH 7.5, 25°C, N-domain from lung enzyme
0.5
N-(3-(2-furyl)acryloyl)-Phe-Gly-Gly
-
pH 7.5, 25°C, enzyme from testis
0.98
N-(3-(2-furyl)acryloyl)-Phe-Gly-Gly
-
pH 7.5, 25°C
0.05
N-(3-(2-furyl)acryloyl)-Phe-Phe-Arg
-
pH 7.5, 25°C, enzyme from lung
0.05
N-(3-(2-furyl)acryloyl)-Phe-Phe-Arg
-
pH 7.5, 25°C, N-domain from lung enzyme
0.1
N-(3-(2-furyl)acryloyl)-Phe-Phe-Arg
-
pH 7.5, 25°C
0.12
N-(3-(2-furyl)acryloyl)-Phe-Phe-Arg
-
pH 7.5, 25°C, enzyme from testis
0.125
N-benzyloxycarbonyl-L-Phe-L-His-L-Leu
-
-
0.6
N-benzyloxycarbonyl-L-Phe-L-His-L-Leu
-
pH 7.5, 25°C, enzyme from testis
1.16
N-hippuryl-His-Leu
-
kinetic study by capillary electrophoresis
1.8
N-hippuryl-His-Leu
-
pH 7.5, 25°C
0.0753
NKLKPSQ
-
pH 7.0, N-domain
0.0905
NKLKPSQ
-
pH 7.0, somatic enzyme
0.01472
NKLKPSQWI
-
pH 7.0
0.0622
NKLKPSQWI
-
pH 7.0, N-domain
0.0815
NKLKPSQWI
-
pH 7.0, somatic enzyme
0.5237
NKLKPSQWI
-
pH 7.0, C-domain
0.0027
NKLKPSQWISL
-
pH 7.0
0.0069
NKLKPSQWISL
-
pH 7.0, N-domain
0.017
NKLKPSQWISL
-
pH 7.0, somatic enzyme
0.1505
NKLKPSQWISL
-
pH 7.0, C-domain
0.1367
NKLKPSQWISLSD
-
pH 7.0, somatic enzyme
0.2314
NKLKPSQWISLSD
-
pH 7.0, N-domain
0.459
NKLKPSQWISLSD
-
pH 7.0
0.6738
NKLKPSQWISLSD
-
pH 7.0, C-domain
0.011
o-aminobenzoyl-FDK-(dinitrophenyl)-P-OH
-
pH 8.0, 37°C, wild-type enzyme
0.0187
o-aminobenzoyl-FDK-(dinitrophenyl)-P-OH
-
pH 8.0, 37°C, N-domain
0.0248
o-aminobenzoyl-FDK-(dinitrophenyl)-P-OH
-
pH 8.0, 37°C, C-domain
0.0027
o-aminobenzoyl-FRK-(dinitrophenyl)-P-OH
-
pH 8.0, 37°C, C-domain
0.0034
o-aminobenzoyl-FRK-(dinitrophenyl)-P-OH
-
pH 8.0, 37°C, N-domain
0.004
o-aminobenzoyl-FRK-(dinitrophenyl)-P-OH
-
pH 8.0, 37°C, wild-type enzyme
0.001
o-aminobenzoyl-GFSPFAQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, N-domain
0.0013
o-aminobenzoyl-GFSPFAQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, wild-type enzyme
0.002
o-aminobenzoyl-GFSPFAQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, C-domain
0.0024
o-aminobenzoyl-GFSPFFQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, N-domain
0.0026
o-aminobenzoyl-GFSPFFQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, wild-type enzyme
0.0037
o-aminobenzoyl-GFSPFFQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, C-domain
0.0021
o-aminobenzoyl-GFSPFLQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, wild-type enzyme
0.003
o-aminobenzoyl-GFSPFLQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, N-domain
0.0034
o-aminobenzoyl-GFSPFLQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, C-domain
0.00006
o-aminobenzoyl-GFSPFQQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, N-domain
0.0009
o-aminobenzoyl-GFSPFQQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, C-domain
0.0011
o-aminobenzoyl-GFSPFQQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, wild-type enzyme
0.0013
o-aminobenzoyl-GFSPFRA-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, wild-type enzyme
0.0014
o-aminobenzoyl-GFSPFRA-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, C-domain
0.0018
o-aminobenzoyl-GFSPFRA-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, N-domain
0.0007
o-aminobenzoyl-GFSPFRF-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, N-domain
0.0011
o-aminobenzoyl-GFSPFRF-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, C-domain
0.0014
o-aminobenzoyl-GFSPFRF-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, wild-type enzyme
0.0014
o-aminobenzoyl-GFSPFRI-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, N-domain
0.0015
o-aminobenzoyl-GFSPFRI-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, wild-type enzyme
0.0024
o-aminobenzoyl-GFSPFRI-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, C-domain
0.0009
o-aminobenzoyl-GFSPFRN-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, wild-type enzyme
0.0033
o-aminobenzoyl-GFSPFRN-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, C-domain
0.005
o-aminobenzoyl-GFSPFRN-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, N-domain
0.0016
o-aminobenzoyl-GFSPFRQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, wild-type enzyme
0.003
o-aminobenzoyl-GFSPFRQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, N-domain
0.006
o-aminobenzoyl-GFSPFRQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, C-domain
0.0009
o-aminobenzoyl-GFSPFRR-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, wild-type enzyme
0.0014
o-aminobenzoyl-GFSPFRR-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, C-domain
0.0014
o-aminobenzoyl-GFSPFRR-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, N-domain
0.0007
o-aminobenzoyl-GFSPFRS-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, wild-type enzyme
0.003
o-aminobenzoyl-GFSPFRS-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, C-domain
0.003
o-aminobenzoyl-GFSPFRS-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, N-domain
0.0021
o-aminobenzoyl-GFSPFSQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, C-domain
0.0023
o-aminobenzoyl-GFSPFSQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, N-domain
0.0025
o-aminobenzoyl-GFSPFSQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, wild-type enzyme
0.017
o-aminobenzoyl-SDK-(dinitrophenyl)-P-OH
-
pH 8.0, 37°C, wild-type enzyme
0.022
o-aminobenzoyl-SDK-(dinitrophenyl)-P-OH
-
pH 8.0, 37°C, N-domain
0.032
o-aminobenzoyl-SDK-(dinitrophenyl)-P-OH
-
pH 8.0, 37°C, C-domain
0.0144
o-aminobenzoyl-SRK-(dinitrophenyl)-P-OH
-
pH 8.0, 37°C, N-domain
0.0148
o-aminobenzoyl-SRK-(dinitrophenyl)-P-OH
-
pH 8.0, 37°C, wild-type enzyme
0.0229
o-aminobenzoyl-SRK-(dinitrophenyl)-P-OH
-
pH 8.0, 37°C, C-domain
0.0154
o-aminobenzoyl-TDK-(dinitrophenyl)-P-OH
-
pH 8.0, 37°C, wild-type enzyme
0.0157
o-aminobenzoyl-TDK-(dinitrophenyl)-P-OH
-
pH 8.0, 37°C, N-domain
0.0609
o-aminobenzoyl-TDK-(dinitrophenyl)-P-OH
-
pH 8.0, 37°C, C-domain
0.0031
o-aminobenzoyl-TRK-(dinitrophenyl)-P-OH
-
pH 8.0, 37°C, N-domain
0.0074
o-aminobenzoyl-TRK-(dinitrophenyl)-P-OH
-
pH 8.0, 37°C, C-domain
0.0102
o-aminobenzoyl-TRK-(dinitrophenyl)-P-OH
-
pH 8.0, 37°C, wild-type enzyme
0.0051
o-aminobenzoyl-YDK-(dinitrophenyl)-P-OH
-
pH 8.0, 37°C, N-domain
0.0111
o-aminobenzoyl-YDK-(dinitrophenyl)-P-OH
-
pH 8.0, 37°C, wild-type enzyme
0.015
o-aminobenzoyl-YDK-(dinitrophenyl)-P-OH
-
pH 8.0, 37°C, C-domain
0.0047
o-aminobenzoyl-YRK-(dinitrophenyl)-P-OH
-
pH 8.0, 37°C, C-domain
0.005
o-aminobenzoyl-YRK-(dinitrophenyl)-P-OH
-
pH 8.0, 37°C, N-domain
0.0051
o-aminobenzoyl-YRK-(dinitrophenyl)-P-OH
-
pH 8.0, 37°C, wild-type enzyme
0.108
SLKPSNWLTPSE
-
pH 7.0, N-domain
0.2338
SLKPSNWLTPSE
-
pH 7.0
0.3117
SLKPSNWLTPSE
-
pH 7.0, somatic enzyme
0.044
[Arg10]angiotensin I
-
37°C, pH 7.5, wild-type enzyme
0.046
[Arg10]angiotensin I
-
37°C, pH 7.5, mutant enzyme Y1096F
0.22
[Arg10]angiotensin I
-
37°C, pH 7.5, mutant enzyme R1098Q
0.011
[Phe9,Arg10]angiotensin I
-
37°C, pH 7.5, wild-type enzyme
0.014
[Phe9,Arg10]angiotensin I
-
37°C, pH 7.5, mutant enzyme Y1096F
0.02
[Phe9,Arg10]angiotensin I
-
37°C, pH 7.5, mutant enzyme R1098Q
0.025
[Phe9,Arg10]angiotensin I
-
37°C, pH 7.5, mutant enzyme K1087A
0.032
[Phe9]angiotensin I
-
37°C, pH 7.5, wild-type enzyme
0.042
[Phe9]angiotensin I
-
37°C, pH 7.5, mutant enzyme R1098Q
0.056
[Phe9]angiotensin I
-
37°C, pH 7.5, mutant enzyme Y1096F
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
Km values for wild-type and mutant enzymes
-
additional information
additional information
-
Km for angiotensin I as a function of pH
-
additional information
additional information
-
Km-values of underglycosylated mutant enzymes
-
additional information
additional information
-
the two active sites within bovine lung enzyme exhibits strong negative cooperativity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
320 - 987
2-furanacryloyl-Phe-Gly-Gly
5520 - 7590
2-furylacryloyl-Phe-Gly-Gly
1.9
Abz-FRK(Dnp)P-OH
-
pH 9.5, 37°C
3
Abz-SDK(Dnp)P-OH
-
pH 7.4, 37°C
4.2
amyloid beta-protein 1-42
-
-
-
2.41
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Tyr-Arg
Drosophila sp. (in: flies)
-
35°C, pH 8.0
0.24
Arg-Pro-Pro-Gly-Phe-Thr-Pro-Phe-Arg
Drosophila sp. (in: flies)
-
35°C, pH 8.0
283
benzoyl-Gly-Gly-Gly
-
-
76.7 - 345
benzoyl-Gly-His-Leu
383
benzoyl-Gly-Phe-Arg
-
-
2.1 - 128
benzyloxycarbonyl-Phe-His-Leu
179 - 210
furanacryloyl-L-Phe-Gly-Gly
5.4 - 545
hippuryl-His-Leu
1.1
Ile-Ser-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
Drosophila sp. (in: flies)
-
35°C, pH 8.0
20.33
Mca-RPPGFSAFK(Dnp)-OH
-
pH 7.4, 37°C
18.8
MKRSRGPSPRR
Drosophila sp. (in: flies)
-
35°C, pH 8.0
178
N-(3-(2-furyl)acryloyl)-Phe-Ala-Ala
-
pH 7.5, 25°C, enzyme from testis
35 - 85
N-(3-(2-furyl)acryloyl)-Phe-Ala-Lys
8 - 45
N-(3-(2-furyl)acryloyl)-Phe-Ala-Pro
260 - 315
N-(3-(2-furyl)acryloyl)-Phe-Gly-Gly
30 - 76
N-(3-(2-furyl)acryloyl)-Phe-Phe-Arg
987.3
N-(3-[2-furyl]acryloyl)-L-phenylalanylglycylglycine
pH 7.5, 22°C
12
N-benzyloxycarbonyl-L-Phe-L-His-L-Leu
-
pH 7.5, 25°C, enzyme from testis
6.5
N-hippuryl-His-Leu
-
pH 7.5, 25°C
31 - 101.7
o-aminobenzoyl-FDK-(dinitrophenyl)-P-OH
26.7 - 69.2
o-aminobenzoyl-FRK-(dinitrophenyl)-P-OH
1 - 3.3
o-aminobenzoyl-GFSPFAQ-(N-2,4-dinitrophenyl)ethylenediamine
2.2
o-aminobenzoyl-GFSPFEQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, wild-type enzyme
2.4 - 12.6
o-aminobenzoyl-GFSPFFQ-(N-2,4-dinitrophenyl)ethylenediamine
3 - 4.8
o-aminobenzoyl-GFSPFLQ-(N-2,4-dinitrophenyl)ethylenediamine
0.3 - 2
o-aminobenzoyl-GFSPFQQ-(N-2,4-dinitrophenyl)ethylenediamine
3.4 - 10.4
o-aminobenzoyl-GFSPFRA-(N-2,4-dinitrophenyl)ethylenediamine
1 - 4.2
o-aminobenzoyl-GFSPFRF-(N-2,4-dinitrophenyl)ethylenediamine
2.6 - 8.7
o-aminobenzoyl-GFSPFRI-(N-2,4-dinitrophenyl)ethylenediamine
1.8 - 3.8
o-aminobenzoyl-GFSPFRN-(N-2,4-dinitrophenyl)ethylenediamine
2.2 - 4.2
o-aminobenzoyl-GFSPFRQ-(N-2,4-dinitrophenyl)ethylenediamine
0.9 - 1.4
o-aminobenzoyl-GFSPFRR-(N-2,4-dinitrophenyl)ethylenediamine
0.9 - 2.4
o-aminobenzoyl-GFSPFRS-(N-2,4-dinitrophenyl)ethylenediamine
0.8 - 2.3
o-aminobenzoyl-GFSPFSQ-(N-2,4-dinitrophenyl)ethylenediamine
0.1 - 44.2
o-aminobenzoyl-SDK-(dinitrophenyl)-P-OH
13.7 - 28.6
o-aminobenzoyl-SRK-(dinitrophenyl)-P-OH
0.06 - 36.3
o-aminobenzoyl-TDK-(dinitrophenyl)-P-OH
0.2 - 82
o-aminobenzoyl-TRK-(dinitrophenyl)-P-OH
7 - 62.5
o-aminobenzoyl-YDK-(dinitrophenyl)-P-OH
1.01 - 85.6
o-aminobenzoyl-YRK-(dinitrophenyl)-P-OH
5.83
TOAC1-angiotensin I
-
-
2.56
TOAC3-angiotensin I
-
-
57 - 460
[Arg10]angiotensin I
6.5 - 1700
[Phe9,Arg10]angiotensin I
110 - 1500
[Phe9]angiotensin I
additional information
additional information
-
320
2-furanacryloyl-Phe-Gly-Gly
-
recombinant enzyme
368
2-furanacryloyl-Phe-Gly-Gly
-
wild-type enzyme
987
2-furanacryloyl-Phe-Gly-Gly
-
pH 7.5, 20°C
5520
2-furylacryloyl-Phe-Gly-Gly
-
pH 7.5, 25°C, cobalt-ACE
7590
2-furylacryloyl-Phe-Gly-Gly
-
pH 7.5, 25°C
0.8
Abz-LFK(Dnp)-OH
-
pH 9.5, 37°C
23
Abz-LFK(Dnp)-OH
-
pH 7.4, 37°C
0.58
angiotensin
-
37°C
0.03 - 0.55
angiotensin I
Drosophila sp. (in: flies)
-
35°C, pH 7.0, 0 mM NaCl
0.057 - 0.65
angiotensin I
Drosophila sp. (in: flies)
-
35°C, pH 8.0, 0 mM NaCl
0.057 - 0.65
angiotensin I
Drosophila sp. (in: flies)
-
35°C, pH 8.0, 100 mM NaCl
1.4
angiotensin I
-
pH 7.5, 37°C, enzyme from brain, 200 mM NaCl
2.95
angiotensin I
-
detergent-solubilized enzyme
6.58
angiotensin I
-
trypsin-extracted enzyme
6.83
