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Information on EC 3.4.15.1 - peptidyl-dipeptidase A and Organism(s) Homo sapiens and UniProt Accession Q9BYF1

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.15 Peptidyl-dipeptidases
                3.4.15.1 peptidyl-dipeptidase A
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Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: Q9BYF1 not found.
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
release of a C-terminal dipeptide, oligopeptide-/-Xaa-Yaa, when Xaa is not Pro, and Yaa is neither Asp nor Glu. Thus, conversion of angiotensin I to angiotensin II, with increase in vasoconstrictor activity, but no action on angiotensin II
Synonyms
angiotensin-converting enzyme, angiotensin converting enzyme, angiotensin converting enzyme inhibitor, angiotensin i-converting enzyme, angiotensin-converting-enzyme, angiotensin i converting enzyme, ace-1, kininase ii, angiotensin-i converting enzyme, angiotensin-converting enzyme-2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
angiotensin-converting enzyme 2
-
ACE2
-
-
angiotensin 1 converting enzyme
-
-
-
-
angiotensin converting enzyme
angiotensin converting enzyme inhibitor
-
-
angiotensin I converting enzyme
-
-
angiotensin I-converting enzyme
angiotensin-converting enzyme
angiotensin-converting enzyme type 1
-
angiotensin-converting enzyme-2
-
-
angiotensin-converting-enzyme
-
-
angiotensin-I converting enzyme
-
angiotensin-I-converting enzyme
carboxycathepsin
-
-
-
-
carboxypeptidase, dipeptidyl
-
-
-
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CD143
CD143 antigen
-
-
-
-
Dipeptidyl carboxypeptidase
-
-
-
-
dipeptidyl carboxypeptidase I
-
-
-
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endothelial cell peptidyl dipeptidase
-
-
-
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gACE
-
-
germinal ACE
-
-
kininase II
PDH
-
-
-
-
peptidase P
-
-
-
-
peptidyl dipeptidase
peptidyl dipeptidase A
-
-
-
-
peptidyl dipeptidase I
-
-
-
-
peptidyl dipeptidase-4
-
-
-
-
peptidyl dipeptide hydrolase
-
-
-
-
peptidyl-dipeptide hydrolase
-
-
-
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peptidyldipeptide hydrolase
-
-
-
-
rhACE2
-
-
sACE-1
-
-
somatic ACE
somatic angiotensin I-converting enzyme
-
testicular ACE
-
-
testis ACE
-
Zn2+ peptidyldipeptidase
-
additional information
-
ACE is a M2 family metallopeptidase
CAS REGISTRY NUMBER
COMMENTARY hide
9015-82-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
MCA-Tyr-Val-Ala-Asp-Ala-Pro-Lys(DNP)-OH + H2O
?
show the reaction diagram
(7-methoxycoumarin-2-acetic acid)-Ala-Ser-Asp-Lys-(N3-(2,4-dinitrophenyl)-L-2,3-diaminopropyl) + H2O
?
show the reaction diagram
-
-
-
?
(7-methoxycoumarin-2-acetic acid)-Ser-Asp-Lys-(N3-(2,4-dinitrophenyl)-L-2,3-diaminopropyl) + H2O
?
show the reaction diagram
-
-
-
?
(7-methoxycoumarin-2-acetyl)-Tyr-Val-Ala-Asp-Ala-Phe-Lys-(2,4-dinitrophenyl)-OH + H2O
?
show the reaction diagram
-
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Ala-Ser-Asp-Lys-N3-(2,4-dinitrophenyl)-L-diaminopropionionate + H2O
?
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Ala-Ala-Leu-Ala-Gly-nitrobenzylamide + H2O
?
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Ala-Ala-Tyr-Leu-Ala-Gly-nitrobenzylamide + H2O
?
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Ala-Tyr-Leu-Ala-Gly-nitrobenzylamide + H2O
?
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Val-Tyr-Leu-Ala-Gly-nitrobenzylamide + H2O
?
show the reaction diagram
-
-
-
-
?
2-furanacryloyl-Phe-Gly-Gly + H2O
2-furanacryloyl-Phe + Gly-Gly
show the reaction diagram
3-hydroxybutyryl-Gly-Gly-Gly + H2O
3-hydroxybutyryl-Gly + Gly-Gly
show the reaction diagram
-
-
-
-
?
Abz-LFK(Dnp)-OH + H2O
Abz-Leu-Phe + N6-(2,4-dinitrophenyl)-L-lysine
show the reaction diagram
-
-
-
-
?
Abz-SDK(Dnp)P-OH + H2O
Abz-Ser-Asp + Lys(Dnp)-Pro
show the reaction diagram
-
-
-
-
?
Abz-YRK(2,4-dinitrophenyl)P + H2O
?
show the reaction diagram
-
-
-
-
?
amyloid beta-peptide(1-40) + H2O
amyloid beta-peptide(1-7) + amyloid beta-peptide(8-40)
show the reaction diagram
amyloid beta-protein 1-40 + H2O
amyloid beta-peptide(1-7) + amyloid beta-peptide(8-40)
show the reaction diagram
-
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)
show the reaction diagram
-
ACE cleaves amyloid beta-protein 1-42 at multiple sites
-
-
?
amyloid beta-protein 1-42 + H2O
amyloid beta-protein 1-420 + ?
show the reaction diagram
-
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 Alzheimer’s disease
-
-
?
angiotensin (1-9) + H2O
?
show the reaction diagram
-
-
-
-
?
angiotensin I + H2O
?
show the reaction diagram
-
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
show the reaction diagram
angiotensin I + H2O
angiotensin II + L-His-L-Leu
show the reaction diagram
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met + H2O
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly + Leu-Met
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
benzoyl-Gly-Gly-Gly + H2O
benzoyl-Gly + Gly-Gly
show the reaction diagram
-
-
-
-
?
benzoyl-Gly-His-Leu + H2O
benzoyl-Gly + His-Leu
show the reaction diagram
-
-
-
-
?
benzoyl-Gly-Phe-Arg + H2O
benzoyl-Gly + Phe-Arg
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Gly-Gly-Gly + H2O
benzyloxycarbonyl-Gly + Gly-Gly
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Leu-Gly-Gly + H2O
benzyloxycarbonyl-Leu + Gly-Gly
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Phe-His-Leu + H2O
?