angiotensin I
Drosophila sp. (in: flies)
-
35°C, pH 7.0, 100 mM NaCl
6.84
angiotensin I
Drosophila sp. (in: flies)
-
35°C, pH 7.0, 0 mM NaCl
10.78
angiotensin I
Drosophila sp. (in: flies)
-
35°C, pH 8.0, 100 mM NaCl
11.06
angiotensin I
Drosophila sp. (in: flies)
-
35°C, pH 8.0, 0 mM NaCl
12
angiotensin I
-
enzyme from testis
13.2
angiotensin I
-
enzyme from testis
13.5
angiotensin I
-
enzyme from lung
52
angiotensin I
-
37°C, pH 7.5, wild-type enzyme
60
angiotensin I
-
37°C, pH 7.5, mutant enzyme R1098Q
76.7
benzoyl-Gly-His-Leu
-
-
345
benzoyl-Gly-His-Leu
-
-
2.1
benzyloxycarbonyl-Phe-His-Leu
37°C, pH 8.3, ACE
19
benzyloxycarbonyl-Phe-His-Leu
-
pH 7.5, 25°C, enzyme from testis
21.5
benzyloxycarbonyl-Phe-His-Leu
-
pH 7.5
34.4
benzyloxycarbonyl-Phe-His-Leu
37°C, pH 8.3, chimeric enzyme C417-579Ndom-ACE
36.8
benzyloxycarbonyl-Phe-His-Leu
37°C, pH 8.3, chimeric enzyme C583-623Ndom-ACE
73.2
benzyloxycarbonyl-Phe-His-Leu
37°C, pH 8.3, ACE
97.5
benzyloxycarbonyl-Phe-His-Leu
37°C, pH 8.3, chimeric enzyme C1-163Ndom-ACE
100
benzyloxycarbonyl-Phe-His-Leu
-
pH 7.5, 25°C
128
benzyloxycarbonyl-Phe-His-Leu
37°C, pH 8.3, N-domain of tACE
1.09
bradykinin
Drosophila sp. (in: flies)
-
35°C, pH 8.0
179
furanacryloyl-L-Phe-Gly-Gly
-
-
210
furanacryloyl-L-Phe-Gly-Gly
-
-
5.4
hippuryl-His-Leu
-
detergent-solubilized enzyme
8.58
hippuryl-His-Leu
-
trypsin-extracted enzyme
11.8
hippuryl-His-Leu
37°C, pH 8.3, chimeric enzyme C417-579Ndom-ACE
12.9
hippuryl-His-Leu
37°C, pH 8.3, chimeric enzyme C583-623Ndom-ACE
15.1
hippuryl-His-Leu
37°C, pH 8.3, chimeric enzyme C1163Ndom-ACE
24.5
hippuryl-His-Leu
37°C, pH 8.3, tACE
262.5
hippuryl-His-Leu
37°C, pH 8.3, N-domain of tACE
302
hippuryl-His-Leu
-
enzyme from lung
308
hippuryl-His-Leu
-
enzyme from testis
408
hippuryl-His-Leu
-
recombinant enzyme
414
hippuryl-His-Leu
-
wild-type enzyme
51
LVVYPWTQRY
-
pH 7.5, 37°C, enzyme from testis, 10 mM NaCl
77
LVVYPWTQRY
-
pH 7.5, 37°C, enzyme from testis, 200 mM NaCl
89
LVVYPWTQRY
-
pH 7.5, 37°C, enzyme from brain, 200 mM NaCl
230
LVVYPWTQRY
-
pH 7.5, 37°C, enzyme from brain, 10 mM NaCl
35
N-(3-(2-furyl)acryloyl)-Phe-Ala-Lys
-
pH 7.5, 25°C, N-domain from lung enzyme
54
N-(3-(2-furyl)acryloyl)-Phe-Ala-Lys
-
pH 7.5, 25°C, enzyme from lung
85
N-(3-(2-furyl)acryloyl)-Phe-Ala-Lys
-
pH 7.5, 25°C, enzyme from testis
8
N-(3-(2-furyl)acryloyl)-Phe-Ala-Pro
-
pH 7.5, 25°C, N-domain from lung enzyme
30
N-(3-(2-furyl)acryloyl)-Phe-Ala-Pro
-
pH 7.5, 25°C, enzyme from lung
45
N-(3-(2-furyl)acryloyl)-Phe-Ala-Pro
-
pH 7.5, 25°C, enzyme from testis
260
N-(3-(2-furyl)acryloyl)-Phe-Gly-Gly
-
pH 7.5, 25°C, enzyme from testis
315
N-(3-(2-furyl)acryloyl)-Phe-Gly-Gly
-
pH 7.5, 25°C
30
N-(3-(2-furyl)acryloyl)-Phe-Phe-Arg
-
pH 7.5, 25°C
45
N-(3-(2-furyl)acryloyl)-Phe-Phe-Arg
-
pH 7.5, 25°C, N-domain from lung enzyme
76
N-(3-(2-furyl)acryloyl)-Phe-Phe-Arg
-
pH 7.5, 25°C, enzyme from testis
31
o-aminobenzoyl-FDK-(dinitrophenyl)-P-OH
-
pH 8.0, 37°C, C-domain
79
o-aminobenzoyl-FDK-(dinitrophenyl)-P-OH
-
pH 8.0, 37°C, N-domain
79.9
o-aminobenzoyl-FDK-(dinitrophenyl)-P-OH
-
pH 8.0, 37°C, wild-type enzyme
101.7
o-aminobenzoyl-FDK-(dinitrophenyl)-P-OH
-
pH 8.0, 37°C, N-domain
26.7
o-aminobenzoyl-FRK-(dinitrophenyl)-P-OH
-
pH 8.0, 37°C, wild-type enzyme
54.9
o-aminobenzoyl-FRK-(dinitrophenyl)-P-OH
-
pH 8.0, 37°C, N-domain
69.2
o-aminobenzoyl-FRK-(dinitrophenyl)-P-OH
-
pH 8.0, 37°C, C-domain
1
o-aminobenzoyl-GFSPFAQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, N-domain
2
o-aminobenzoyl-GFSPFAQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, C-domain
3.3
o-aminobenzoyl-GFSPFAQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, wild-type enzyme
2.4
o-aminobenzoyl-GFSPFFQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, N-domain
10.1
o-aminobenzoyl-GFSPFFQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, wild-type enzyme
12.6
o-aminobenzoyl-GFSPFFQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, C-domain
3
o-aminobenzoyl-GFSPFLQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, N-domain
3.7
o-aminobenzoyl-GFSPFLQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, wild-type enzyme
4.8
o-aminobenzoyl-GFSPFLQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, C-domain
0.3
o-aminobenzoyl-GFSPFQQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, C-domain
0.6
o-aminobenzoyl-GFSPFQQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, N-domain
2
o-aminobenzoyl-GFSPFQQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, wild-type enzyme
3.4
o-aminobenzoyl-GFSPFRA-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, N-domain
5
o-aminobenzoyl-GFSPFRA-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, C-domain
10.4
o-aminobenzoyl-GFSPFRA-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, wild-type enzyme
1
o-aminobenzoyl-GFSPFRF-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, N-domain
1.4
o-aminobenzoyl-GFSPFRF-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, C-domain
4.2
o-aminobenzoyl-GFSPFRF-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, wild-type enzyme
2.6
o-aminobenzoyl-GFSPFRI-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, N-domain
2.9
o-aminobenzoyl-GFSPFRI-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, C-domain
8.7
o-aminobenzoyl-GFSPFRI-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, wild-type enzyme
1.8
o-aminobenzoyl-GFSPFRN-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, wild-type enzyme
3.3
o-aminobenzoyl-GFSPFRN-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, C-domain
3.8
o-aminobenzoyl-GFSPFRN-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, N-domain
2.2
o-aminobenzoyl-GFSPFRQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, wild-type enzyme
2.7
o-aminobenzoyl-GFSPFRQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, N-domain
4.2
o-aminobenzoyl-GFSPFRQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, C-domain
0.9
o-aminobenzoyl-GFSPFRR-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, N-domain
1
o-aminobenzoyl-GFSPFRR-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, wild-type enzyme
1.4
o-aminobenzoyl-GFSPFRR-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, C-domain
0.9
o-aminobenzoyl-GFSPFRS-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, wild-type enzyme
1.3
o-aminobenzoyl-GFSPFRS-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, N-domain
2.4
o-aminobenzoyl-GFSPFRS-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, C-domain
0.8
o-aminobenzoyl-GFSPFSQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, C-domain
2
o-aminobenzoyl-GFSPFSQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, wild-type enzyme
2.3
o-aminobenzoyl-GFSPFSQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37°C, N-domain
0.1
o-aminobenzoyl-SDK-(dinitrophenyl)-P-OH
-
pH 8.0, 37°C, C-domain
24.6
o-aminobenzoyl-SDK-(dinitrophenyl)-P-OH
-
pH 8.0, 37°C, N-domain
44.2
o-aminobenzoyl-SDK-(dinitrophenyl)-P-OH
-
pH 8.0, 37°C, wild-type enzyme
13.7
o-aminobenzoyl-SRK-(dinitrophenyl)-P-OH
-
pH 8.0, 37°C, C-domain
28.6
o-aminobenzoyl-SRK-(dinitrophenyl)-P-OH
-
pH 8.0, 37°C, N-domain
0.06
o-aminobenzoyl-TDK-(dinitrophenyl)-P-OH
-
pH 8.0, 37°C, C-domain
1.1
o-aminobenzoyl-TDK-(dinitrophenyl)-P-OH
-
pH 8.0, 37°C, N-domain
18.7
o-aminobenzoyl-TDK-(dinitrophenyl)-P-OH
-
pH 8.0, 37°C, N-domain
36.3
o-aminobenzoyl-TDK-(dinitrophenyl)-P-OH
-
pH 8.0, 37°C, wild-type enzyme
0.2
o-aminobenzoyl-TRK-(dinitrophenyl)-P-OH
-
pH 8.0, 37°C, C-domain
13.9
o-aminobenzoyl-TRK-(dinitrophenyl)-P-OH
-
pH 8.0, 37°C, N-domain
82
o-aminobenzoyl-TRK-(dinitrophenyl)-P-OH
-
pH 8.0, 37°C, wild-type enzyme
7
o-aminobenzoyl-YDK-(dinitrophenyl)-P-OH
-
pH 8.0, 37°C, C-domain
28.9
o-aminobenzoyl-YDK-(dinitrophenyl)-P-OH
-
pH 8.0, 37°C, N-domain
62.5
o-aminobenzoyl-YDK-(dinitrophenyl)-P-OH
-
pH 8.0, 37°C, wild-type enzyme
1.01
o-aminobenzoyl-YRK-(dinitrophenyl)-P-OH
-
pH 8.0, 37°C, wild-type enzyme
58.8
o-aminobenzoyl-YRK-(dinitrophenyl)-P-OH
-
pH 8.0, 37°C, C-domain
85.6
o-aminobenzoyl-YRK-(dinitrophenyl)-P-OH
-
pH 8.0, 37°C, N-domain
3.75
Substance P
-
-
21.3
Substance P
-
free acid, recombinant enzyme, and wild-type enzyme
57
[Arg10]angiotensin I
-
37°C, pH 7.5, mutant enzyme Y1096F
100
[Arg10]angiotensin I
-
37°C, pH 7.5, mutant enzyme R1098Q
460
[Arg10]angiotensin I
-
37°C, pH 7.5, wild-type enzyme
6.5
[Phe9,Arg10]angiotensin I
-
37°C, pH 7.5, mutant enzyme K1087A
220
[Phe9,Arg10]angiotensin I
-
37°C, pH 7.5, mutant enzyme Y1096F
1400
[Phe9,Arg10]angiotensin I
-
37°C, pH 7.5, wild-type enzyme
1700
[Phe9,Arg10]angiotensin I
-
37°C, pH 7.5, mutant enzyme R1098Q
110
[Phe9]angiotensin I
-
37°C, pH 7.5, mutant enzyme Y1096F
550
[Phe9]angiotensin I
-
37°C, pH 7.5, wild-type enzyme
1500
[Phe9]angiotensin I
-
37°C, pH 7.5, mutant enzyme R1098Q
additional information
additional information
-
Km-values for angiotensin I as a function of pH
-
additional information
additional information
-
Km values for wild-type and mutant enzymes
-
additional information
additional information
-
the two active sites within bovine lung enzyme exhibitsstrong negative cooperativity
-
additional information
additional information
-
turnover numbers of underglycosylated mutant enzymes
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.00000061 - 0.00012
(2R)-2-((3-[hydroxyl (2-phenyl-(1R)-1-([(benzyloxy) carbonyl]-amino)ethyl)phosphinyl]-2-[(3-phenylisoxazol-5-yl)methyl]-1-oxopropyl)amino)-3-(4-hydroxy-phenyl) propanoic acid
0.00000041 - 0.000024
(2S)-2-((3-[hydroxyl (2-phenyl-(1R)-1-([(benzyloxy) carbonyl]-amino)ethyl)phosphinyl]-2-[(3-phenylisoxazol-5-yl)methyl]-1-oxopropyl)amino)-3-(4-hydroxy-phenyl) propanoic acid
0.0000004
(2S)-2-((3-[hydroxyl(2-phenyl-(1R)-1([(benzyloxy)carbonyl]amino)ethyl)phosphinyl]-(2R)-2-[(3-phenylisoxazol-5-yl)methyl]-1-oxopropyl)amino)-3-phenyl propanoic acid
-
pH and temperature not specified in the publication
0.0000014
(2S)-2-((3-[hydroxyl(2-phenyl-(1R)-1-([(benzyloxy)carbonyl]-amino)ethyl)phosphinyl]-(2R)-2-[(3-phenylisoxazol-5-yl)methyl]-1-oxopropyl)amino) 1H-Indole-3-propanoic acid
-
pH and temperature not specified in the publication
0.00000065
(2S)-2-((3-[hydroxyl(2-phenyl-(1R)-1-([(benzyloxy)carbonyl]-amino)ethyl)phosphinyl]-(2R)-2-[(3-phenylisoxazol-5-yl)methyl]-1-oxopropyl)amino)-3-(4-hydroxy-phenyl) propanoic acid
-
pH and temperature not specified in the publication
0.000012
(2S)-2-((3-[hydroxyl(2-phenyl-(1R)-1-([(benzyloxy)carbonyl]-amino)ethyl)phosphinyl]-(2S)-2-[(3-phenylisoxazol-5-yl)methyl]-1-oxopropyl)amino) 1H-indole-3-propanoic acid
-
pH and temperature not specified in the publication
0.0000038
(2S)-2-((3-[hydroxyl(2-phenyl-(1R)-1-([(benzyloxy)carbonyl]-amino)ethyl)phosphinyl]-(2S)-2-[(3-phenylisoxazol-5-yl)methyl]-1-oxopropyl)amino)-3-(4-hydroxy-phenyl) propanoic acid
-
pH and temperature not specified in the publication
0.000016
(2S)-2-([3-(1,1'-biphenyl)-2-([hydroxyl(2-phenyl-(1R)-1-([(benzyloxy)carbonyl]amino)ethyl)phosphinyl]methyl)-1-oxopropyl]-amino) 1H-indole-3-propanoic acid
-
pH and temperature not specified in the publication
0.000025
(2S)-2-([3-(3'-[1,1'-biphenyl]-4''-yl-4',5'-dihydro-5'-isoxazolyl)-2-([hydroxyl(2-phenyl-(1R)-1-([(benzyloxy)carbonyl]amino)ethyl)-phosphinyl]methyl)-1-oxopropyl]amino) 1H-indole-3-propanoic acid
-
pH and temperature not specified in the publication
0.0000022 - 0.0018
(2S)-2-[[(2S)-2-mercapto-3-methylpentanoyl]amino]-3-(1-naphthyl)propanoic acid
0.0000018 - 0.00031
(2S)-2-[[(2S)-2-mercapto-3-methylpentanoyl]amino]-3-(2-naphthyl)propanoic acid
0.0000015 - 0.00057
(2S)-2-[[(2S)-2-mercapto-3-methylpentanoyl]amino]-3-phenylpropanoic acid
0.000014 - 0.00018
(2S)-2-[[(2S)-2-mercapto-3-methylpentanoyl]amino]propanoic acid
0.0000013 - 0.00041
(2S)-3-(4-hydroxyphenyl)-2-[[(2S)-2-mercapto-3-methylpentanoyl]amino]propanoic acid
0.0000015 - 0.02
(2S)-3-biphenyl-2-yl-2-[[(2S)-3-methyl-2-sulfanylpentanoyl]amino]propanoic acid
0.0000015 - 0.001
(2S)-3-biphenyl-3-yl-2-[[(2S)-3-methyl-2-sulfanylpentanoyl]amino]propanoic acid
0.0023 - 0.0034
(2S)-3-biphenyl-4-yl-2-[(2-mercapto-2-methylpropanoyl)amino]propanoic acid
0.000016 - 0.00032
(2S)-3-biphenyl-4-yl-2-[(mercaptoacetyl)amino]propanoic acid
0.0000014 - 0.0000086
(2S)-3-biphenyl-4-yl-2-[[(2S)-2-mercaptobutanoyl]amino]propanoic acid
0.0000069 - 0.000021
(2S)-3-biphenyl-4-yl-2-[[(2S)-2-mercaptopropanoyl]amino]propanoic acid
0.0000015 - 0.00049
(2S)-3-biphenyl-4-yl-2-[[(2S)-3-methyl-2-sulfanylpentanoyl]amino]propanoic acid
0.00081 - 0.0181
(5S)-5-[(N-benzoyl)amino]-4-oxo-6-phenylhexanoyl-L-phenylalanine
0.000064 - 0.00974
(5S)-5-[(N-benzoyl)amino]-4-oxo-6-phenylhexanoyl-L-tryptophan
0.000003 - 0.0001
(pE)WPRPQIPP
0.0018 - 0.0452
1-[(5S)-4-oxo-6-phenyl-5-[(phenylcarbonyl)amino]hexanoyl]-L-proline
0.0336 - 0.1435
1-[(5S)-5-[(tert-butoxycarbonyl)amino]-4-oxo-6-phenylhexanoyl]-L-proline
0.000006 - 0.013
2-(benzyloxy)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-phenylalanine
0.0000024 - 0.00075
3-(benzyloxy)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-phenylalanine
0.000002747
angiotensin I
-
-
0.004 - 0.076
angiotensin II
0.035
angiotensin IV
-
pH 7.5
0.3176
Arg-Met-Leu
-
pH 8.5
0.365
benzyloxycarbonyl-PhePSI[PO2-CH]Ala-Ala
Drosophila sp. (in: flies)
-
35°C, pH 8.0
0.152
benzyloxycarbonyl-PhePSI[PO2-CH]Ala-Trp
Drosophila sp. (in: flies)
-
35°C, pH 8.0
0.000001278
bradykinin
-
-
0.0000003 - 0.000191
captopril
0.0569
cyanidin-3-O-sambubioside
-
pH 8.3, 37°C
0.0319
delphinidin-3-O-sambubioside
-
pH 8.3, 37°C
0.00000194
enalaprilat
-
-
0.828
epicatechin
-
pH 8.3, 37°C
0.124
epicatechin dimer
-
pH 8.3, 37°C
0.0047
epicatechin hexamer
-
pH 8.3, 37°C
0.0116
epicatechin pentamer
-
pH 8.3, 37°C
0.0056
epicatechin tetramer
-
pH 8.3, 37°C
0.059
epicatechin trimer
-
pH 8.3, 37°C
0.000083
gluco-aurantioobtusin
-
in 50 mM Tris-HCl buffer (pH 7.5)
0.01148
Gly-Phe-Hyp-Gly-Thr-Hyp-Gly-Leu-Hyp-Gly-Phe
-
37°C, pH 8.3
0.0000001 - 0.00028
lisinopril
0.0000066 - 0.0017
lisW-S
0.0008 - 0.017
LRPARPTSPP
0.0003 - 0.017
LRPARPTSPPA
0.000013
N-(3-{[(1R)-1-{[(benzyloxy)carbonyl]amino}-2-phenylethyl](hydroxy)phosphoryl}-2-{[3-(biphenyl-4-yl)-4,5-dihydro-1,2-oxazol-5-yl]methyl}propanoyl)-L-tryptophan
-
pH and temperature not specified in the publication
0.0000009 - 0.005
N-[(2S)-3-methyl-2-sulfanylpentanoyl]-2-phenoxy-L-phenylalanine
0.0000024 - 0.0011
N-[(2S)-3-methyl-2-sulfanylpentanoyl]-3-phenoxy-L-phenylalanine
0.0000018 - 0.0007
N-[(2S)-3-methyl-2-sulfanylpentanoyl]-O-phenyl-L-tyrosine
0.000035 - 0.0026
N-[(2S)-3-methyl-2-sulfanylpentanoyl]-O-[4-(trifluoromethyl)benzyl]-L-tyrosine
0.0237 - 0.0843
N-[(5S)-4-oxo-6-phenyl-5-[(phenylcarbonyl)amino]hexanoyl]-L-phenylalanine
0.0008 - 0.1957
N-[(5S)-4-oxo-6-phenyl-5-[(phenylcarbonyl)amino]hexanoyl]-L-tryptophan
0.043 - 0.3129
N-[(5S)-5-[(tert-butoxycarbonyl)amino]-4-oxo-6-phenylhexanoyl]-L-phenylalanine
0.0133 - 0.3813
N-[(5S)-5-[(tert-butoxycarbonyl)amino]-4-oxo-6-phenylhexanoyl]-L-tryptophan
0.000005
N-[3-{[(1R)-1-{[(benzyloxy)carbonyl]amino}-2-phenylethyl](hydroxy)phosphoryl}-2-(biphenyl-4-ylmethyl)propanoyl]-L-tryptophan
-
pH and temperature not specified in the publication
0.000036
N-{(2R)-3-{[(1R)-1-{[(benzyloxy)carbonyl]amino}-2-phenylethyl](hydroxy)phosphoryl}-2-[(3-phenyl-1,2-oxazol-5-yl)methyl]propanoyl}-L-tyrosine
-
pH and temperature not specified in the publication
0.00002
N-{(2S)-3-{[(1R)-1-{[(benzyloxy)carbonyl]amino}-2-phenylethyl](hydroxy)phosphoryl}-2-[(3-phenyl-1,2-oxazol-5-yl)methyl]propanoyl}-L-tryptophan
-
pH and temperature not specified in the publication
0.0266
noncompetitive inhibitor
-
-
-
0.000002 - 0.00095
O-(2,4-difluorobenzyl)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-tyrosine
0.0000085 - 0.0018
O-(3,4-difluorobenzyl)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-tyrosine
0.0000025 - 0.004
O-(4-fluorobenzyl)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-tyrosine
0.0000014 - 0.00057
O-benzyl-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-tyrosine
0.000084 - 0.025
O-[3,5-bis(trifluoromethyl)benzyl]-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-tyrosine
0.00000105
perindoprilat
-
-
0.0000015 - 0.0002
pGlu-Asn-Trp-Pro-His-Pro-Gln-Ile-Pro-Pro
0.00003 - 0.01
pGlu-Gly-Leu-Pro-Pro-Arg-Pro-Lys-Ile-Pro-Pro
0.00008
pGlu-Gly-Leu-Pro-Pro-Gly-Pro-Pro-Ile-Pro-Pro
0.000001 - 0.0001
pGlu-Trp-Pro-Arg-Pro-Gln-Ile-Pro-Pro
0.02825
Pro-Arg-Tyr
pH and temperature not specified in the publication
0.00000035
quinaprilat
-
-
0.00000076
ramiprilat
-
-
0.0606
RMLGQTPTK
-
pH 8.5
0.005 - 0.019
Ser-Pro-Pro
0.0024 - 0.2
SSYVHLRPARPTSPP
0.00000057
trandolaprilat
-
-
0.20027
Trp-Gly
pH and temperature not specified in the publication
0.0045
Val-Leu-Ile-Val-Pro
-
-
0.138
Val-Trp
-
pH 8.3, 37°C
0.203
Val-Tyr
-
pH 8.3, 37°C
0.0144
VVYPWTQRF
-
pH 7.5
0.0008 - 0.01
YVHLRPARPTSPP
0.000008 - 0.000018
[CB-TE2A]1--lisinopril
-
0.0003 - 0.0023
[Co-DOTA]1--lisinopril
-
0.00041 - 0.0027
[Co-EDTA]1--lisinopril
-
0.000027 - 0.000189
[Co-GGH]0-lisinopril
0.00000012 - 0.00004
[Co-NTA]0-lisinopril
0.000014 - 0.000028
[Cu-CB-TE2A]1+-lisinopril
-
0.00029 - 0.0018
[Cu-DOTA]1--lisinopril
-
0.00023 - 0.0017
[Cu-EDTA]1--lisinopril
-
0.0001 - 0.0019
[Cu-GGH]0-lisinopril
0.00000033 - 0.000038
[Cu-NTA]0-lisinopril
0.00034 - 0.0022
[DOTA]1--lisinopril
-
0.00014 - 0.00058
[EDTA]3-lisinopril
-
0.000015 - 0.00054
[Fe-CB-TE2A]2+-lisinopril
-
0.00042 - 0.0021
[Fe-DOTA]0-lisinopril
-
0.000016 - 0.00015
[Fe-EDTA]0-lisinopril
-
0.00000024 - 0.000035
[Fe-NTA]1+-lisinopril
0.000029 - 0.000102
[GGH]1+-lisinopril
0.000017 - 0.000023
[Ni-CB-TE2A]1+-lisinopril
-
0.00045 - 0.0026
[Ni-DOTA]1--lisinopril
-
0.00049 - 0.0026
[Ni-EDTA]1--lisinopril
-
0.00011 - 0.001
[Ni-GGH]0-lisinopril
0.00000026 - 0.000033
[Ni-NTA]0-lisinopril
0.00000031 - 0.000057
[NTA]2-lisinopril
0.00009 - 0.0014
[[(2S)-2-mercapto-3-methylpentanoyl]amino]acetic acid
additional information
additional information
-
0.00000061
(2R)-2-((3-[hydroxyl (2-phenyl-(1R)-1-([(benzyloxy) carbonyl]-amino)ethyl)phosphinyl]-2-[(3-phenylisoxazol-5-yl)methyl]-1-oxopropyl)amino)-3-(4-hydroxy-phenyl) propanoic acid
C-catalytic domain of ACE, pH 7.5, temperature not specified in the publication
0.00012
(2R)-2-((3-[hydroxyl (2-phenyl-(1R)-1-([(benzyloxy) carbonyl]-amino)ethyl)phosphinyl]-2-[(3-phenylisoxazol-5-yl)methyl]-1-oxopropyl)amino)-3-(4-hydroxy-phenyl) propanoic acid
C-catalytic domain of ACE, pH 7.5, temperature not specified in the publication
0.00000041
(2S)-2-((3-[hydroxyl (2-phenyl-(1R)-1-([(benzyloxy) carbonyl]-amino)ethyl)phosphinyl]-2-[(3-phenylisoxazol-5-yl)methyl]-1-oxopropyl)amino)-3-(4-hydroxy-phenyl) propanoic acid
C-catalytic domain of ACE, pH 7.5, temperature not specified in the publication
0.000024
(2S)-2-((3-[hydroxyl (2-phenyl-(1R)-1-([(benzyloxy) carbonyl]-amino)ethyl)phosphinyl]-2-[(3-phenylisoxazol-5-yl)methyl]-1-oxopropyl)amino)-3-(4-hydroxy-phenyl) propanoic acid
C-catalytic domain of ACE, pH 7.5, temperature not specified in the publication
0.0000022
(2S)-2-[[(2S)-2-mercapto-3-methylpentanoyl]amino]-3-(1-naphthyl)propanoic acid
pH 7.5, angiotensin-converting enzyme 2
0.0018
(2S)-2-[[(2S)-2-mercapto-3-methylpentanoyl]amino]-3-(1-naphthyl)propanoic acid
pH 7.5, angiotensin-converting enzyme
0.0000018
(2S)-2-[[(2S)-2-mercapto-3-methylpentanoyl]amino]-3-(2-naphthyl)propanoic acid
pH 7.5, angiotensin-converting enzyme 2
0.0000024
(2S)-2-[[(2S)-2-mercapto-3-methylpentanoyl]amino]-3-(2-naphthyl)propanoic acid
pH 7.5, angiotensin-converting enzyme 2
0.0000093
(2S)-2-[[(2S)-2-mercapto-3-methylpentanoyl]amino]-3-(2-naphthyl)propanoic acid
pH 7.5, angiotensin-converting enzyme
0.00031
(2S)-2-[[(2S)-2-mercapto-3-methylpentanoyl]amino]-3-(2-naphthyl)propanoic acid
pH 7.5, angiotensin-converting enzyme
0.0000015
(2S)-2-[[(2S)-2-mercapto-3-methylpentanoyl]amino]-3-phenylpropanoic acid
pH 7.5, angiotensin-converting enzyme 2
0.00057
(2S)-2-[[(2S)-2-mercapto-3-methylpentanoyl]amino]-3-phenylpropanoic acid
pH 7.5, angiotensin-converting enzyme
0.000014
(2S)-2-[[(2S)-2-mercapto-3-methylpentanoyl]amino]propanoic acid
pH 7.5, angiotensin-converting enzyme 2
0.00018
(2S)-2-[[(2S)-2-mercapto-3-methylpentanoyl]amino]propanoic acid
pH 7.5, angiotensin-converting enzyme
0.0000013
(2S)-3-(4-hydroxyphenyl)-2-[[(2S)-2-mercapto-3-methylpentanoyl]amino]propanoic acid
pH 7.5, angiotensin-converting enzyme 2
0.00041
(2S)-3-(4-hydroxyphenyl)-2-[[(2S)-2-mercapto-3-methylpentanoyl]amino]propanoic acid
pH 7.5, angiotensin-converting enzyme
0.0000015
(2S)-3-biphenyl-2-yl-2-[[(2S)-3-methyl-2-sulfanylpentanoyl]amino]propanoic acid
pH 7.5, angiotensin-converting enzyme 2
0.000037
(2S)-3-biphenyl-2-yl-2-[[(2S)-3-methyl-2-sulfanylpentanoyl]amino]propanoic acid
pH 7.5, angiotensin-converting enzyme 2
0.0002
(2S)-3-biphenyl-2-yl-2-[[(2S)-3-methyl-2-sulfanylpentanoyl]amino]propanoic acid
pH 7.5, angiotensin-converting enzyme
0.02
(2S)-3-biphenyl-2-yl-2-[[(2S)-3-methyl-2-sulfanylpentanoyl]amino]propanoic acid
pH 7.5, angiotensin-converting enzyme
0.0000015
(2S)-3-biphenyl-3-yl-2-[[(2S)-3-methyl-2-sulfanylpentanoyl]amino]propanoic acid
pH 7.5, angiotensin-converting enzyme 2
0.0000022
(2S)-3-biphenyl-3-yl-2-[[(2S)-3-methyl-2-sulfanylpentanoyl]amino]propanoic acid
pH 7.5, angiotensin-converting enzyme 2
0.00049
(2S)-3-biphenyl-3-yl-2-[[(2S)-3-methyl-2-sulfanylpentanoyl]amino]propanoic acid
pH 7.5, angiotensin-converting enzyme
0.001
(2S)-3-biphenyl-3-yl-2-[[(2S)-3-methyl-2-sulfanylpentanoyl]amino]propanoic acid
pH 7.5, angiotensin-converting enzyme
0.0023
(2S)-3-biphenyl-4-yl-2-[(2-mercapto-2-methylpropanoyl)amino]propanoic acid
pH 7.5, angiotensin-converting enzyme 2
0.0034
(2S)-3-biphenyl-4-yl-2-[(2-mercapto-2-methylpropanoyl)amino]propanoic acid
pH 7.5, angiotensin-converting enzyme
0.000016
(2S)-3-biphenyl-4-yl-2-[(mercaptoacetyl)amino]propanoic acid
pH 7.5, angiotensin-converting enzyme
0.00032
(2S)-3-biphenyl-4-yl-2-[(mercaptoacetyl)amino]propanoic acid
pH 7.5, angiotensin-converting enzyme 2
0.0000014
(2S)-3-biphenyl-4-yl-2-[[(2S)-2-mercaptobutanoyl]amino]propanoic acid
pH 7.5, angiotensin-converting enzyme 2
0.0000086
(2S)-3-biphenyl-4-yl-2-[[(2S)-2-mercaptobutanoyl]amino]propanoic acid
pH 7.5, angiotensin-converting enzyme
0.0000069
(2S)-3-biphenyl-4-yl-2-[[(2S)-2-mercaptopropanoyl]amino]propanoic acid
pH 7.5, angiotensin-converting enzyme 2
0.000021
(2S)-3-biphenyl-4-yl-2-[[(2S)-2-mercaptopropanoyl]amino]propanoic acid
pH 7.5, angiotensin-converting enzyme
0.0000015
(2S)-3-biphenyl-4-yl-2-[[(2S)-3-methyl-2-sulfanylpentanoyl]amino]propanoic acid