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Phe-His-Leu + H2O
benzyloxycarbonyl-Phe + His-Leu
show the reaction diagram
bradykinin + H2O
?
show the reaction diagram
bradykinin + H2O
Phe-Arg + Ser-Pro + Arg-Pro-Pro-Gly-Phe
show the reaction diagram
-
-
-
-
?
furanacryloyl-L-Phe-Gly-Gly + H2O
furanacryloyl-L-Phe + Gly-Gly
show the reaction diagram
-
-
-
-
?
Gly-Gly-Tyr-Arg + H2O
Gly-Gly + Tyr-Arg
show the reaction diagram
-
-
-
?
gonadotropin-releasing hormone + H2O
?
show the reaction diagram
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
-
-
?
Hip-His-Leu + H2O
?
show the reaction diagram
hippuryl-Gly-Gly + H2O
hippuric acid + Gly-Gly
show the reaction diagram
-
-
-
-
?
hippuryl-His-Leu + H2O
hippuric acid + His-Leu
show the reaction diagram
hippuryl-histidyl-leucine + H2O
?
show the reaction diagram
-
-
-
?
hippuryl-L-His-L-Leu + H2O
hippuric acid + L-His-L-Leu
show the reaction diagram
hippuryl-Phe-Arg + H2O
hippuric acid + Phe-Arg
show the reaction diagram
-
-
-
-
?
LEQIYHL + H2O
?
show the reaction diagram
-
-
-
?
Leu5-enkephalin + H2O
Tyr-Gly-Gly + Phe-Leu
show the reaction diagram
-
-
-
-
?
MCA-Ala-Ser-Asp-Lys-Dap(DNP)-OH + H2O
?
show the reaction diagram
Mca-RPPGFSAFK(Dnp)-OH + H2O
?
show the reaction diagram
-
-
-
-
?
Met5-enkephalin + H2O
Tyr-Gly-Gly + Phe-Met
show the reaction diagram
-
-
-
-
?
N-benzyloxycarbonyl-L-Phe-L-His-L-Leu + H2O
N-benzyloxycarbonyl-L-Phe + L-His-L-Leu
show the reaction diagram
-
-
-
-
?
N-benzyloxycarbonyl-Phe-His-Leu + H2O
N-benzyloxycarbonyl-Phe + His-Leu
show the reaction diagram
-
-
-
?
neurotensin + H2O
pGlu-Leu-Tyr-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Tyr + Ile-Leu
show the reaction diagram
-
-
-
-
?
NKLKPSQ + H2O
?
show the reaction diagram
-
-
-
?
NKLKPSQWI + H2O
?
show the reaction diagram
-
-
-
?
NKLKPSQWISL + H2O
?
show the reaction diagram
-
-
-
?
NKLKPSQWISLSD + H2O
?
show the reaction diagram
-
-
-
?
o-aminobenzoyl-FDK-(dinitrophenyl)-P-OH + H2O
o-aminobenzoyl-FD + K-(dinitrophenyl)-P-OH
show the reaction diagram
-
-
-
?
o-aminobenzoyl-FRK-(dinitrophenyl)-P-OH + H2O
o-aminobenzoyl-FR + K-(dinitrophenyl)-P-OH
show the reaction diagram
-
-
-
?
o-aminobenzoyl-GFSPFAQ-(N-2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoyl-GFSPFA + Gln-(N-2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
o-aminobenzoyl-GFSPFEQ-(N-2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoyl-GFSPFE + Gln-(N-2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
o-aminobenzoyl-GFSPFFQ-(N-2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoyl-GFSPFF + Gln-(N-2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
o-aminobenzoyl-GFSPFLQ-(N-2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoyl-GFSPFL + Gln-(N-2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
o-aminobenzoyl-GFSPFQQ-(N-2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoyl-GFSPFQ + Gln-(N-2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
o-aminobenzoyl-GFSPFRA-(N-2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoyl-GFSPFR + Ala-(N-2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
o-aminobenzoyl-GFSPFRF-(N-2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoyl-GFSPFR + Phe-(N-2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
o-aminobenzoyl-GFSPFRI-(N-2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoyl-GFSPFR + Ile-(N-2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
o-aminobenzoyl-GFSPFRN-(N-2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoyl-GFSPFR + Asn-(N-2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
o-aminobenzoyl-GFSPFRQ-(N-2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoyl-GFSPFR + Gln-(N-2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
o-aminobenzoyl-GFSPFRR-(N-2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoyl-GFSPFR + Arg-(N-2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
o-aminobenzoyl-GFSPFRS-(N-2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoyl-GFSPFR + Ser-(N-2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
o-aminobenzoyl-GFSPFSQ-(N-2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoyl-GFSPFS + Gln-(N-2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
o-aminobenzoyl-Phe-Arg-Lys(2,4-dinitrophenyl)-Pro-hydroxide + H2O
?
show the reaction diagram
-
-
-
?
o-aminobenzoyl-SDK-(dinitrophenyl)-P-OH + H2O
o-aminobenzoyl-SD + K-(dinitrophenyl)-P-OH
show the reaction diagram
-
-
-
?
o-aminobenzoyl-SRK-(dinitrophenyl)-P-OH + H2O
o-aminobenzoyl-SR + K-(dinitrophenyl)-P-OH
show the reaction diagram
-
-
-
?