pH 7.5, angiotensin-converting enzyme 2
0.00003
(2S)-3-biphenyl-4-yl-2-[[(2S)-3-methyl-2-sulfanylpentanoyl]amino]propanoic acid
pH 7.5, angiotensin-converting enzyme
0.000086
(2S)-3-biphenyl-4-yl-2-[[(2S)-3-methyl-2-sulfanylpentanoyl]amino]propanoic acid
pH 7.5, angiotensin-converting enzyme 2
0.00049
(2S)-3-biphenyl-4-yl-2-[[(2S)-3-methyl-2-sulfanylpentanoyl]amino]propanoic acid
pH 7.5, angiotensin-converting enzyme
0.00081
(5S)-5-[(N-benzoyl)amino]-4-oxo-6-phenylhexanoyl-L-phenylalanine
mutant enzyme V379S, in 50 mM HEPES buffer (pH 6.8) containing 200 mM NaCl, and 0.01 mM ZnCl2, at 25°C
0.00083
(5S)-5-[(N-benzoyl)amino]-4-oxo-6-phenylhexanoyl-L-phenylalanine
wild type enzyme, in 50 mM HEPES buffer (pH 6.8) containing 200 mM NaCl, and 0.01 mM ZnCl2, at 25°C
0.0019
(5S)-5-[(N-benzoyl)amino]-4-oxo-6-phenylhexanoyl-L-phenylalanine
mutant enzyme V380T, in 50 mM HEPES buffer (pH 6.8) containing 200 mM NaCl, and 0.01 mM ZnCl2, at 25°C
0.0024
(5S)-5-[(N-benzoyl)amino]-4-oxo-6-phenylhexanoyl-L-phenylalanine
mutant enzyme E376D, in 50 mM HEPES buffer (pH 6.8) containing 200 mM NaCl, and 0.01 mM ZnCl2, at 25°C
0.0039
(5S)-5-[(N-benzoyl)amino]-4-oxo-6-phenylhexanoyl-L-phenylalanine
mutant enzyme F391Y, in 50 mM HEPES buffer (pH 6.8) containing 200 mM NaCl, and 0.01 mM ZnCl2, at 25°C
0.0181
(5S)-5-[(N-benzoyl)amino]-4-oxo-6-phenylhexanoyl-L-phenylalanine
mutant enzyme V518T, in 50 mM HEPES buffer (pH 6.8) containing 200 mM NaCl, and 0.01 mM ZnCl2, at 25°C
0.000064
(5S)-5-[(N-benzoyl)amino]-4-oxo-6-phenylhexanoyl-L-tryptophan
mutant enzyme V379S, in 50 mM HEPES buffer (pH 6.8) containing 200 mM NaCl, and 0.01 mM ZnCl2, at 25°C
0.00024
(5S)-5-[(N-benzoyl)amino]-4-oxo-6-phenylhexanoyl-L-tryptophan
mutant enzyme E304R, in 50 mM HEPES buffer (pH 6.8) containing 200 mM NaCl, and 0.01 mM ZnCl2, at 25°C
0.000497
(5S)-5-[(N-benzoyl)amino]-4-oxo-6-phenylhexanoyl-L-tryptophan
mutant enzyme S516N, in 50 mM HEPES buffer (pH 6.8) containing 200 mM NaCl, and 0.01 mM ZnCl2, at 25°C
0.000618
(5S)-5-[(N-benzoyl)amino]-4-oxo-6-phenylhexanoyl-L-tryptophan
mutant enzyme D543E, in 50 mM HEPES buffer (pH 6.8) containing 200 mM NaCl, and 0.01 mM ZnCl2, at 25°C
0.000679
(5S)-5-[(N-benzoyl)amino]-4-oxo-6-phenylhexanoyl-L-tryptophan
wild type enzyme, in 50 mM HEPES buffer (pH 6.8) containing 200 mM NaCl, and 0.01 mM ZnCl2, at 25°C
0.00087
(5S)-5-[(N-benzoyl)amino]-4-oxo-6-phenylhexanoyl-L-tryptophan
mutant enzyme V379S/V380T, in 50 mM HEPES buffer (pH 6.8) containing 200 mM NaCl, and 0.01 mM ZnCl2, at 25°C
0.00087
(5S)-5-[(N-benzoyl)amino]-4-oxo-6-phenylhexanoyl-L-tryptophan
mutant enzyme V380T, in 50 mM HEPES buffer (pH 6.8) containing 200 mM NaCl, and 0.01 mM ZnCl2, at 25°C
0.00092
(5S)-5-[(N-benzoyl)amino]-4-oxo-6-phenylhexanoyl-L-tryptophan
mutant enzyme T282S, in 50 mM HEPES buffer (pH 6.8) containing 200 mM NaCl, and 0.01 mM ZnCl2, at 25°C
0.00233
(5S)-5-[(N-benzoyl)amino]-4-oxo-6-phenylhexanoyl-L-tryptophan
mutant enzyme E376D, in 50 mM HEPES buffer (pH 6.8) containing 200 mM NaCl, and 0.01 mM ZnCl2, at 25°C
0.00475
(5S)-5-[(N-benzoyl)amino]-4-oxo-6-phenylhexanoyl-L-tryptophan
mutant enzyme F391Y, in 50 mM HEPES buffer (pH 6.8) containing 200 mM NaCl, and 0.01 mM ZnCl2, at 25°C
0.00974
(5S)-5-[(N-benzoyl)amino]-4-oxo-6-phenylhexanoyl-L-tryptophan
mutant enzyme V518T, in 50 mM HEPES buffer (pH 6.8) containing 200 mM NaCl, and 0.01 mM ZnCl2, at 25°C
0.0004
(pE)KWAP
-
37°C, pH 7.0, recombinant wild-type enzyme
0.0006
(pE)KWAP
-
37°C, pH 7.0, full-length mutant containing only a functional N-domain catalytic site
0.0007
(pE)KWAP
-
37°C, pH 7.0, full-length mutant containing only a functional C-domain catalytic site
0.0008
(pE)KWAP
-
37°C, pH 7.0, enzyme from testis
0.000003
(pE)WPRPQIPP
-
37°C, pH 7.0, full-length mutant containing only a functional C-domain catalytic site
0.00001
(pE)WPRPQIPP
-
37°C, pH 7.0, enzyme from testis
0.00003
(pE)WPRPQIPP
-
37°C, pH 7.0, recombinant wild-type enzyme
0.0001
(pE)WPRPQIPP
-
37°C, pH 7.0, full-length mutant containing only a functional N-domain catalytic site
0.0018
1-[(5S)-4-oxo-6-phenyl-5-[(phenylcarbonyl)amino]hexanoyl]-L-proline
inhibition of C-domain
0.0452
1-[(5S)-4-oxo-6-phenyl-5-[(phenylcarbonyl)amino]hexanoyl]-L-proline
inhibition of N-domain
0.0336
1-[(5S)-5-[(tert-butoxycarbonyl)amino]-4-oxo-6-phenylhexanoyl]-L-proline
inhibition of N-domain
0.1435
1-[(5S)-5-[(tert-butoxycarbonyl)amino]-4-oxo-6-phenylhexanoyl]-L-proline
inhibition of C-domain
0.000006
2-(benzyloxy)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-phenylalanine
pH 7.5, angiotensin-converting enzyme 2
0.000065
2-(benzyloxy)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-phenylalanine
pH, angiotensin-converting enzyme 2
0.00077
2-(benzyloxy)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-phenylalanine
pH, angiotensin-converting enzyme
0.013
2-(benzyloxy)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-phenylalanine
pH, angiotensin-converting enzyme
0.0000024
3-(benzyloxy)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-phenylalanine
pH 7.5, angiotensin-converting enzyme 2
0.000084
3-(benzyloxy)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-phenylalanine
pH 7.5, angiotensin-converting enzyme 2
0.00075
3-(benzyloxy)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-phenylalanine
pH 7.5, angiotensin-converting enzyme
0.004
angiotensin II
C-terminal domain of sACE, pH 7.5, temperature not specified in the publication
0.076
angiotensin II
N-terminal domain of sACE, pH 7.5, temperature not specified in the publication
0.0000003
captopril
-
pH 7.5, 25°C
0.0000005
captopril
-
pH 7.5, 37°C, N-domain from lung enzyme
0.0000006
captopril
-
pH 7.5, 37°C, enzyme from lung
0.000009
captopril
-
pH 7.5, 37°C, enzyme from testis
0.000009
captopril
-
pH 8.0, 37°C, N-domain, hydrolysis of o-aminobenzoyl-SDK-(dinitrophenyl)-P-OH
0.00001
captopril
-
pH 8.0, 37°C, wild-type enzyme, hydrolysis of o-aminobenzoyl-SDK-(dinitrophenyl)-P-OH
0.000016
captopril
-
pH 8.0, 37°C, C-domain, hydrolysis of o-aminobenzoyl-FRK-(dinitrophenyl)-P-OH
0.0000165
captopril
-
pH 7.5, 20°C
0.0000166
captopril
pH 7.5, 22°C
0.000025
captopril
-
pH 8.0, 37°C, N-domain, hydrolysis of o-aminobenzoyl-FRK-(dinitrophenyl)-P-OH
0.000046
captopril
-
pH 8.0, 37°C, wild-type enzyme, hydrolysis of o-aminobenzoyl-FRK-(dinitrophenyl)-P-OH
0.000191
captopril
-
pH 8.0, 37°C, C-domain, hydrolysis of o-aminobenzoyl-SDK-(dinitrophenyl)-P-OH
0.0000001
lisinopril
-
-
0.0000001
lisinopril
-
with Abz-LFK(Dnp)-OH (C-domain), pH 7.4, 37°C
0.00000012
lisinopril
-
pH 7.5, 37°C, enzyme from testis
0.00000018
lisinopril
-
pH 7.5, 37°C, enzyme from lung
0.0000002
lisinopril
-
pH 7.5, 37°C, N-domain from lung enzyme
0.00000027
lisinopril
-
-
0.0000006
lisinopril
-
pH 7.5, 25°C
0.000001
lisinopril
-
with Abz-SDK(Dnp)P-OH (N-domain), pH 7.4, 37°C
0.0000012
lisinopril
pH 6.8, 25°C, recombinant testis ACE C-domain
0.00000126
lisinopril
-
pH 9.5, 37°C
0.00000207
lisinopril
-
-
0.0000048
lisinopril
pH 6.8, 25°C, recombinant testis ACE N-domain
0.00000996
lisinopril
-
-
0.000051
lisinopril
inhibition of C-domain
0.0001315
lisinopril
inhibition of N-domain
0.00028
lisinopril
-
pH 8.3, 37°C
0.0000066
lisW-S
pH 6.8, 25°C, recombinant testis ACE C-domain
0.0017
lisW-S
pH 6.8, 25°C, recombinant testis ACE N-domain
0.0008
LRPARPTSPP
-
37°C, pH 7.0, enzyme from testis
0.0026
LRPARPTSPP
-
37°C, pH 7.0, recombinant wild-type enzyme
0.0032
LRPARPTSPP
-
37°C, pH 7.0, full-length mutant containing only a functional C-domain catalytic site
0.017
LRPARPTSPP
-
37°C, pH 7.0, full-length mutant containing only a functional N-domain catalytic site
0.0003
LRPARPTSPPA
-
37°C, pH 7.0, enzyme from testis
0.0046
LRPARPTSPPA
-
37°C, pH 7.0, full-length mutant containing only a functional C-domain catalytic site
0.012
LRPARPTSPPA
-
37°C, pH 7.0, full-length mutant containing only a functional N-domain catalytic site
0.017
LRPARPTSPPA
-
37°C, pH 7.0, recombinant wild-type enzyme
0.0000009
N-[(2S)-3-methyl-2-sulfanylpentanoyl]-2-phenoxy-L-phenylalanine
pH 7.5, angiotensin-converting enzyme 2
0.0000016
N-[(2S)-3-methyl-2-sulfanylpentanoyl]-2-phenoxy-L-phenylalanine
pH 7.5, angiotensin-converting enzyme 2
0.0002
N-[(2S)-3-methyl-2-sulfanylpentanoyl]-2-phenoxy-L-phenylalanine
pH 7.5, angiotensin-converting enzyme
0.005
N-[(2S)-3-methyl-2-sulfanylpentanoyl]-2-phenoxy-L-phenylalanine
pH 7.5, angiotensin-converting enzyme
0.0000024
N-[(2S)-3-methyl-2-sulfanylpentanoyl]-3-phenoxy-L-phenylalanine
pH 7.5, angiotensin-converting enzyme 2
0.0000058
N-[(2S)-3-methyl-2-sulfanylpentanoyl]-3-phenoxy-L-phenylalanine
pH 7.5, angiotensin-converting enzyme 2
0.00062
N-[(2S)-3-methyl-2-sulfanylpentanoyl]-3-phenoxy-L-phenylalanine
pH 7.5, angiotensin-converting enzyme
0.0011
N-[(2S)-3-methyl-2-sulfanylpentanoyl]-3-phenoxy-L-phenylalanine
pH 7.5, angiotensin-converting enzyme
0.0000018
N-[(2S)-3-methyl-2-sulfanylpentanoyl]-O-phenyl-L-tyrosine
pH 7.5, angiotensin-converting enzyme 2
0.0000022
N-[(2S)-3-methyl-2-sulfanylpentanoyl]-O-phenyl-L-tyrosine
pH 7.5, angiotensin-converting enzyme 2
0.00025
N-[(2S)-3-methyl-2-sulfanylpentanoyl]-O-phenyl-L-tyrosine
pH 7.5, angiotensin-converting enzyme
0.0007
N-[(2S)-3-methyl-2-sulfanylpentanoyl]-O-phenyl-L-tyrosine
pH 7.5, angiotensin-converting enzyme
0.000035
N-[(2S)-3-methyl-2-sulfanylpentanoyl]-O-[4-(trifluoromethyl)benzyl]-L-tyrosine
pH 7.5, angiotensin-converting enzyme 2
0.000093
N-[(2S)-3-methyl-2-sulfanylpentanoyl]-O-[4-(trifluoromethyl)benzyl]-L-tyrosine
pH 7.5, angiotensin-converting enzyme
0.00086
N-[(2S)-3-methyl-2-sulfanylpentanoyl]-O-[4-(trifluoromethyl)benzyl]-L-tyrosine
pH 7.5, angiotensin-converting enzyme 2
0.0026
N-[(2S)-3-methyl-2-sulfanylpentanoyl]-O-[4-(trifluoromethyl)benzyl]-L-tyrosine
pH 7.5, angiotensin-converting enzyme
0.0237
N-[(5S)-4-oxo-6-phenyl-5-[(phenylcarbonyl)amino]hexanoyl]-L-phenylalanine
inhibition of C-domain
0.0843
N-[(5S)-4-oxo-6-phenyl-5-[(phenylcarbonyl)amino]hexanoyl]-L-phenylalanine
inhibition of N-domain
0.0008
N-[(5S)-4-oxo-6-phenyl-5-[(phenylcarbonyl)amino]hexanoyl]-L-tryptophan
inhibition of C-domain
0.1957
N-[(5S)-4-oxo-6-phenyl-5-[(phenylcarbonyl)amino]hexanoyl]-L-tryptophan
inhibition of N-domain
0.043
N-[(5S)-5-[(tert-butoxycarbonyl)amino]-4-oxo-6-phenylhexanoyl]-L-phenylalanine
inhibition of N-domain
0.3129
N-[(5S)-5-[(tert-butoxycarbonyl)amino]-4-oxo-6-phenylhexanoyl]-L-phenylalanine
inhibition of C-domain
0.0133
N-[(5S)-5-[(tert-butoxycarbonyl)amino]-4-oxo-6-phenylhexanoyl]-L-tryptophan
inhibition of N-domain
0.3813
N-[(5S)-5-[(tert-butoxycarbonyl)amino]-4-oxo-6-phenylhexanoyl]-L-tryptophan
inhibition of C-domain
0.000002
O-(2,4-difluorobenzyl)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-tyrosine
pH 7.5, angiotensin-converting enzyme 2
0.00042
O-(2,4-difluorobenzyl)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-tyrosine
pH 7.5, angiotensin-converting enzyme 2
0.00084
O-(2,4-difluorobenzyl)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-tyrosine
pH 7.5, angiotensin-converting enzyme
0.00095
O-(2,4-difluorobenzyl)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-tyrosine
pH 7.5, angiotensin-converting enzyme
0.0000085
O-(3,4-difluorobenzyl)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-tyrosine