o-aminobenzoyl-TDK-(dinitrophenyl)-P-OH + H2O
o-aminobenzoyl-TD + K-(dinitrophenyl)-P-OH
show the reaction diagram
-
-
-
?
o-aminobenzoyl-TRK-(dinitrophenyl)-P-OH + H2O
o-aminobenzoyl-TR + K-(dinitrophenyl)-P-OH
show the reaction diagram
-
-
-
?
o-aminobenzoyl-YDK-(dinitrophenyl)-P-OH + H2O
o-aminobenzoyl-YD + K-(dinitrophenyl)-P-OH
show the reaction diagram
-
-
-
?
o-aminobenzoyl-YRK-(dinitrophenyl)-P-OH + H2O
o-aminobenzoyl-YR + K-(dinitrophenyl)-P-OH
show the reaction diagram
-
-
-
?
p-hydroxyhippuryl-His-Leu + H2O
?
show the reaction diagram
-
-
-
?
p-nitrobenzyloxycarbonyl-Gly + H2O
?
show the reaction diagram
-
-
-
-
?
p-nitrobenzyloxycarbonyl-Gly-Gly-Gly + H2O
?
show the reaction diagram
-
-
-
-
?
SLKPSNWLTPSE + H2O
?
show the reaction diagram
-
-
-
?
Substance P + H2O
?
show the reaction diagram
-
-
-
-
?
tert-butoxycarbonyl-Phe-Ala-Pro + H2O
tert-butoxycarbonyl-Phe + Ala-Pro
show the reaction diagram
-
-
-
-
?
Z-Phe-His-Leu + H2O
Z-Phe + His-Leu
show the reaction diagram
-
-
-
?
Z-phenylalanyl-histidyl-leucine + H2O
Z-phenylalanine + histidyl-leucine
show the reaction diagram
-
-
-
?
[Arg10]angiotensin I + H2O
?
show the reaction diagram
-
-
-
-
?
[Phe9,Arg10]angiotensin I + H2O
?
show the reaction diagram
-
-
-
-
?
[Phe9]angiotensin I + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
amyloid beta-peptide(1-40) + H2O
amyloid beta-peptide(1-7) + amyloid beta-peptide(8-40)
show the reaction diagram
-
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 Alzheimer‘s disease
-
?
amyloid beta-protein 1-40 + H2O
amyloid beta-peptide(1-7) + amyloid beta-peptide(8-40)
show the reaction diagram
-
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)
show the reaction diagram
-
ACE cleaves amyloid beta-protein 1-42 at multiple sites
-
-
?
amyloid beta-protein 1-42 + H2O
amyloid beta-protein 1-420 + ?
show the reaction diagram
-
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 Alzheimer’s disease
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
show the reaction diagram
angiotensin I + H2O
angiotensin II + L-His-L-Leu
show the reaction diagram
bradykinin + H2O
?
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CaCl2
-
activates in absence of Cl-, maximal activity at 0.3 mM
Cl-
-
the activity of the C-domain of sACE depends highly on chloride ion concentration and is inactive in its absence, whereas the N-domain can be completely activated at relatively low concentrations of this anion and is still active in the absence of chloride
Na2SO4
-
activates in absence of Cl-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(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
2-(benzyloxy)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-phenylalanine
3-(benzyloxy)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-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]-O-phenyl-L-tyrosine
N-[(2S)-3-methyl-2-sulfanylpentanoyl]-O-[4-(trifluoromethyl)benzyl]-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-(4-fluorobenzyl)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-tyrosine
O-benzyl-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-tyrosine
O-[3,5-bis(trifluoromethyl)benzyl]-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-tyrosine
-
[[(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
-
(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
(pE)KWAP
-
-
(pE)WPRPQIPP
-
-
1,10-phenanthroline
-
-
1-Fluoro-2,4-dinitrobenzene
-
1 mM, 96% inhibition of N-domain ACE
1-[(5S)-4-oxo-6-phenyl-5-[(phenylcarbonyl)amino]hexanoyl]-L-proline
-
1-[(5S)-5-[(tert-butoxycarbonyl)amino]-4-oxo-6-phenylhexanoyl]-L-proline
-
15 B1
-
-
15 B2
-
-
2,3-dimercapto-1-propanol
-
-
2-(benzyloxy)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-phenylalanine
2-mercaptoethanol
-
-
2-[([2-[(1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]cyclopentyl]carbonyl)amino]-3-(2,3-dihydro-1H-indol-3-yl)propanoate
-
3-(benzyloxy)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-phenylalanine
3-mercapto-2-D-methylpropanoyl-L-Pro
-
i.e. SQ-14,225
8-hydroxyquinoline
-
-
A 58365A
-
-
A 58365B
-
-
Ala-Gly-Ser
-
-
Ala-Gly-Ser-Pro
-
-
Ala-Gly-Ser-Ser
-
-
Ala-His-Ser-Tyr
-
a noncompetitive inhibitor, the peptide is resistant to further degenration by pepsin, trypsin, and chymotrypsin
Ala-Leu-Pro-His-Ala
-
-
Ala-Phe
-
-
Ala-Pro-Gly-Ala-Gly-Val-Tyr
-
-
Ala-Trp-Pro-Phe
-
-
Ala-Tyr
-
-
Ala-Val-Val
-
-
alcacepril
-
synthetic ACE inhibitor and antihypertensive drug
ancovenin
-
-
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
-
-
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 II