pH 7.5, angiotensin-converting enzyme 2
0.00021
O-(3,4-difluorobenzyl)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-tyrosine
pH 7.5, angiotensin-converting enzyme
0.00055
O-(3,4-difluorobenzyl)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-tyrosine
pH 7.5, angiotensin-converting enzyme 2
0.0018
O-(3,4-difluorobenzyl)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-tyrosine
pH 7.5, angiotensin-converting enzyme
0.0000025
O-(4-fluorobenzyl)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-tyrosine
pH 7.5, angiotensin-converting enzyme 2
0.0000071
O-(4-fluorobenzyl)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-tyrosine
pH 7.5, angiotensin-converting enzyme 2
0.0027
O-(4-fluorobenzyl)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-tyrosine
pH 7.5, angiotensin-converting enzymepotent and long-acting DPP-IV inhibitor and effective with single daily dosing
0.004
O-(4-fluorobenzyl)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-tyrosine
pH 7.5, angiotensin-converting enzyme
0.0000014
O-benzyl-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-tyrosine
pH 7.5, angiotensin-converting enzyme 2
0.0000027
O-benzyl-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-tyrosine
pH 7.5, angiotensin-converting enzyme 2
0.0000032
O-benzyl-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-tyrosine
pH 7.5, angiotensin-converting enzyme
0.00057
O-benzyl-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-tyrosine
pH 7.5, angiotensin-converting enzyme
0.000084
O-[3,5-bis(trifluoromethyl)benzyl]-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-tyrosine
pH 7.5, angiotensin-converting enzyme 2
0.025
O-[3,5-bis(trifluoromethyl)benzyl]-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-tyrosine
pH 7.5, angiotensin-converting enzyme
0.0015
PARPTSPP
-
37°C, pH 7.0, enzyme from testis
0.0021
PARPTSPP
-
37°C, pH 7.0, full-length mutant containing only a functional C-domain catalytic site
0.0053
PARPTSPP
-
37°C, pH 7.0, recombinant wild-type enzyme
0.049
PARPTSPP
-
37°C, pH 7.0, full-length mutant containing only a functional N-domain catalytic site
0.0000015
pGlu-Asn-Trp-Pro-His-Pro-Gln-Ile-Pro-Pro
-
pH 6.8, 25°C, reaction with (7-methoxycoumarin-2-acetic acid)-Ala-Ser-Asp-Lys-(N3-(2,4-dinitrophenyl)-L-2,3-diaminopropyl), C-domain
0.0000015
pGlu-Asn-Trp-Pro-His-Pro-Gln-Ile-Pro-Pro
-
pH 6.8, 25°C, reaction with (7-methoxycoumarin-2-acetic acid)-Ser-Asp-Lys-(N3-(2,4-dinitrophenyl)-L-2,3-diaminopropyl), C-domain
0.0002
pGlu-Asn-Trp-Pro-His-Pro-Gln-Ile-Pro-Pro
-
pH 6.8, 25°C, reaction with (7-methoxycoumarin-2-acetic acid)-Ala-Ser-Asp-Lys-(N3-(2,4-dinitrophenyl)-L-2,3-diaminopropyl), N-domain
0.0002
pGlu-Asn-Trp-Pro-His-Pro-Gln-Ile-Pro-Pro
-
pH 6.8, 25°C, reaction with (7-methoxycoumarin-2-acetic acid)-Ser-Asp-Lys-(N3-(2,4-dinitrophenyl)-L-2,3-diaminopropyl), N-domain
0.00003
pGlu-Gly-Leu-Pro-Pro-Arg-Pro-Lys-Ile-Pro-Pro
-
pH 6.8, 25°C, reaction with (7-methoxycoumarin-2-acetic acid)-Ala-Ser-Asp-Lys-(N3-(2,4-dinitrophenyl)-L-2,3-diaminopropyl), C-domain
0.00003
pGlu-Gly-Leu-Pro-Pro-Arg-Pro-Lys-Ile-Pro-Pro
-
pH 6.8, 25°C, reaction with (7-methoxycoumarin-2-acetic acid)-Ser-Asp-Lys-(N3-(2,4-dinitrophenyl)-L-2,3-diaminopropyl), C-domain
0.008
pGlu-Gly-Leu-Pro-Pro-Arg-Pro-Lys-Ile-Pro-Pro
-
pH 6.8, 25°C, reaction with (7-methoxycoumarin-2-acetic acid)-Ser-Asp-Lys-(N3-(2,4-dinitrophenyl)-L-2,3-diaminopropyl), N-domain
0.01
pGlu-Gly-Leu-Pro-Pro-Arg-Pro-Lys-Ile-Pro-Pro
-
pH 6.8, 25°C, reaction with (7-methoxycoumarin-2-acetic acid)-Ala-Ser-Asp-Lys-(N3-(2,4-dinitrophenyl)-L-2,3-diaminopropyl), N-domain
0.00008
pGlu-Gly-Leu-Pro-Pro-Gly-Pro-Pro-Ile-Pro-Pro
-
pH 6.8, 25°C, reaction with (7-methoxycoumarin-2-acetic acid)-Ala-Ser-Asp-Lys-(N3-(2,4-dinitrophenyl)-L-2,3-diaminopropyl), C-domain
0.00008
pGlu-Gly-Leu-Pro-Pro-Gly-Pro-Pro-Ile-Pro-Pro
-
pH 6.8, 25°C, reaction with (7-methoxycoumarin-2-acetic acid)-Ala-Ser-Asp-Lys-(N3-(2,4-dinitrophenyl)-L-2,3-diaminopropyl), N-domain
0.00008
pGlu-Gly-Leu-Pro-Pro-Gly-Pro-Pro-Ile-Pro-Pro
-
pH 6.8, 25°C, reaction with (7-methoxycoumarin-2-acetic acid)-Ser-Asp-Lys-(N3-(2,4-dinitrophenyl)-L-2,3-diaminopropyl), C-domain
0.00008
pGlu-Gly-Leu-Pro-Pro-Gly-Pro-Pro-Ile-Pro-Pro
-
pH 6.8, 25°C, reaction with (7-methoxycoumarin-2-acetic acid)-Ser-Asp-Lys-(N3-(2,4-dinitrophenyl)-L-2,3-diaminopropyl), N-domain
0.000001
pGlu-Trp-Pro-Arg-Pro-Gln-Ile-Pro-Pro
-
pH 6.8, 25°C, reaction with (7-methoxycoumarin-2-acetic acid)-Ala-Ser-Asp-Lys-(N3-(2,4-dinitrophenyl)-L-2,3-diaminopropyl), C-domain
0.000001
pGlu-Trp-Pro-Arg-Pro-Gln-Ile-Pro-Pro
-
pH 6.8, 25°C, reaction with (7-methoxycoumarin-2-acetic acid)-Ser-Asp-Lys-(N3-(2,4-dinitrophenyl)-L-2,3-diaminopropyl), C-domain
0.0001
pGlu-Trp-Pro-Arg-Pro-Gln-Ile-Pro-Pro
-
pH 6.8, 25°C, reaction with (7-methoxycoumarin-2-acetic acid)-Ala-Ser-Asp-Lys-(N3-(2,4-dinitrophenyl)-L-2,3-diaminopropyl), N-domain
0.0001
pGlu-Trp-Pro-Arg-Pro-Gln-Ile-Pro-Pro
-
pH 6.8, 25°C, reaction with (7-methoxycoumarin-2-acetic acid)-Ser-Asp-Lys-(N3-(2,4-dinitrophenyl)-L-2,3-diaminopropyl), N-domain
0.0009
RPARPTSPP
-
37°C, pH 7.0, full-length mutant containing only a functional C-domain catalytic site
0.001
RPARPTSPP
-
37°C, pH 7.0, enzyme from testis
0.0068
RPARPTSPP
-
37°C, pH 7.0, recombinant wild-type enzyme
0.023
RPARPTSPP
-
37°C, pH 7.0, full-length mutant containing only a functional N-domain catalytic site
0.000007
RXP407
-
pH 6.8, 25°C, reaction with (7-methoxycoumarin-2-acetic acid)-Ala-Ser-Asp-Lys-(N3-(2,4-dinitrophenyl)-L-2,3-diaminopropyl), N-domain
0.000007
RXP407
-
pH 6.8, 25°C, reaction with (7-methoxycoumarin-2-acetic acid)-Ser-Asp-Lys-(N3-(2,4-dinitrophenyl)-L-2,3-diaminopropyl), N-domain
0.001
RXP407
-
pH 6.8, 25°C, reaction with (7-methoxycoumarin-2-acetic acid)-Ala-Ser-Asp-Lys-(N3-(2,4-dinitrophenyl)-L-2,3-diaminopropyl), C-domain
0.004
RXP407
-
pH 6.8, 25°C, reaction with (7-methoxycoumarin-2-acetic acid)-Ser-Asp-Lys-(N3-(2,4-dinitrophenyl)-L-2,3-diaminopropyl), C-domain
0.005
Ser-Pro-Pro
-
37°C, pH 7.0, enzyme from testis
0.0069
Ser-Pro-Pro
-
37°C, pH 7.0, recombinant wild-type enzyme
0.013
Ser-Pro-Pro
-
37°C, pH 7.0, full-length mutant containing only a functional N-domain catalytic site
0.019
Ser-Pro-Pro
-
37°C, pH 7.0, full-length mutant containing only a functional C-domain catalytic site
0.0024
SSYVHLRPARPTSPP
-
37°C, pH 7.0, enzyme from testis
0.0031
SSYVHLRPARPTSPP
-
37°C, pH 7.0, full-length mutant containing only a functional C-domain catalytic site
0.0077
SSYVHLRPARPTSPP
-
37°C, pH 7.0, recombinant wild-type enzyme
0.2
SSYVHLRPARPTSPP
-
37°C, pH 7.0, full-length mutant containing only a functional N-domain catalytic site
0.0008
YVHLRPARPTSPP
-
37°C, pH 7.0, enzyme from testis
0.002
YVHLRPARPTSPP
-
37°C, pH 7.0, full-length mutant containing only a functional C-domain catalytic site
0.0058
YVHLRPARPTSPP
-
37°C, pH 7.0, recombinant wild-type enzyme
0.01
YVHLRPARPTSPP
-
37°C, pH 7.0, full-length mutant containing only a functional N-domain catalytic site
0.000008
[CB-TE2A]1--lisinopril
-
with Abz-LFK(Dnp)-OH (C-domain), pH 7.4, 37°C
-
0.000018
[CB-TE2A]1--lisinopril
-
with Abz-SDK(Dnp)P-OH (N-domain), pH 7.4, 37°C
-
0.0003
[Co-DOTA]1--lisinopril
-
with Abz-LFK(Dnp)-OH (C-domain), pH 7.4, 37°C
-
0.0023
[Co-DOTA]1--lisinopril
-
with Abz-SDK(Dnp)P-OH (N-domain), pH 7.4, 37°C
-
0.00041
[Co-EDTA]1--lisinopril
-
with Abz-LFK(Dnp)-OH (C-domain), pH 7.4, 37°C
-
0.0027
[Co-EDTA]1--lisinopril
-
with Abz-SDK(Dnp)P-OH (N-domain), pH 7.4, 37°C
-
0.000027
[Co-GGH]0-lisinopril
-
with Abz-LFK(Dnp)-OH (C-domain), pH 7.4, 37°C
0.000189
[Co-GGH]0-lisinopril
-
with Abz-SDK(Dnp)P-OH (N-domain), pH 7.4, 37°C
0.00000012
[Co-NTA]0-lisinopril
-
with Abz-LFK(Dnp)-OH (C-domain), pH 7.4, 37°C
0.00004
[Co-NTA]0-lisinopril
-
with Abz-SDK(Dnp)P-OH (N-domain), pH 7.4, 37°C
0.000014
[Cu-CB-TE2A]1+-lisinopril
-
with Abz-LFK(Dnp)-OH (C-domain), pH 7.4, 37°C
-
0.000028
[Cu-CB-TE2A]1+-lisinopril
-
with Abz-SDK(Dnp)P-OH (N-domain), pH 7.4, 37°C
-
0.00029
[Cu-DOTA]1--lisinopril
-
with Abz-LFK(Dnp)-OH (C-domain), pH 7.4, 37°C
-
0.0018
[Cu-DOTA]1--lisinopril
-
with Abz-SDK(Dnp)P-OH (N-domain), pH 7.4, 37°C
-
0.00023
[Cu-EDTA]1--lisinopril
-
with Abz-LFK(Dnp)-OH (C-domain), pH 7.4, 37°C
-
0.0017
[Cu-EDTA]1--lisinopril
-
with Abz-SDK(Dnp)P-OH (N-domain), pH 7.4, 37°C
-
0.0001
[Cu-GGH]0-lisinopril
-
with Abz-LFK(Dnp)-OH (C-domain), pH 7.4, 37°C
0.0019
[Cu-GGH]0-lisinopril
-
with Abz-SDK(Dnp)P-OH (N-domain), pH 7.4, 37°C
0.00000033
[Cu-NTA]0-lisinopril
-
with Abz-LFK(Dnp)-OH (C-domain), pH 7.4, 37°C
0.000038
[Cu-NTA]0-lisinopril
-
with Abz-SDK(Dnp)P-OH (N-domain), pH 7.4, 37°C
0.00034
[DOTA]1--lisinopril
-
with Abz-LFK(Dnp)-OH (C-domain), pH 7.4, 37°C
-
0.0022
[DOTA]1--lisinopril
-
with Abz-SDK(Dnp)P-OH (N-domain), pH 7.4, 37°C
-
0.00014
[EDTA]3-lisinopril
-
with Abz-LFK(Dnp)-OH (C-domain), pH 7.4, 37°C
-
0.00058
[EDTA]3-lisinopril
-
with Abz-SDK(Dnp)P-OH (N-domain), pH 7.4, 37°C
-
0.000015
[Fe-CB-TE2A]2+-lisinopril
-
with Abz-LFK(Dnp)-OH (C-domain), pH 7.4, 37°C
-
0.00054
[Fe-CB-TE2A]2+-lisinopril
-
with Abz-SDK(Dnp)P-OH (N-domain), pH 7.4, 37°C
-
0.00042
[Fe-DOTA]0-lisinopril
-
with Abz-LFK(Dnp)-OH (C-domain), pH 7.4, 37°C
-
0.0021
[Fe-DOTA]0-lisinopril
-
with Abz-SDK(Dnp)P-OH (N-domain), pH 7.4, 37°C
-
0.000016
[Fe-EDTA]0-lisinopril
-
with Abz-LFK(Dnp)-OH (C-domain), pH 7.4, 37°C
-
0.00015
[Fe-EDTA]0-lisinopril
-
with Abz-SDK(Dnp)P-OH (N-domain), pH 7.4, 37°C
-
0.00000024
[Fe-NTA]1+-lisinopril
-
with Abz-LFK(Dnp)-OH (C-domain), pH 7.4, 37°C
0.000035
[Fe-NTA]1+-lisinopril
-
with Abz-SDK(Dnp)P-OH (N-domain), pH 7.4, 37°C
0.000029
[GGH]1+-lisinopril
-
with Abz-LFK(Dnp)-OH (C-domain), pH 7.4, 37°C
0.000102
[GGH]1+-lisinopril
-
with Abz-SDK(Dnp)P-OH (N-domain), pH 7.4, 37°C
0.000017
[Ni-CB-TE2A]1+-lisinopril
-
with Abz-LFK(Dnp)-OH (C-domain), pH 7.4, 37°C
-
0.000023
[Ni-CB-TE2A]1+-lisinopril
-
with Abz-SDK(Dnp)P-OH (N-domain), pH 7.4, 37°C
-
0.00045
[Ni-DOTA]1--lisinopril
-
with Abz-LFK(Dnp)-OH (C-domain), pH 7.4, 37°C
-
0.0026
[Ni-DOTA]1--lisinopril
-
with Abz-SDK(Dnp)P-OH (N-domain), pH 7.4, 37°C
-
0.00049
[Ni-EDTA]1--lisinopril
-
with Abz-LFK(Dnp)-OH (C-domain), pH 7.4, 37°C
-
0.0026
[Ni-EDTA]1--lisinopril
-
with Abz-SDK(Dnp)P-OH (N-domain), pH 7.4, 37°C
-
0.00011
[Ni-GGH]0-lisinopril
-
with Abz-LFK(Dnp)-OH (C-domain), pH 7.4, 37°C
0.001
[Ni-GGH]0-lisinopril
-
with Abz-SDK(Dnp)P-OH (N-domain), pH 7.4, 37°C
0.00000026
[Ni-NTA]0-lisinopril
-
with Abz-LFK(Dnp)-OH (C-domain), pH 7.4, 37°C
0.000033
[Ni-NTA]0-lisinopril
-
with Abz-SDK(Dnp)P-OH (N-domain), pH 7.4, 37°C
0.00000031
[NTA]2-lisinopril
-
with Abz-LFK(Dnp)-OH (C-domain), pH 7.4, 37°C
0.000057
[NTA]2-lisinopril
-
with Abz-SDK(Dnp)P-OH (N-domain), pH 7.4, 37°C
0.00009
[[(2S)-2-mercapto-3-methylpentanoyl]amino]acetic acid
pH 7.5, angiotensin-converting enzyme 2
0.00025
[[(2S)-2-mercapto-3-methylpentanoyl]amino]acetic acid
pH 7.5, angiotensin-converting enzyme
0.00052
[[(2S)-2-mercapto-3-methylpentanoyl]amino]acetic acid
pH 7.5, angiotensin-converting enzyme
0.0014
[[(2S)-2-mercapto-3-methylpentanoyl]amino]acetic acid
pH 7.5, angiotensin-converting enzyme 2
additional information
additional information
inhibition kinetics
-
additional information
additional information