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
-
Arg-Pro-Pro
-
inhibition of enzyme form I and II, enzyme form III is not inhibited
Asn-Phe
-
-
Asn-Trp-Gly-Pro-Leu-Val
-
-
Asn-Tyr
-
-
Asp-Gly
-
-
Asp-Ile-Gly-Tyr-Tyr
-
-
Asp-Leu-Pro
-
-
Asp-Phe-Gly
-
-
Asp-Tyr-Val-Gly-Asn
-
-
aspergillomarasmine A
-
-
aspergillomarasmine B
-
-
benazepril
benzapril
-
-
bradykinin
-
-
bradykinin potentiating peptide b
interaction with sACE in a Zn-dependent manner
-
bradykinin potentiator C
bradykinin-potentiating factor SQ 20881
-
-
bradykinin-potentiating peptide 9a
-
-
captopril
CGS-35066
-
-
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
-
cilazapril
-
-
D-3-thio-2-methylpropanoyl-Pro
-
-
D-Cys-L-Pro
-
competitive to hippuryl-His-Leu
dieckol
-
deribed from Ecklonia stolonifera
dithiothreitol
-
-
DQVFPMNPPK
-
-
eckol
-
derived from Ecklonia stolonifera
enalapril
enalaprilat
enalaprilate
enaprilat
-
-
FDKPVSPL
-
-
foroxymithine
-
-
fosinopril
Gly-Asp-Ala-Pro
-
-
Gly-Glu-Pro
-
-
Gly-Gly-Val-Ile-Pro-Asn
-
-
Gly-His-Gly
-
-
Gly-Pro-Pro
-
-
Gly-Tyr
-
-
Gly-Val-His-His-Ala
-
-
guanethidine
-
weak
H2S
-
Zn2+ but not Cd2+, Ca2+ or Mg2+ could counteract the inhibitory effect
His-His-Leu
-
-
Ile-Ala
-
-
Ile-Ala-Tyr-Lys-Pro-Ala-Gly
-
-
Ile-Ala-Val
-
-
Ile-Asn-Ser-Gln
-
-
Ile-Gln-Pro
-
-
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-Phe-Leu
-
-
Ile-Pro-Pro
Ile-Pro-Pro-Gly-Val-Pro-Tyr
-
-
Ile-Pro-Pro-Gly-Val-Pro-Tyr-Trp-Thr
-
-
Ile-Thr-Phe
-
-
Ile-Trp
-
-
Ile-Trp-His-His-Thr
-
-
Ile-Tyr-Leu-Leu
-
-
Ile-Val-Tyr
-
-
imidapril
-
-
ITTNPY
-
-
K-13
-
-
K-26
-
-
KAPVA
-
a peptide derived from muscle titin
L-681,176
-
-
L-Ala-L-Trp
-
-
L-Cys-L-Pro
-
-
L-Val-L-Phe
-
-
L-Val-L-Tyr
-
-
Leu-Ala-Ile-pro-Val-Asn-Lys-Pro
-
-
Leu-Arg-Ile-Pro-Val-Ala
-
-
Leu-Arg-Pro
-
-
Leu-Gln-Pro
-
-
Leu-Gly-Ile
-
-
Leu-Phe
-
-
Leu-Tyr
-
-
LFDKPVSPL
-
-
lisinopril
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
LKPNM
-
-
LRPARPTSPP
-
-
LRPARPTSPPA
-
-
Lys-Asp-Tyr-Arg-Leu
-
-
Lys-Leu-Pro-Arg-Gly-Thr-Leu-Phe
-
-
Met-Arg-Trp
-
-
Met-Arg-Trp-Arg-Asp
-
-
MLGQTPT
-
-
muracein A
-
-
muracein B
-
-
muracein C
-
-
MYPGIA
-
-
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-[(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-[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
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-[3,5-bis(trifluoromethyl)benzyl]-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-tyrosine
-
omapatrilat
-
-
PARPTSPP
-
-
perindopril
perindoprilat
-
-
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-Gly-Gly
-
-
Phe-Phe-Leu
-
-
Phe-Tyr
-
-
Phe-Val-Asn-Pro-Gln-Ala-Gly-Ser
-
-
phenacein
-
-
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
-
phosphoramidon
-
-
Pro-Asn-Asn-Lys-Pro-Phe-Gln
-
-
Pro-Ser-Tyr
-
-
PTPVP
-
a peptide derived from muscle titin
Pyr-Trp-Pro-Arg-Pro-Gln-Ile-Pro
-
therapeutical useful
quinapril
quinaprilat
-
-
ramipril
ramiprilat
rampiril
-
-
RPARPTSPP
-
-
RVAPEEHPT
-
-
RXP407
-
-
RXPA380
SCH 54470
-
-
Ser-Phe
-
-
Ser-Pro-Pro
-
-
Ser-Trp-Ser-Phe
-
-
Ser-Tyr
-
-
snake venom peptide
-
-
-
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
-
spirapril
-
-
SSYVHLRPARPTSPP
-
-
talopeptin
-
-
tannin
-
-
-
temocapril
-
chronic treatment with temocapril improves the carotid arterial stiffness in healthy, normotensive elderly, and hence may reduce their risk for cardiovascular disease
Teprotide
Thr-Ala-Pro-Tyr
-
-
Thr-Gln-Val-Tyr
-
-
Thr-Phe
-
-
Thr-Tyr-Leu-Gly-Ser
-
-
Thr-Val-Pro-Tyr
-
-
Thr-Val-Tyr
-
-
Thr-Val-Val-Pro-Gly
-
-
trandolapril
-
the angiotensin-converting enzyme inhibitor has no effect on the rate of endothelial apoptosis in vitro in HUVEC cells
trandolaprilat
-
-
Trp-Leu
-
-
Trp-Val-Pro-Ser-Val-Tyr
-
-
Tyr-Ala-Leu-Pro-His-Ala
-
-
Tyr-Gln-Tyr
-
-
Tyr-Leu
-
-
Tyr-Leu-Ala-Gly-Asn-Gln
-
-
Tyr-Pro-Lys
-
-
Tyr-Tyr-Ala-Pro-Phe
-
-
Tyr-Tyr-Ala-Pro-Phe-Asp-Gly-Ile-Leu
-
-
Tyr-Val-Val-Phe-Lys
-
-
Urea
-
weak
Val-Ile-Glu-Lys-Tyr-Pro
-
-
Val-Leu-Ile-Val-Pro
-
-
Val-Lys
-
-
Val-Met-Asp-Lys-Pro-Gln-Gly
-
-
Val-Phe
-
-
Val-Phe-Pro-Ser
-
-
Val-Phe-Pro-Tyr
-
-
Val-Pro-Pro
Val-Thr-Pro-Ala-Leu-Arg
-
-
Val-Thr-Val-Asn-Pro-Tyr-Lys-Trp-Leu-Pro
-
-
Val-Trp
-
-
VAPEEHPT
-
-
VIPEL
-
-
warfarin
-
-
WF-10,129
-
-
YVHLRPARPTSPP
-
-
zofenpril
-
-
[CB-TE2A]1--lisinopril
-
-
-
[Co-DOTA]1--lisinopril
-
-
-
[Co-EDTA]1--lisinopril
-
-
-
[Co-GGH]0-lisinopril
-
-
[Co-NTA]0-lisinopril
-
-
[Cu-CB-TE2A]1+-lisinopril
-
-
-
[Cu-DOTA]1--lisinopril
-
-
-
[Cu-EDTA]1--lisinopril
-
-
-
[Cu-GGH]0-lisinopril
-
-
[Cu-NTA]0-lisinopril
-
-
[DOTA]1--lisinopril
-
-
-
[EDTA]3-lisinopril
-
-
-
[Fe-CB-TE2A]2+-lisinopril
-
-
-
[Fe-DOTA]0-lisinopril
-
-
-
[Fe-EDTA]0-lisinopril
-
-
-
[Fe-NTA]1+-lisinopril
-
-
[GGH]1+-lisinopril
-
-
[Ni-CB-TE2A]1+-lisinopril
-
-
-
[Ni-DOTA]1--lisinopril
-
-
-
[Ni-EDTA]1--lisinopril
-
-
-
[Ni-GGH]0-lisinopril
-
-
[Ni-NTA]0-lisinopril
-
-
[NTA]2-lisinopril
-
-
[[(2S)-2-mercapto-3-methylpentanoyl]amino]acetic acid
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.136 - 0.174
2-furanacryloyl-Phe-Gly-Gly
28.54
3-hydroxybutyryl-Gly-Gly-Gly
-
37°C
0.012
Abz-LFK(Dnp)-OH
-
pH 7.4, 37°C
0.035
Abz-SDK(Dnp)P-OH
-
pH 7.4, 37°C
0.007
amyloid beta-protein 1-42
-
-
-
0.028
angiotensin
-
37°C
0.01 - 0.54
angiotensin I
0.002
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met
-
-
6.2
benzoyl-Gly-Gly-Gly
-
-
1.2 - 1.3
benzoyl-Gly-His-Leu
0.6
benzoyl-Gly-Phe-Arg
-
-
0.3 - 2.8
benzyloxycarbonyl-Phe-His-Leu
0.0004
bradykinin
-
-
0.5 - 3
hippuryl-His-Leu
5
hippuryl-L-His-L-Leu
-
-
0.0157 - 0.1592
LEQIYHL
1
Leu5-enkephalin
-
-
0.0045
Mca-RPPGFSAFK(Dnp)-OH
-
pH 7.4, 37°C
1
Met5-enkephalin
-
-
0.125
N-benzyloxycarbonyl-L-Phe-L-His-L-Leu
-
-
0.014
neurotensin
-
-
0.0753 - 0.0905
NKLKPSQ
0.0622 - 0.5237
NKLKPSQWI
0.0069 - 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
0.108 - 0.3117
SLKPSNWLTPSE
0.025
Substance P
-
-
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
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
320 - 368
2-furanacryloyl-Phe-Gly-Gly
23
Abz-LFK(Dnp)-OH
-
pH 7.4, 37°C
3
Abz-SDK(Dnp)P-OH
-
pH 7.4, 37°C
4.2
amyloid beta-protein 1-42
-
-
-
0.58 - 8.33
angiotensin
8.7 - 60
angiotensin I
283
benzoyl-Gly-Gly-Gly
-
-
76.7
benzoyl-Gly-His-Leu
-
-
383
benzoyl-Gly-Phe-Arg
-
-
2.1 - 128
benzyloxycarbonyl-Phe-His-Leu
8.33
bradykinin
-
-
179
furanacryloyl-L-Phe-Gly-Gly
-
-
11.8 - 545
hippuryl-His-Leu
11.7
Leu5-enkephalin
-
-
20.33
Mca-RPPGFSAFK(Dnp)-OH
-
pH 7.4, 37°C
58.3
Met5-enkephalin
-
-
0.567
neurotensin
-
-
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
3.75 - 21.3
Substance P
57 - 460
[Arg10]angiotensin I
6.5 - 1700
[Phe9,Arg10]angiotensin I
110 - 1500
[Phe9]angiotensin I
additional information
additional information
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0000022
(2S)-2-[[(2S)-2-mercapto-3-methylpentanoyl]amino]-3-(1-naphthyl)propanoic acid
pH 7.5, angiotensin-converting enzyme 2
0.0000018 - 0.0000024
(2S)-2-[[(2S)-2-mercapto-3-methylpentanoyl]amino]-3-(2-naphthyl)propanoic acid
0.0000015
(2S)-2-[[(2S)-2-mercapto-3-methylpentanoyl]amino]-3-phenylpropanoic acid
pH 7.5, angiotensin-converting enzyme 2
0.000014
(2S)-2-[[(2S)-2-mercapto-3-methylpentanoyl]amino]propanoic acid
pH 7.5, angiotensin-converting enzyme 2
0.0000013
(2S)-3-(4-hydroxyphenyl)-2-[[(2S)-2-mercapto-3-methylpentanoyl]amino]propanoic acid
pH 7.5, angiotensin-converting enzyme 2
0.0000015 - 0.000037
(2S)-3-biphenyl-2-yl-2-[[(2S)-3-methyl-2-sulfanylpentanoyl]amino]propanoic acid
0.0000015 - 0.0000022
(2S)-3-biphenyl-3-yl-2-[[(2S)-3-methyl-2-sulfanylpentanoyl]amino]propanoic acid
0.0023
(2S)-3-biphenyl-4-yl-2-[(2-mercapto-2-methylpropanoyl)amino]propanoic acid
pH 7.5, angiotensin-converting enzyme 2
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
0.0000069
(2S)-3-biphenyl-4-yl-2-[[(2S)-2-mercaptopropanoyl]amino]propanoic acid
pH 7.5, angiotensin-converting enzyme 2
0.0000015 - 0.000086
(2S)-3-biphenyl-4-yl-2-[[(2S)-3-methyl-2-sulfanylpentanoyl]amino]propanoic acid
0.000006 - 0.000065
2-(benzyloxy)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-phenylalanine
0.0000024 - 0.000084
3-(benzyloxy)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-phenylalanine
0.0000009 - 0.0000016
N-[(2S)-3-methyl-2-sulfanylpentanoyl]-2-phenoxy-L-phenylalanine
0.0000024 - 0.0000058
N-[(2S)-3-methyl-2-sulfanylpentanoyl]-3-phenoxy-L-phenylalanine
0.0000018 - 0.0000022
N-[(2S)-3-methyl-2-sulfanylpentanoyl]-O-phenyl-L-tyrosine
0.000035 - 0.00086
N-[(2S)-3-methyl-2-sulfanylpentanoyl]-O-[4-(trifluoromethyl)benzyl]-L-tyrosine
0.000002 - 0.00042
O-(2,4-difluorobenzyl)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-tyrosine
0.0000085 - 0.00055
O-(3,4-difluorobenzyl)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-tyrosine
0.0000025 - 0.0000071
O-(4-fluorobenzyl)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-tyrosine
0.0000014 - 0.0000027
O-benzyl-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-tyrosine
0.000084
O-[3,5-bis(trifluoromethyl)benzyl]-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-tyrosine
pH 7.5, angiotensin-converting enzyme 2
0.00009 - 0.0014
[[(2S)-2-mercapto-3-methylpentanoyl]amino]acetic acid
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
0.00000041
(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