inhibition kinetics of point exchange mutants with lisinopril and lisW-S, the mutants show highly decreased Ki for inhibitor lisW-S with their N-domain, overview
-
additional information
additional information
-
inhibition kinetics of point exchange mutants with lisinopril and lisW-S, the mutants show highly decreased Ki for inhibitor lisW-S with their N-domain, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1.6
(+)-catechin
Oryctolagus cuniculus
-
IC50: about 1.6 mM
1.7
(-)-epicatechin
Oryctolagus cuniculus
-
IC50: about 1.7 mM
0.219
(2E)-3-(3-amino-4-methoxyphenyl)-1-(3,4,5-trimethoxyphenyl)prop-2-en-1-one
Oryctolagus cuniculus
-
37°C
0.57
(2E)-3-(3-fluoro-4-methoxyphenyl)-1-(3,4,5-trimethoxyphenyl)prop-2-en-1-one
Oryctolagus cuniculus
-
37°C
0.246
(2E)-3-(3-hydroxy-4-methoxyphenyl)-1-(3,4,5-trimethoxyphenyl)prop-2-en-1-one
Oryctolagus cuniculus
-
37°C
0.552
(2E)-3-(3-hydroxy-4-nitrophenyl)-1-(3,4,5-trimethoxyphenyl)prop-2-en-1-one
Oryctolagus cuniculus
-
37°C
0.574
(2E)-3-(3-methoxyphenyl)-1-(3,4,5-trimethoxyphenyl)prop-2-en-1-one
Oryctolagus cuniculus
-
37°C
0.225
(2E)-3-(4-hydroxy-3-methoxyphenyl)-1-(3,4,5-trimethoxyphenyl)prop-2-en-1-one
Oryctolagus cuniculus
-
37°C
0.516
(2E)-3-(4-methoxy-3-nitrophenyl)-1-(3,4,5-trimethoxyphenyl)prop-2-en-1-one
Oryctolagus cuniculus
-
37°C
0.622
(2E)-3-(4-methoxyphenyl)-1-(3,4,5-trimethoxyphenyl)prop-2-en-1-one
Oryctolagus cuniculus
-
37°C
0.338
(2E)-3-phenyl-1-(3,4,5-trimethoxyphenyl)prop-2-en-1-one
Oryctolagus cuniculus
-
37°C
0.0033
(2S)-1-((3S)-3-amino-3-carboxypropyl)azetidine-2-carboxylic acid
Oryctolagus cuniculus
-
IC50: 0.0033 mM
0.805
1-methyl-5-phenyl-3-(3,4,5-trimethoxyphenyl)-4,5-dihydro-1H-pyrazole
Oryctolagus cuniculus
-
37°C
0.00008
2''-hydroxynicotianamide
Oryctolagus cuniculus
-
angiotensin-I converting enzyme inhibitor from buckwheat (Fagopyrum esculentum Moench) flour, IC50: 0.00008 mM
0.674
2-methoxy-4-[1-methyl-3-(3,4,5-trimethoxyphenyl)-4,5-dihydro-1H-pyrazol-5-yl]phenol
Oryctolagus cuniculus
-
37°C
0.749
2-methoxy-5-[1-methyl-3-(3,4,5-trimethoxyphenyl)-4,5-dihydro-1H-pyrazol-5-yl]aniline
Oryctolagus cuniculus
-
37°C
0.762
2-methoxy-5-[1-methyl-3-(3,4,5-trimethoxyphenyl)-4,5-dihydro-1H-pyrazol-5-yl]phenol
Oryctolagus cuniculus
-
37°C
5.95
4-hydroxybenzoic acid
0.77
5-(3-fluoro-4-methoxyphenyl)-1-methyl-3-(3,4,5-trimethoxyphenyl)-4,5-dihydro-1H-pyrazole
Oryctolagus cuniculus
-
37°C
0.889
5-(3-methoxyphenyl)-1-methyl-3-(3,4,5-trimethoxyphenyl)-4,5-dihydro-1H-pyrazole
Oryctolagus cuniculus
-
37°C
0.213
5-(4-methoxy-3-nitrophenyl)-1-methyl-3-(3,4,5-trimethoxyphenyl)-4,5-dihydro-1H-pyrazole
Oryctolagus cuniculus
-
37°C
0.435
5-(4-methoxyphenyl)-1-methyl-3-(3,4,5-trimethoxyphenyl)-4,5-dihydro-1H-pyrazole
Oryctolagus cuniculus
-
37°C
0.599
5-[1-methyl-3-(3,4,5-trimethoxyphenyl)-4,5-dihydro-1H-pyrazol-5-yl]-2-nitrophenol
Oryctolagus cuniculus
-
37°C
2.69
acteoside
Oryctolagus cuniculus
-
-
0.5279
Ala-Gly-Ser
Homo sapiens
-
-
0.0372
Ala-Gly-Ser-Pro
Homo sapiens
-
-
0.672
Ala-Gly-Ser-Ser
Homo sapiens
-
-
0.0116
Ala-His-Ser-Tyr
Homo sapiens
-
-
0.132
Ala-Ile
Rattus norvegicus
-
-
0.01
Ala-Leu-Pro-His-Ala
Homo sapiens
-
pH 8.2, 37°C
0.0017 - 0.0027
Ala-Pro-Gly-Ala-Gly-Val-Tyr
0.0183
Ala-Trp-Pro-Phe
Homo sapiens
-
pH and temperature not specified in the publication
0.0666
Ala-Val-Val
Homo sapiens
-
-
0.000038 - 0.000103
aminoethyl-chitin
0.07
angiotensin IV
Oryctolagus cuniculus
-
IC50: 0.07 mM
1.019
Arg-Met-Leu
Bos taurus
-
IC50: 1.019 mM, competitive inhibition
4.365
Arg-Phe
Alitta virens
-
IC50: 4.365 mM
0.0463
Asn-Phe
Homo sapiens
-
pH and temperature not specified in the publication
0.021
Asn-Trp-Gly-Pro-Leu-Val
Homo sapiens
-
pH and temperature not specified in the publication
0.0326
Asn-Tyr
Homo sapiens
-
pH and temperature not specified in the publication
0.00964
Asp-Asp-Thr-Gly-His-Asp-Phe-Glu-Asp-Thr-Gly-Glu-Ala-Met
Oryctolagus cuniculus
-
-
0.0123
Asp-Gly
Homo sapiens
-
pH and temperature not specified in the publication
0.0034
Asp-Ile-Gly-Tyr-Tyr
Homo sapiens
-
pH and temperature not specified in the publication
0.00048
Asp-Leu-Pro
Homo sapiens
-
pH and temperature not specified in the publication
0.0447
Asp-Phe-Gly
Homo sapiens
-
-
0.00072
Asp-Tyr-Val-Gly-Asn
Homo sapiens
-
pH and temperature not specified in the publication
0.92
ASYDTKF
Rattus norvegicus
-
-
0.00000028 - 0.00000081
benazeprilat
0.0068
bradykinin-potentiator B
Rattus norvegicus
-
-
0.031
bradykinin-potentiator C
Rattus norvegicus
-
-
3.129
caffeoyl acetate
Oryctolagus cuniculus
-
pH 8.3, 37°C
0.0000001 - 0.041
captopril
1.593
catechin
Oryctolagus cuniculus
-
IC50: 1.593 mM, competitive
0.0009
chitosan trimer
Rattus norvegicus
-
-
1.8 - 15.08
chlorogenic acid
0.1388
cyanidin-3-O-beta-D-glucoside
Oryctolagus cuniculus
-
pH 8.3, 37°C
0.1178
cyanidin-3-O-sambubioside
Oryctolagus cuniculus
-
pH 8.3, 37°C
0.1416
delphinidin-3-O-sambubioside
Oryctolagus cuniculus
-
pH 8.3, 37°C
1.729
DKIHPF
Oryctolagus cuniculus
-
-
0.9455
DQVFPMNPPK
Homo sapiens
-
-
0.73
EDENNPFYLR
Rattus norvegicus
-
-
0.552
EKERERQ
Rattus norvegicus
-
-
0.00000109
enalaprilat
Canis lupus familiaris
-
-
1.381 - 1.781
epicatechin
0.267
epicatechin dimer
Oryctolagus cuniculus
-
IC50: 0.267 mM, competitive
0.01
epicatechin hexamer
Oryctolagus cuniculus
-
IC50: 0.01 mM, competitive
0.025
epicatechin pentamer
Oryctolagus cuniculus
-
IC50: 0.025 mM, competitive
0.012
epicatechin tetramer
Oryctolagus cuniculus
-
IC50: 0.012 mM, competitive
0.126
epicatechin trimer
Oryctolagus cuniculus
-
IC50: 0.126 mM, competitive
0.3
epigallocatechin
Oryctolagus cuniculus
-
IC50: about 0.3 mM
0.00003
fosinoprilat
Xanthomonas axonopodis
-
-
0.03024
gluco-aurantioobtusin
Oryctolagus cuniculus
-
in 50 mM Tris-HCl buffer (pH 7.5)
0.0225
Gly-Asp-Ala-Pro
Homo sapiens
-
-
5.63
Gly-Gln
Bos taurus
-
IC50: 5.63 mM, competitive inhibition
0.04
Gly-Glu-Pro
Homo sapiens
-
pH and temperature not specified in the publication
0.00074
Gly-Gly-Val-Ile-Pro-Asn
Homo sapiens
-
pH and temperature not specified in the publication
0.122
Gly-His-Gly
Homo sapiens
-
-
0.0294
Gly-L-Ala-Hyp-Gly-L-Leu-Hyp-Gly-L-Pro
Oryctolagus cuniculus
-
in 100 mM sodium borate buffer (pH 8.3), 500 mM NaCl, at 37°C
0.0456
Gly-L-Ala-Hyp-Gly-L-Pro-L-Ala-Gly-L-Pro-Gly-Gly-L-Ile-Hyp-Gly-L-Glu-L-Arg-Gly
Oryctolagus cuniculus
-
in 100 mM sodium borate buffer (pH 8.3), 500 mM NaCl, at 37°C
0.0434
Gly-L-Ile-Hyp-Gly-L-Glu-L-Arg-Gly-L-Pro-L-Val-Gly-L-Pro-L-Ser-Gly
Oryctolagus cuniculus
-
in 100 mM sodium borate buffer (pH 8.3), 500 mM NaCl, at 37°C
0.0608
Gly-L-Leu-Hyp-Gly-L-Ser-L-Arg-Gly-L-Glu-L-Arg-Gly-L-Leu-Hyp-Gly
Oryctolagus cuniculus
-
in 100 mM sodium borate buffer (pH 8.3), 500 mM NaCl, at 37°C
0.00554
Gly-L-Thr-Gly
Oryctolagus cuniculus
-
in 0.02 mM sodium borate buffer (pH 8.3), at 37°C
1.62
Gly-Leu-Pro
Gadus chalcogrammus
-
IC50: 1.62 mM
10.471
Gly-Phe
Alitta virens
-
IC50: 10.471 mM
0.026
Gly-Phe-Hyp-Gly-Thr-Hyp-Gly-Leu-Hyp-Gly-Phe
Oryctolagus cuniculus
-
IC50: 0.026 mM. Inhibitory peptide derived from chicken breast muscle
252.63
Gly-Pro
Gadus chalcogrammus
-
IC50: 252.63 mM
2.65
Gly-Pro-Leu
Gadus chalcogrammus
-
IC50: 2.65 mM
0.00625
Gly-Pro-Pro
Homo sapiens
-
pH and temperature not specified in the publication
0.0718
Gly-Val-His-His-Ala
Homo sapiens
-
-
0.25 - 4
GQGGP
Oryctolagus cuniculus
-
-
0.008
HERDPTHIKWGD
Oryctolagus cuniculus
-
IC50: about 0.008 mM. Production kinetics of angiotensin-I converting enzyme inhibitory peptides from bonito meat in artificial gastric juice
0.0022
His-His-Leu
Homo sapiens
-
pH and temperature not specified in the publication
0.433
Hyp-Gly-Phe
Oryctolagus cuniculus
-
IC50: 0.433 mM
0.2
hyperosid
Sus scrofa
-
IC50: 0.2 mM
0.153
Ile-Ala
Homo sapiens
-
pH and temperature not specified in the publication
0.0042
Ile-Ala-Tyr-Lys-Pro-Ala-Gly
Homo sapiens
-
pH and temperature not specified in the publication
0.1534
Ile-Ala-Val
Homo sapiens
-
-
0.046
Ile-Asn-Ser-Gln
Homo sapiens
-
pH and temperature not specified in the publication
0.0038
Ile-Gln-Pro
Homo sapiens
-
-
0.018
Ile-Glu-Pro
Sus scrofa
-
-
0.104
Ile-Glu-Trp
Sus scrofa
-
-
0.182
Ile-Glu-Tyr
Sus scrofa
-
-
0.007
Ile-Lys-Pro
Sus scrofa
-
-
0.019
Ile-Lys-Trp
Sus scrofa
-
-
0.034
Ile-Lys-Tyr
Sus scrofa
-
-
0.0448
Ile-Phe-Leu
Homo sapiens
-
pH and temperature not specified in the publication
0.005
Ile-Pro-Pro
Homo sapiens
-
-
0.0175
Ile-Pro-Pro-Gly-Val-Pro-Tyr
Homo sapiens
-
pH and temperature not specified in the publication
0.064
Ile-Pro-Pro-Gly-Val-Pro-Tyr-Trp-Thr
Homo sapiens
-
pH and temperature not specified in the publication
0.039
Ile-Thr-Phe
Homo sapiens
-
pH and temperature not specified in the publication
0.0058
Ile-Trp-His-His-Thr
Homo sapiens
-
pH 8.2, 37°C
0.042
Ile-Tyr-Leu-Leu
Homo sapiens
-
pH and temperature not specified in the publication
0.00000278
imidaprilat
Canis lupus familiaris
-
-
0.064
IPPGVPYWT
Rattus norvegicus
-
-
2.46
isoacteoside
Oryctolagus cuniculus
-
-
0.3
isoquercitrin
Sus scrofa
-
IC50: 0.3 mM
0.4089
isorhamnetin-3-beta-glucopyranoside
Rattus norvegicus
-
IC50: 0.4089 mM
0.549
ITTNPY
Homo sapiens
-
-
0.3928
kaempferol-3-alpha-arabinopyranoside
Rattus norvegicus
-
IC50: 0.3928 mM
0.32
kaempferol-3-O-alpha-L-arabinopyranoside
Oryctolagus cuniculus
-
37°C
0.26
kaempferol-3-O-beta-D-galactopyranoside
Oryctolagus cuniculus
-
37°C
0.0466
KAPVA
Homo sapiens
-
-
0.0262
KRQKYDI
Rattus norvegicus
-
-
1
KVLPVPQ
Rattus norvegicus
-
-
0.0065
L-Ala-L-Trp
Oryctolagus cuniculus
-
in 0.1 mM sodium borate buffer, 0.3 mM NaCl, pH 8.3, at 37°C
0.00215
L-Asp-L-Pro
Oryctolagus cuniculus
-
in 0.02 mM sodium borate buffer (pH 8.3), at 37°C
0.00876
L-Glu-L-Arg-L-Tyr-L-Pro-L-Ile
Oryctolagus cuniculus
-
in 100 mM potassium phosphate buffer containing 300 mM NaCl, at 37°C
0.00878
L-Ile-L-Pro-L-Phe
Oryctolagus cuniculus
-
in 100 mM potassium phosphate buffer containing 300 mM NaCl, at 37°C
0.01059
L-Leu-L-Pro-L-Phe
Oryctolagus cuniculus
-
in 100 mM potassium phosphate buffer containing 300 mM NaCl, at 37°C
0.01798
L-Met-L-Pro-L-Phe
Oryctolagus cuniculus
-
in 100 mM potassium phosphate buffer containing 300 mM NaCl, at 37°C
0.00403
L-Ser-L-Thr
Oryctolagus cuniculus
-
in 0.02 mM sodium borate buffer (pH 8.3), at 37°C
0.02494
L-Thr-L-Thr-L-Ile
Oryctolagus cuniculus
-
in 100 mM potassium phosphate buffer containing 300 mM NaCl, at 37°C
0.02338
L-Tyr-L-Thr-L-Ala-Gly-L-Val
Oryctolagus cuniculus
-
in 100 mM potassium phosphate buffer containing 300 mM NaCl, at 37°C
0.00659
L-Val-L-Asp-L-Phe
Oryctolagus cuniculus
-
in 100 mM potassium phosphate buffer containing 300 mM NaCl, at 37°C
0.051
L-Val-L-Phe
Oryctolagus cuniculus
-
in 0.1 mM sodium borate buffer, 0.3 mM NaCl, pH 8.3, at 37°C
0.0122 - 0.02956
L-Val-L-Tyr
0.07
Leu-Ala-Ile-pro-Val-Asn-Lys-Pro
Homo sapiens
-
pH and temperature not specified in the publication
0.00038
Leu-Arg-Ile-Pro-Val-Ala
Homo sapiens
-
pH and temperature not specified in the publication
0.00021
Leu-Arg-Pro
Homo sapiens
-
-
0.0022
Leu-Gln-Pro
Homo sapiens
-
-
0.029
Leu-Gly-Ile
Homo sapiens
-
pH and temperature not specified in the publication
0.72
Leu-Gly-Pro
Gadus chalcogrammus
-
IC50: 0.72 mM
0.00082
Leu-Ile-Tyr
Oryctolagus cuniculus
-
i.e. acein-2, isolated from tryptic hydrolysate of human plasma, non-competitive inhibitor, IC50: 0.00082 mM.