0.0000004
(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
0.0018
(2S)-2-[[(2S)-2-mercapto-3-methylpentanoyl]amino]-3-(1-naphthyl)propanoic acid
pH 7.5, angiotensin-converting enzyme
0.0000093 - 0.00031
(2S)-2-[[(2S)-2-mercapto-3-methylpentanoyl]amino]-3-(2-naphthyl)propanoic acid
0.00057
(2S)-2-[[(2S)-2-mercapto-3-methylpentanoyl]amino]-3-phenylpropanoic acid
pH 7.5, angiotensin-converting enzyme
0.00018
(2S)-2-[[(2S)-2-mercapto-3-methylpentanoyl]amino]propanoic acid
pH 7.5, angiotensin-converting enzyme
0.00041
(2S)-3-(4-hydroxyphenyl)-2-[[(2S)-2-mercapto-3-methylpentanoyl]amino]propanoic acid
pH 7.5, angiotensin-converting enzyme
0.0002 - 0.02
(2S)-3-biphenyl-2-yl-2-[[(2S)-3-methyl-2-sulfanylpentanoyl]amino]propanoic acid
0.00049 - 0.001
(2S)-3-biphenyl-3-yl-2-[[(2S)-3-methyl-2-sulfanylpentanoyl]amino]propanoic acid
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
0.0000086
(2S)-3-biphenyl-4-yl-2-[[(2S)-2-mercaptobutanoyl]amino]propanoic acid
pH 7.5, angiotensin-converting enzyme
0.000021
(2S)-3-biphenyl-4-yl-2-[[(2S)-2-mercaptopropanoyl]amino]propanoic acid
pH 7.5, angiotensin-converting enzyme
0.00003 - 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
0.0004 - 0.0008
(pE)KWAP
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
0.00077 - 0.013
2-(benzyloxy)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-phenylalanine
0.00075
3-(benzyloxy)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-phenylalanine
pH 7.5, angiotensin-converting enzyme
0.000002747
angiotensin I
-
-
0.004 - 0.076
angiotensin II
0.000001278
bradykinin
-
-
0.000009 - 0.000191
captopril
0.00000194
enalaprilat
-
-
0.0072
Ile-Glu-Pro
-
-
0.055
Ile-Glu-Trp
-
-
0.0835
Ile-Glu-Tyr
-
-
0.0027
Ile-Lys-Pro
-
-
0.0085
Ile-Lys-Trp
-
-
0.013
Ile-Lys-Tyr
-
-
0.0000001 - 0.0001315
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
0.0002 - 0.005
N-[(2S)-3-methyl-2-sulfanylpentanoyl]-2-phenoxy-L-phenylalanine
0.00062 - 0.0011
N-[(2S)-3-methyl-2-sulfanylpentanoyl]-3-phenoxy-L-phenylalanine
0.00025 - 0.0007
N-[(2S)-3-methyl-2-sulfanylpentanoyl]-O-phenyl-L-tyrosine
0.000093 - 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
0.00084 - 0.00095
O-(2,4-difluorobenzyl)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-tyrosine
0.00021 - 0.0018
O-(3,4-difluorobenzyl)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-tyrosine
0.0027 - 0.004
O-(4-fluorobenzyl)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-tyrosine
0.0000032 - 0.00057
O-benzyl-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-tyrosine
0.025
O-[3,5-bis(trifluoromethyl)benzyl]-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-tyrosine
pH 7.5, angiotensin-converting enzyme
0.0015 - 0.049
PARPTSPP
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
0.00000035
quinaprilat
-
-
0.00000076
ramiprilat
-
-
0.0009 - 0.023
RPARPTSPP
0.000007 - 0.004
RXP407
0.005 - 0.019
Ser-Pro-Pro
0.0024 - 0.2
SSYVHLRPARPTSPP
0.00000057
trandolaprilat
-
-
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
0.00025 - 0.00052
[[(2S)-2-mercapto-3-methylpentanoyl]amino]acetic acid
additional information
additional information
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
-
-
0.01
Ala-Leu-Pro-His-Ala
Homo sapiens
-
pH 8.2, 37°C
0.0151
Ala-Phe
Homo sapiens
-
pH and temperature not specified in the publication
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
0.0142 - 0.1
Ala-Tyr
0.0666
Ala-Val-Val
Homo sapiens
-
-
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
0.0123
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
0.00001 - 0.041
captopril
0.9455
DQVFPMNPPK
Homo sapiens
-
-
0.0225
Gly-Asp-Ala-Pro
Homo sapiens
-
-
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
-
-
0.00625
Gly-Pro-Pro
Homo sapiens
-
pH and temperature not specified in the publication
0.0721
Gly-Tyr
Homo sapiens
-
pH and temperature not specified in the publication
0.0718
Gly-Val-His-His-Ala
Homo sapiens
-
-
0.0022
His-His-Leu
Homo sapiens
-
pH and temperature not specified in the publication
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
-
-
0.0448
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
0.0047
Ile-Trp
Homo sapiens
-
pH 8.2, 37°C
0.0058
Ile-Trp-His-His-Thr
Homo sapiens
-
pH 8.2, 37°C
0.0021 - 0.0034
Ile-Tyr
0.042
Ile-Tyr-Leu-Leu
Homo sapiens
-
pH and temperature not specified in the publication
0.00048
Ile-Val-Tyr
0.549
ITTNPY
Homo sapiens
-
-
0.0466
KAPVA
Homo sapiens
-
-
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
0.126
Leu-Phe
Homo sapiens
-
pH and temperature not specified in the publication
0.0064
Leu-Tyr
Homo sapiens
-
pH and temperature not specified in the publication
0.00000025 - 0.0000015
lisinopril
0.0024
LKPNM
Homo sapiens
-
-
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
0.034
MLGQTPT
Homo sapiens
-
-
0.0825
Phe-Gly-Gly
Homo sapiens
-
-
0.037
Phe-Phe-Leu
Homo sapiens
-
pH and temperature not specified in the publication
0.00374 - 0.025
Phe-Tyr
0.0069
Phe-Val-Asn-Pro-Gln-Ala-Gly-Ser
Homo sapiens
-
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
0.016
Pro-Ser-Tyr
Homo sapiens
-
pH and temperature not specified in the publication
0.2564
PTPVP
Homo sapiens
-
-
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
0.0663
Ser-Tyr
Homo sapiens
-
pH and temperature not specified in the publication
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
0.0178 - 0.018
Thr-Phe
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
0.0299 - 0.065
Trp-Leu
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
0.0105
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
0.097
Val-Ile-Glu-Lys-Tyr-Pro
Homo sapiens
-
pH and temperature not specified in the publication
0.00169
Val-Leu-Ile-Val-Pro
Homo sapiens
-
pH and temperature not specified in the publication
0.013
Val-Lys
Homo sapiens
-
pH and temperature not specified in the publication
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
0.0824
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
0.0014
Val-Trp
Homo sapiens
-
pH 8.2, 37°C
0.0071 - 0.021
Val-Tyr
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
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
104
-
lung
2.824
-
-
30.7
-
lung
40.6
-
-
43.8
-
-
49.09
pH 8.3, 37°C
88
-
kidney
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
hydrolysis of o-aminobenzoyl-FRK-(dinitrophenyl)-P-OH
7.1
-
without Cl-
7.3 - 8
-
hydrolysis of hippuryl-His-Leu, borate/sodium carbonate buffer
7.4
-
assay at
7.5
assay at
7.7 - 8
-
-
7.8
-
hydrolysis of benzoyl-Gly-His-Leu
8.2
-
assay at
8.2 - 8.4
-
hydrolysis of hippuryl-His-Leu
8.5
-
recombinant and wild-type enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 9
-
about 40% of maximal activity at pH 7.0 and at pH 9.0
7.5 - 9
-
pH 7.5: about 40% of maximal activity, pH 9.0: about 75% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.1
lung enzyme
5.2
kidney enzyme
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
at 11-13 weeks of gestation ACE-positive cells are observed in the primitive epidermis, as the fetuses develops ACE-positive cells appear in all the epidermal layers, and from 21 weeks of gestation ACE expression is largely restricted to the basal layer of the fetal epidermis, while ACE-positive cells are found only in the adult skin basal layer which harbours epidermal stem cells
Manually annotated by BRENDA team
-
stably transfected with full-length ACE2
Manually annotated by BRENDA team
-
endogenously expressing ACE2
Manually annotated by BRENDA team
classical, CD14++CD16- cells
Manually annotated by BRENDA team
-
fetal skin
Manually annotated by BRENDA team
stably overexpressing human somatic ACE
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
ACE undergoes domain shedding and changes from membrane to soluble status
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ACE2_HUMAN
805
1
92463
Swiss-Prot
Mitochondrion (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
130000
-
x * 130000, enzyme from lung, SDS-PAGE with 7% acryl amide
140000
145000
-
1 * 145000, enzyme in reduced and unreduced samples, SDS-PAGE
150000
155000
160000
-
x * 160000, lung and kidney enzyme, SDS-PAGE with or without 1% 2-mercaptoethanol
165000
-
x * 165000, SDS-PAGE with 5% acryl amide
170000
180000
199000
-
equilibrium sedimentation
244000
gel filtration
280000
-
gel filtration
290000
330000
-
enzyme from semen, gel filtration
55000
-
x * 55000 + x * 65000, SDS-PAGE
65000
-
x * 55000 + x * 65000, SDS-PAGE
98000
-
enzyme form III, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
the N domain of ACE influences domain shedding and enzyme dimerization, overview. Epitope mapping using monoclonal antibodies directed to the N domain of ACE, overview
monomer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
proteolytic modification
-
the secreted form is derived from the membrane-bound form by a post-translational proteolytic cleavage of the C-terminal region
sialoglycoprotein