5.73
Leu-Pro-Gly
Gadus chalcogrammus
-
IC50: 5.73 mM
0.0174
Leu-Trp
Oryctolagus cuniculus
-
IC50: 0.0174 mM, non-competitive
0.0064
Leu-Tyr
Homo sapiens
-
pH and temperature not specified in the publication
0.00492
LGFPTTKTYFPHF
Oryctolagus cuniculus
-
-
0.00000025 - 0.0018
lisinopril
0.0024
LKPNM
Homo sapiens
-
-
0.29
luteolin
Oryctolagus cuniculus
-
37°C
0.28
luteolin-7-O-beta-D-glucopyranoside
Oryctolagus cuniculus
-
37°C
0.0265
Lys-Asp-Tyr-Arg-Leu
Homo sapiens
-
pH and temperature not specified in the publication
0.0134
Lys-Leu-Pro-Arg-Gly-Thr-Leu-Phe
Homo sapiens
-
pH and temperature not specified in the publication
0.0006
Met-Arg-Trp
Homo sapiens
-
pH and temperature not specified in the publication
0.0021
Met-Arg-Trp-Arg-Asp
Homo sapiens
-
pH and temperature not specified in the publication
0.0098
Met-Trp
Oryctolagus cuniculus
-
IC50: 0.0098 mM, non-competitive
0.034
MLGQTPT
Homo sapiens
-
-
0.00028
mugineic acid
Oryctolagus cuniculus
-
IC50: 0.00028 mM
0.000085 - 0.442
nicotianamine
0.807
NIPPLTQTPV
Oryctolagus cuniculus
-
-
0.021
NWGPLV
Rattus norvegicus
-
-
0.25
oenothein B
Sus scrofa
-
IC50: 0.25 mM
0.5265
peimisine
Rattus norvegicus
-
IC50: 0.5265 mM
134.9
Phe-Gly
Alitta virens
-
IC50: 134.9 mM
0.0147
Phe-Gly-Ala-Ser-Thr-Arg-Gly-Ala
Oryctolagus cuniculus
-
IC50: 0.0147 mM, noncompetitive
0.0825
Phe-Gly-Gly
Homo sapiens
-
-
0.171
Phe-Hyp-Gly
Oryctolagus cuniculus
-
IC50: 0.171 mM
0.0136
Phe-Leu
Oryctolagus cuniculus
-
IC50: 0.0136 mM, non-competitive
0.037
Phe-Phe-Leu
Homo sapiens
-
pH and temperature not specified in the publication
0.0069
Phe-Val-Asn-Pro-Gln-Ala-Gly-Ser
Homo sapiens
-
pH and temperature not specified in the publication
0.0127
phlorofucofuroeckol A
Rattus norvegicus
-
-
0.001
phosphoramidon
Bos taurus
-
weak, IC50: 0.001 mM
2.17
plantainoside D
Oryctolagus cuniculus
-
-
2.47
plantamajoside
Oryctolagus cuniculus
-
-
0.033
PNNKPFQ
Rattus norvegicus
-
-
0.09533
Pro-Arg-Tyr
Oryctolagus cuniculus
pH and temperature not specified in the publication
0.033
Pro-Asn-Asn-Lys-Pro-Phe-Gln
Homo sapiens
-
pH and temperature not specified in the publication
13.93
Pro-Gly-Leu
Gadus chalcogrammus
-
IC50: 13.93 mM
337.32
Pro-Leu
Gadus chalcogrammus
-
IC50: 337.32 mM
4.74
Pro-Leu-Gly
Gadus chalcogrammus
-
IC50: 4.74 mM
0.016
Pro-Ser-Tyr
Homo sapiens
-
pH and temperature not specified in the publication
0.11
PRVF
Rattus norvegicus
-
-
0.1
PSGQYY
Rattus norvegicus
-
-
0.008
PTHIKWGD
Oryctolagus cuniculus
-
IC50: about 0.008 mM. Production kinetics of angiotensin-I converting enzyme inhibitory peptides from bonito meat in artificial gastric juice
0.2564
PTPVP
Homo sapiens
-
-
1
puqienine A
Oryctolagus cuniculus
-
37°C
0.6
puqienine B
Oryctolagus cuniculus
-
37°C
0.068
puqienine E
Oryctolagus cuniculus
-
37°C
0.16
quercetin 3-O-(6''-galloyl)-galactoside
Sus scrofa
-
IC50: 0.16 mM
0.351
quercetin 3-O-alpha-(6''-p-coumaroylglucosyl-beta -1,2-rhamnoside)
Rattus norvegicus
-
IC50: 0.351 mM
0.7088
quercetin-3-beta-glucopyranoside
Rattus norvegicus
-
IC50: 0.7088 mM
0.1589
quercetin-3-O-alpha-(6''-caffeoylglucosyl-beta-1,2-rhamnoside)
Rattus norvegicus
-
IC50: 0.1589 mM
0.31
quercetin-3-O-alpha-L-arabinopyranoside
Oryctolagus cuniculus
-
37°C
0.25
quercitrin
Sus scrofa
-
IC50: 0.25 mM
0.2
quercitrin glucuronide
Sus scrofa
-
IC50: 0.2 mM
0.16
QVVF
Rattus norvegicus
-
-
0.0000004
ramiprilat
Canis lupus familiaris
-
-
0.358
RMLGQ
Bos taurus
-
IC50: 0.358 mM, competitive inhibition
0.503
RMLGQTP
Bos taurus
-
IC50: 0.503 mM, mixed-type inhibition
0.034
RMLGQTPTK
Bos taurus
-
IC50: 0.034 mM, noncompetitive inhibition
0.1302
Ser-Phe
Homo sapiens
-
pH and temperature not specified in the publication
0.0763
Ser-Trp-Ser-Phe
Homo sapiens
-
pH and temperature not specified in the publication
0.467
SLVYPFPGPI
Oryctolagus cuniculus
-
-
0.0001
thiorphan
Bos taurus
-
weak, IC50: 0.0001 mM
0.0136
Thr-Ala-Pro-Tyr
Homo sapiens
-
pH and temperature not specified in the publication
0.0182
Thr-Gln-Val-Tyr
Homo sapiens
-
pH and temperature not specified in the publication
1.634
Thr-Lys
Bos taurus
-
IC50: 1.634 mM, mixed-type inhibition
2.071
Thr-Pro
Bos taurus
-
IC50: 2.071 mM, competitive inhibition
0.00086
Thr-Tyr-Leu-Gly-Ser
Homo sapiens
-
pH and temperature not specified in the publication
0.002
Thr-Val-Pro-Tyr
Homo sapiens
-
pH and temperature not specified in the publication
0.015
Thr-Val-Tyr
Homo sapiens
-
pH 8.2, 37°C
0.0022
Thr-Val-Val-Pro-Gly
Homo sapiens
-
pH and temperature not specified in the publication
0.2
TPRVF
Rattus norvegicus
-
-
0.2773
Trp-Ala
Oryctolagus cuniculus
-
IC50: 0.2773 mM, competitive
0.11234
Trp-Gly
Oryctolagus cuniculus
pH and temperature not specified in the publication
0.0986
Trp-Met
Oryctolagus cuniculus
-
IC50: 0.0986 mM, competitive
0.0216
Trp-Pro-Glu-Ala-Ala-Glu-Leu-Met-Met-Glu-Val-Asp-Pro
Oryctolagus cuniculus
-
-
0.57
Trp-Tyr
Oryctolagus cuniculus
-
-
0.5005
Trp-Val
Oryctolagus cuniculus
-
IC50: 0.5005 mM, competitive
0.0257
Trp-Val-Pro-Ser-Val-Tyr
Homo sapiens
-
pH and temperature not specified in the publication
0.0098
Tyr-Ala-Leu-Pro-His-Ala
Homo sapiens
-
pH 8.2, 37°C
0.004
Tyr-Gln-Tyr
Homo sapiens
-
pH and temperature not specified in the publication
0.0164
Tyr-Leu
Homo sapiens
-
pH and temperature not specified in the publication
0.014
Tyr-Leu-Ala-Gly-Asn-Gln
Homo sapiens
-
pH and temperature not specified in the publication
0.72
Tyr-Pro
Oryctolagus cuniculus
-
-
0.0105
Tyr-Pro-Lys
Homo sapiens
-
pH and temperature not specified in the publication
0.0264
Tyr-Tyr-Ala-Pro-Phe
Homo sapiens
-
pH and temperature not specified in the publication
0.083
Tyr-Tyr-Ala-Pro-Phe-Asp-Gly-Ile-Leu
Homo sapiens
-
pH and temperature not specified in the publication
0.044
Tyr-Val-Val-Phe-Lys
Homo sapiens
-
pH and temperature not specified in the publication
0.172
Val-Gly
Rattus norvegicus
-
-
0.097
Val-Ile-Glu-Lys-Tyr-Pro
Homo sapiens
-
pH and temperature not specified in the publication
0.00169
Val-Leu-Ile-Val-Pro
0.013
Val-Lys
Homo sapiens
-
pH and temperature not specified in the publication
0.0285
Val-Lys-Lys-Val-Leu-Gly-Asn-Pro
Rattus norvegicus
-
-
0.039
Val-Met-Asp-Lys-Pro-Gln-Gly
Homo sapiens
-
pH and temperature not specified in the publication
0.0092
Val-Phe
Homo sapiens
-
pH and temperature not specified in the publication
0.00046
Val-Phe-Pro-Ser
Homo sapiens
-
pH 8.2, 37°C
0.00046
Val-Phe-Pro-Tyr
Homo sapiens
-
pH and temperature not specified in the publication
0.172
Val-Pro
Rattus norvegicus
-
-
0.0824
Val-Thr-Pro-Ala-Leu-Arg
Homo sapiens
-
pH and temperature not specified in the publication
0.0055
Val-Thr-Val-Asn-Pro-Tyr-Lys-Trp-Leu-Pro
Homo sapiens
-
pH 8.2, 37°C
0.3128
verticine
Rattus norvegicus
-
IC50: 0.3128 mM
0.165
verticinone
Rattus norvegicus
-
IC50: 0.165 mM
0.00602
VVYPWT
Oryctolagus cuniculus
-
-
0.0162
YGGY
Rattus norvegicus
-
-
0.733
YGLF
Rattus norvegicus
-
-
0.044
YVVFK
Rattus norvegicus
-
-
0.000014 - 0.000023
[CB-TE2A]1--lisinopril
-
0.00062 - 0.0029
[Co-DOTA]1--lisinopril
-
0.00076 - 0.0034
[Co-EDTA]1--lisinopril
-
0.00005 - 0.00024
[Co-GGH]0-lisinopril
0.00000021 - 0.000051
[Co-NTA]0-lisinopril
0.000026 - 0.000036
[Cu-CB-TE2A]1+-lisinopril
-
0.00053 - 0.0023
[Cu-DOTA]1--lisinopril
-
0.00042 - 0.0021
[Cu-EDTA]1--lisinopril
-
0.00019 - 0.0023
[Cu-GGH]0-lisinopril
0.0000006 - 0.000048
[Cu-NTA]0-lisinopril
0.000629 - 0.0027
[DOTA]1--lisinopril
-
0.000257 - 0.00074
[EDTA]3-lisinopril
-
0.000028 - 0.00069
[Fe-CB-TE2A]2+-lisinopril
-
0.00078 - 0.0027
[Fe-DOTA]0-lisinopril
-
0.00003 - 0.00019
[Fe-EDTA]0-lisinopril
-
0.00000044 - 0.000044
[Fe-NTA]1+-lisinopril
0.000054 - 0.00013
[GGH]1+-lisinopril
0.00003 - 0.000032
[Ni-CB-TE2A]1+-lisinopril
-
0.00083 - 0.0033
[Ni-DOTA]1--lisinopril
-
0.0009 - 0.0034
[Ni-EDTA]1--lisinopril
-
0.00021 - 0.0013
[Ni-GGH]0-lisinopril
0.00000047 - 0.000042
[Ni-NTA]0-lisinopril
0.00000056 - 0.000073
[NTA]2-lisinopril
additional information
additional information
-
2.8
4-coumaric acid
Oryctolagus cuniculus
-
37°C, pH not specified in the publication
2.8
4-coumaric acid
Oryctolagus
-
pH not specified in the publication, 37°C
5.95
4-hydroxybenzoic acid
Oryctolagus cuniculus
-
37°C, pH not specified in the publication
5.95
4-hydroxybenzoic acid
Oryctolagus
-
pH not specified in the publication, 37°C
0.0151
Ala-Phe
Homo sapiens
-
pH and temperature not specified in the publication
0.165
Ala-Phe
Oryctolagus cuniculus
-
-
0.224
Ala-Phe
Rattus norvegicus
-
-
0.0017
Ala-Pro-Gly-Ala-Gly-Val-Tyr
Homo sapiens
-
pH and temperature not specified in the publication
0.0027
Ala-Pro-Gly-Ala-Gly-Val-Tyr
Homo sapiens
-
pH and temperature not specified in the publication
0.0064
Ala-Trp
Oryctolagus cuniculus
-
IC50: 0.0064 mM, non-competitive
0.199
Ala-Trp
Rattus norvegicus
-
-
0.0142
Ala-Tyr
Homo sapiens
-
pH and temperature not specified in the publication
0.1
Ala-Tyr
Homo sapiens
-
pH and temperature not specified in the publication
0.132
Ala-Tyr
Rattus norvegicus
-
-
0.000038
aminoethyl-chitin
Rattus norvegicus
-
with 50% deacetylation
0.000064
aminoethyl-chitin
Rattus norvegicus
-
with 10% deacetylation
0.000103
aminoethyl-chitin
Rattus norvegicus
-
with 90% deacetylation
0.28
apigenin
Oryctolagus cuniculus
-
37°C
0.667
apigenin
Oryctolagus cuniculus
-
37°C, pH not specified in the publication
0.667
apigenin
Oryctolagus
-
pH not specified in the publication, 37°C
0.00000028
benazeprilat
Canis lupus familiaris
-
-
0.00000053 - 0.00000081
benazeprilat
Felis catus
-
-
6.2
benzoic acid
Oryctolagus cuniculus
-
37°C, pH not specified in the publication
6.2
benzoic acid
Oryctolagus
-
pH not specified in the publication, 37°C
1.7
caffeic acid
Oryctolagus cuniculus
-
IC50: about 1.7 mM
2.1
caffeic acid
Oryctolagus cuniculus
-
37°C, pH not specified in the publication
2.1
caffeic acid
Oryctolagus
-
pH not specified in the publication, 37°C
2.527
caffeic acid
Oryctolagus cuniculus
-
pH 8.3, 37°C
0.0000001
captopril
Rattus norvegicus
-
-
0.0000014
captopril
Oryctolagus cuniculus
-
37°C
0.00000687
captopril
Oryctolagus cuniculus
-
using 3-hydroxybutyrylglycyl-glycyl-glycine as substrate, at 37°C
0.0000092
captopril
Oryctolagus cuniculus
-
pH 8.3, 37°C
0.00001
captopril
Homo sapiens
-
-
0.00001
captopril
Oryctolagus cuniculus
-
-
0.00002
captopril
Oryctolagus cuniculus
-
37°C
0.0000365
captopril
Struthio camelus australis
pH 7.5, 22°C
0.0000365
captopril
Struthio camelus
-
pH 7.5, 20°C
0.00016
captopril
Xanthomonas axonopodis
-
-
0.041
captopril
Homo sapiens
-
pH and temperature not specified in the publication
7.7
catechol
Oryctolagus cuniculus
-
37°C, pH not specified in the publication
7.7
catechol
Oryctolagus
-
pH not specified in the publication, 37°C
1.8
chlorogenic acid
Oryctolagus cuniculus
-
IC50: about 1.8 mM
15.08
chlorogenic acid
Oryctolagus cuniculus
-
pH 8.3, 37°C
0.4
ellagic acid
Sus scrofa
-
IC50: 0.4 mM
2
ellagic acid
Oryctolagus cuniculus
-
37°C, pH not specified in the publication
2
ellagic acid
Oryctolagus
-
pH not specified in the publication, 37°C
1.381
epicatechin
Oryctolagus cuniculus
-
37°C, pH not specified in the publication
1.381
epicatechin
Oryctolagus
-
pH not specified in the publication, 37°C
1.781
epicatechin
Oryctolagus cuniculus
-
IC50: 1.781 mM, competitive
4.4
ferulic acid
Oryctolagus cuniculus
-
37°C, pH not specified in the publication
4.4
ferulic acid
Oryctolagus
-
pH not specified in the publication, 37°C
10.9
ferulic acid
Oryctolagus cuniculus
-
pH 8.3, 37°C
1.7
gallic acid
Oryctolagus cuniculus
-
IC50 : about 1.7 mM
3.7
gallic acid
Oryctolagus cuniculus
-
37°C, pH not specified in the publication
3.7
gallic acid
Oryctolagus
-
pH not specified in the publication, 37°C
0.199
Gly-Trp
Rattus norvegicus
-
-
20.417
Gly-Trp
Alitta virens
-
IC50: 20.417 mM
0.0721
Gly-Tyr
Homo sapiens
-
pH and temperature not specified in the publication
0.132
Gly-Tyr
Rattus norvegicus
-
-
5.495
Gly-Tyr
Alitta virens
-
IC50: 5.495 mM
0.0047
Ile-Trp
Oryctolagus cuniculus
-
IC50: 0.0047 mM, non-competitive
0.0047
Ile-Trp
Homo sapiens
-
pH 8.2, 37°C
0.0021
Ile-Tyr
Homo sapiens
-
pH and temperature not specified in the publication
0.0021
Ile-Tyr
Homo sapiens
-
pH 8.2, 37°C
0.0034
Ile-Tyr
Homo sapiens
-
-
0.00048
Ile-Val-Tyr
Homo sapiens
-
pH and temperature not specified in the publication
0.00048
Ile-Val-Tyr
Homo sapiens
-
pH 8.2, 37°C
0.512
kaempferol
Oryctolagus cuniculus
-
37°C, pH not specified in the publication
0.512
kaempferol
Oryctolagus
-
pH not specified in the publication, 37°C
1.2
kaempferol
Oryctolagus cuniculus
-
IC50: about 1.2 mM
0.0122
L-Val-L-Tyr
Oryctolagus cuniculus
-
in 0.1 mM sodium borate buffer, 0.3 mM NaCl, pH 8.3, at 37°C
0.02956
L-Val-L-Tyr
Oryctolagus cuniculus
-
using 3-hydroxybutyrylglycyl-glycyl-glycine as substrate, at 37°C
0.126
Leu-Phe
Homo sapiens
-
pH and temperature not specified in the publication
0.3832
Leu-Phe
Oryctolagus cuniculus
-
IC50: 0.3832 mM, competitive
0.00000025
lisinopril
Homo sapiens
-
with Abz-LFK(Dnp)-OH (C-domain), pH 7.4, 37°C
0.00000057
lisinopril
Oryctolagus cuniculus
-
using 3-hydroxybutyrylglycyl-glycyl-glycine as substrate, at 37°C
0.000001
lisinopril
Sus scrofa
-
IC50: 1 nM
0.0000015
lisinopril
Homo sapiens
-
with Abz-SDK(Dnp)P-OH (N-domain), pH 7.4, 37°C
0.0018
lisinopril
Oryctolagus cuniculus
-
pH 8.3, 37°C
0.000085
nicotianamine
Oryctolagus cuniculus
-
IC50: 0.000085 mM
0.442
nicotianamine
Rattus norvegicus
-
-
0.00374
Phe-Tyr
Homo sapiens
-
pH and temperature not specified in the publication
0.025
Phe-Tyr
Homo sapiens
-
pH and temperature not specified in the publication
1.1
phloretin
Oryctolagus cuniculus
-
37°C, pH not specified in the publication
1.1
phloretin
Oryctolagus
-
pH not specified in the publication, 37°C
5.07
protocatechuic acid
Oryctolagus cuniculus
-
37°C, pH not specified in the publication
5.07
protocatechuic acid
Oryctolagus
-
pH not specified in the publication, 37°C
1.12
pyrogallol
Oryctolagus cuniculus
-
37°C, pH not specified in the publication
1.12
pyrogallol
Oryctolagus
-
pH not specified in the publication, 37°C
0.415
quercetin
Oryctolagus cuniculus
-
37°C, pH not specified in the publication
0.415
quercetin
Oryctolagus
-
pH not specified in the publication, 37°C
2
quercetin
Oryctolagus cuniculus
-
IC50: about 2.0 mM
0.97
resveratrol
Oryctolagus cuniculus
-
37°C, pH not specified in the publication
0.97
resveratrol
Oryctolagus
-
pH not specified in the publication, 37°C
1.6
resveratrol
Oryctolagus cuniculus
-
IC50: about 1.6 mM
6.359
resveratrol
Oryctolagus cuniculus
-
pH 8.3, 37°C
0.472
rutin
Oryctolagus cuniculus
-
37°C, pH not specified in the publication
0.472
rutin
Oryctolagus
-
pH not specified in the publication, 37°C
0.0663
Ser-Tyr
Homo sapiens
-
pH and temperature not specified in the publication
0.132
Ser-Tyr
Rattus norvegicus
-
-
9.3
syringic acid
Oryctolagus cuniculus
-
37°C, pH not specified in the publication
9.3
syringic acid
Oryctolagus
-
pH not specified in the publication, 37°C
0.23
Tannic acid
Oryctolagus cuniculus
-
37°C, pH not specified in the publication
0.23
Tannic acid
Oryctolagus
-
pH not specified in the publication, 37°C
0.0178
Thr-Phe
Homo sapiens
-
pH and temperature not specified in the publication
0.018
Thr-Phe
Homo sapiens
-
-
8.5
trans-cinnamic acid
Oryctolagus cuniculus
-
37°C, pH not specified in the publication
8.5
trans-cinnamic acid
Oryctolagus
-
pH not specified in the publication, 37°C
0.0299
Trp-Leu
Homo sapiens
-
pH and temperature not specified in the publication
0.0341
Trp-Leu
Oryctolagus cuniculus
-
IC50: 0.0341 mM, non-competitive
0.065
Trp-Leu
Homo sapiens
-
pH and temperature not specified in the publication
0.00169
Val-Leu-Ile-Val-Pro
Sus scrofa
-
IC50: 0.00169 mM. The peptide is resistant to digestion by proteases of the gastrointestinal tract. The antihypertensive property of this peptide derived from glycinin might find importance in the development of therapeutic functional foods
0.00169
Val-Leu-Ile-Val-Pro
Homo sapiens
-
pH and temperature not specified in the publication
0.0014
Val-Trp
Homo sapiens
-
pH 8.2, 37°C
0.0025
Val-Trp
Oryctolagus cuniculus
-
IC50: 0.0025 mM, uncompetitive
3.311
Val-Trp
Alitta virens
-
IC50: 3.311 mM
0.0071
Val-Tyr
Homo sapiens
-
pH 8.2, 37°C
0.0122
Val-Tyr
Homo sapiens
-
-
0.021
Val-Tyr
Homo sapiens
-
-
0.263
Val-Tyr
Alitta virens
-
IC50: 0.263 mM
8
vanillic acid
Oryctolagus cuniculus
-
37°C, pH not specified in the publication
8
vanillic acid
Oryctolagus
-
pH not specified in the publication, 37°C
0.000014
[CB-TE2A]1--lisinopril
Homo sapiens
-
with Abz-LFK(Dnp)-OH (C-domain), pH 7.4, 37°C
-
0.000023
[CB-TE2A]1--lisinopril
Homo sapiens
-
with Abz-SDK(Dnp)P-OH (N-domain), pH 7.4, 37°C
-
0.00062
[Co-DOTA]1--lisinopril
Homo sapiens
-
with Abz-LFK(Dnp)-OH (C-domain), pH 7.4, 37°C
-
0.0029
[Co-DOTA]1--lisinopril
Homo sapiens
-
with Abz-SDK(Dnp)P-OH (N-domain), pH 7.4, 37°C
-
0.00076
[Co-EDTA]1--lisinopril
Homo sapiens
-
with Abz-LFK(Dnp)-OH (C-domain), pH 7.4, 37°C
-
0.0034
[Co-EDTA]1--lisinopril
Homo sapiens
-
with Abz-SDK(Dnp)P-OH (N-domain), pH 7.4, 37°C
-
0.00005
[Co-GGH]0-lisinopril
Homo sapiens
-
with Abz-LFK(Dnp)-OH (C-domain), pH 7.4, 37°C
0.00024
[Co-GGH]0-lisinopril
Homo sapiens
-
with Abz-SDK(Dnp)P-OH (N-domain), pH 7.4, 37°C
0.00000021
[Co-NTA]0-lisinopril
Homo sapiens
-
with Abz-LFK(Dnp)-OH (C-domain), pH 7.4, 37°C
0.000051
[Co-NTA]0-lisinopril
Homo sapiens
-
with Abz-SDK(Dnp)P-OH (N-domain), pH 7.4, 37°C
0.000026
[Cu-CB-TE2A]1+-lisinopril
Homo sapiens
-
with Abz-LFK(Dnp)-OH (C-domain), pH 7.4, 37°C
-
0.000036
[Cu-CB-TE2A]1+-lisinopril
Homo sapiens
-
with Abz-SDK(Dnp)P-OH (N-domain), pH 7.4, 37°C
-
0.00053
[Cu-DOTA]1--lisinopril
Homo sapiens
-
with Abz-LFK(Dnp)-OH (C-domain), pH 7.4, 37°C
-
0.0023
[Cu-DOTA]1--lisinopril
Homo sapiens
-
with Abz-SDK(Dnp)P-OH (N-domain), pH 7.4, 37°C
-
0.00042
[Cu-EDTA]1--lisinopril
Homo sapiens
-
with Abz-LFK(Dnp)-OH (C-domain), pH 7.4, 37°C
-
0.0021
[Cu-EDTA]1--lisinopril
Homo sapiens
-
with Abz-SDK(Dnp)P-OH (N-domain), pH 7.4, 37°C
-
0.00019
[Cu-GGH]0-lisinopril
Homo sapiens
-
with Abz-LFK(Dnp)-OH (C-domain), pH 7.4, 37°C
0.0023
[Cu-GGH]0-lisinopril
Homo sapiens
-
with Abz-SDK(Dnp)P-OH (N-domain), pH 7.4, 37°C
0.0000006
[Cu-NTA]0-lisinopril
Homo sapiens
-
with Abz-LFK(Dnp)-OH (C-domain), pH 7.4, 37°C
0.000048
[Cu-NTA]0-lisinopril
Homo sapiens
-
with Abz-SDK(Dnp)P-OH (N-domain), pH 7.4, 37°C
0.000629
[DOTA]1--lisinopril
Homo sapiens
-
with Abz-LFK(Dnp)-OH (C-domain), pH 7.4, 37°C
-
0.0027
[DOTA]1--lisinopril
Homo sapiens
-
with Abz-SDK(Dnp)P-OH (N-domain), pH 7.4, 37°C
-
0.000257
[EDTA]3-lisinopril
Homo sapiens
-
with Abz-LFK(Dnp)-OH (C-domain), pH 7.4, 37°C
-
0.00074
[EDTA]3-lisinopril
Homo sapiens
-
with Abz-SDK(Dnp)P-OH (N-domain), pH 7.4, 37°C
-
0.000028
[Fe-CB-TE2A]2+-lisinopril
Homo sapiens
-
with Abz-LFK(Dnp)-OH (C-domain), pH 7.4, 37°C
-
0.00069
[Fe-CB-TE2A]2+-lisinopril
Homo sapiens
-
with Abz-SDK(Dnp)P-OH (N-domain), pH 7.4, 37°C
-
0.00078
[Fe-DOTA]0-lisinopril
Homo sapiens
-
with Abz-LFK(Dnp)-OH (C-domain), pH 7.4, 37°C
-
0.0027
[Fe-DOTA]0-lisinopril
Homo sapiens
-
with Abz-SDK(Dnp)P-OH (N-domain), pH 7.4, 37°C
-
0.00003
[Fe-EDTA]0-lisinopril
Homo sapiens
-
with Abz-LFK(Dnp)-OH (C-domain), pH 7.4, 37°C
-
0.00019
[Fe-EDTA]0-lisinopril
Homo sapiens
-
with Abz-SDK(Dnp)P-OH (N-domain), pH 7.4, 37°C
-
0.00000044
[Fe-NTA]1+-lisinopril
Homo sapiens
-
with Abz-LFK(Dnp)-OH (C-domain), pH 7.4, 37°C
0.000044
[Fe-NTA]1+-lisinopril
Homo sapiens
-
with Abz-SDK(Dnp)P-OH (N-domain), pH 7.4, 37°C
0.000054
[GGH]1+-lisinopril
Homo sapiens
-
with Abz-LFK(Dnp)-OH (C-domain), pH 7.4, 37°C
0.00013
[GGH]1+-lisinopril
Homo sapiens
-
with Abz-SDK(Dnp)P-OH (N-domain), pH 7.4, 37°C
0.00003
[Ni-CB-TE2A]1+-lisinopril
Homo sapiens
-
with Abz-SDK(Dnp)P-OH (N-domain), pH 7.4, 37°C
-
0.000032
[Ni-CB-TE2A]1+-lisinopril
Homo sapiens
-
with Abz-LFK(Dnp)-OH (C-domain), pH 7.4, 37°C
-
0.00083
[Ni-DOTA]1--lisinopril
Homo sapiens
-
with Abz-LFK(Dnp)-OH (C-domain), pH 7.4, 37°C
-
0.0033
[Ni-DOTA]1--lisinopril
Homo sapiens
-
with Abz-SDK(Dnp)P-OH (N-domain), pH 7.4, 37°C
-
0.0009
[Ni-EDTA]1--lisinopril
Homo sapiens
-
with Abz-LFK(Dnp)-OH (C-domain), pH 7.4, 37°C
-
0.0034
[Ni-EDTA]1--lisinopril
Homo sapiens
-
with Abz-SDK(Dnp)P-OH (N-domain), pH 7.4, 37°C
-
0.00021
[Ni-GGH]0-lisinopril
Homo sapiens
-
with Abz-LFK(Dnp)-OH (C-domain), pH 7.4, 37°C
0.0013
[Ni-GGH]0-lisinopril
Homo sapiens
-
with Abz-SDK(Dnp)P-OH (N-domain), pH 7.4, 37°C
0.00000047
[Ni-NTA]0-lisinopril
Homo sapiens
-
with Abz-LFK(Dnp)-OH (C-domain), pH 7.4, 37°C
0.000042
[Ni-NTA]0-lisinopril
Homo sapiens
-
with Abz-SDK(Dnp)P-OH (N-domain), pH 7.4, 37°C
0.00000056
[NTA]2-lisinopril
Homo sapiens
-
with Abz-LFK(Dnp)-OH (C-domain), pH 7.4, 37°C
0.000073
[NTA]2-lisinopril
Homo sapiens
-
with Abz-SDK(Dnp)P-OH (N-domain), pH 7.4, 37°C
additional information
additional information
Sus scrofa
-
IC50-value of peptides purified from sunflower hydrolysate: 0.00118 mg/ml, IC50-value of peptides purified from rapeseed hydrolysate: 0.00025 mg/ml
-
additional information
additional information
Oryctolagus cuniculus
-
IC50-value of peptides purified from sunflower hydrolysate: 0.0023 mg/ml
-
additional information
additional information
Oryctolagus cuniculus
-
IC50 value of alcalase hydrolysate of Brachionus rotundiformis inhibitory peptides for ACE inhibitory activity is 0.63 mg/ml
-
additional information
additional information
Homo sapiens
-
IC50 values are 0.6179-0.5860 mM per 0.1-0.4 mg/l proteinhydrolysate BCAA-rich fraction, the FPH-mix with highest Fischer ratio, mixed-type inhibition pattern, inhibition kinetics of flaxseed peptides, overview
-
additional information
additional information
Homo sapiens
-
IC50 values for different parts of the milled wheat seed
-
additional information
additional information
Rattus norvegicus
-
IC50 values of nicotianamine, Val-Gly, Gly-Tyr, Ser-Tyr, Ala-Tyr, Ala-Ile, Val-Pro, Ala-Phe, Gly-Trp, and Ala-Trp are 0.442 mg/ml, 0.172 mg/ml, 0.132 mg/ml, 0.132 mg/ml, 0.132 mg/ml, 0.132 mg/ml, 0.172 mg/ml, 0.224 mg/ml, 0.199 mg/ml, and 0.199 mg/ml
-
additional information
additional information
Homo sapiens
-
nutrient sources of ACE inhibitory peptides derived from marine organisms, enzymes used for hydrolysis, and IC50 values, overview
-
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