angiotensin-converting enzyme (ACE) is expressed as a type-1 membrane glycoprotein on the surface of endothelial and epithelial cells. Desialylation of ACE is performed by comercial neuraminidase from Vibrio cholerae at pH 6.0, 25°C. While desialylation of seminal fluid ACE does not result in the appearance of any neuraminic acid on the ion-exchange chromatogram, desialylation of lung ACE results in the appearance of 5 neuraminic acid residues per molecule of the enzyme. N-glycosylation sites on the N and C domains of human ACE is analyzed by mass spectrometry, detailed overview. Effect of inactivated human plasma on mAbs binding to two types of ACE differed significantly, with seminal fluid ACE being more sensitive to the presence of plasma. Effect of inactivated seminal fluid on mAbs binding to two types of ACE also showed more prominent effect for seminal fluid ACE, strengthening the suggestion that different conformations of these ACEs can participate in different regulation of the functions of ACEs on endothelial and epithelial cells
side-chain modification
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
angiotensin-converting enzyme-lisinopril complex, 2.0 A resolution, vapour diffusion method. The structure provides an opportunity to design domain-selective ACE inhibitors that may exhibit new pharmacological profiles
crystal structure of human C-domain sACE in complex with two natural peptides, angiotensin II, and with a snake venom inhibitor-bradykinin potentiating peptide (BPPb, a human C-domain specific peptide inhibitor) is shown. The structure of the complex with BPPb reveals molecular interactions in a zinc independent manner. The structure of the C-domain sACE-angiotensin II complex reveals the role of the penultimate Pro residue of angiotensin II in conferring resistance to hydrolysis
crystal structure of the N domain of human somatic angiotensin I-converting enzyme both in the presence and absence of the antihypertensive drug lisinopril
crystal structures of the two catalytic domains of human ACE (N- and C-) in complex with (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 and (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 are determined to a resolution of 1.91 and 1.85 A, respectively
hanging drop method, crystal structure at a resolution of 2.25 A of testis enzyme with the highly C-domain-specific phosphinic inhibitor, RXPA380
hanging drop vapour diffusion method, in 10 mM sodium acetate (pH 4.7), 15% PEG 4000, and 0.01 mM ZnSO4, at 16°C
purified recombinant mutant tACE-G13 in complex with inhibitor lisW-S, microseeding, 1.45 mg/ml tACE-G13 with 0.250 mM lisW-S over precipitant solution comprising 15% w/v PEG 4000, 0.010 mM ZnSO4, and 10 mM sodium acetate, pH 4.7, 2 weeks, X-ray diffraction structure determination and analysis at 2.3 A resolution, modelling
structures of full-length, glycosylated sACE in monomeric and dimeric forms. The N- and C-terminal domains of monomeric sACE are resolved at 3.7 and 4.1A, respectively, the interacting N-terminal domains responsible for dimer formation at 3.8 A. The sACE monomer domains interact and are in an open conformation. The open N-domain active site is primed for substrate binding to the zinc site and the catalytic anchor residues Q259, K489, and Y498. sACE homodimerization occurs via the N-domain and increases flexibility at the allosteric site, formed by three C-terminal loops
vapour-diffusion hanging-drop method, wild-type and underglycosylated mutant enzymes. The truncated soluble enzyme DELTA1-36, expressed in the presence of the glucosidase-I inhibitor N-butyldeoxynojirimycin, retains the activity of the native enzyme and yields crystals belongining to the orthorhombic P2(1)2(1)2(1) space group. Cell dimensions: a = 56.47 A, b = 84.9 A, c = 144.99 A, alpha = 90°, beta = 90° and gamma = 90°
-
X-ray crystal structure of tACE and its complex with the inhibitor lisinopril. The structure of tACE is mainly helical with a central cavity or channel that extends for about 30 A into the molecule
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D377Q
site-directed mutagenesis, altered inhibition kinetics with inhibitor lisW-S compared to the wild-type enzyme
D453E
E162D
site-directed mutagenesis, altered inhibition kinetics with inhibitor lisW-S compared to the wild-type enzyme
E376D
site-directed mutagenesis, altered inhibition kinetics with inhibitor lisW-S compared to the wild-type enzyme
E403R
the mutation does not contribute individually to C domain-selective inhibitor binding
F391Y
K1087A
-
no activity with angiotensin I, kcat/KM for [Phe9]angiotensin I is 654fold lower than wild-type value, kcat/KM for [Arg10]angiotensin I is 193fold lower than wild-type value, kcat/KM for [Phe9,Arg10]angiotensin I is 462fold lower than wild-type value
L19E
the mutation alters the binding of monoclonal antibodies to the N domain of ACE and shedding of ACE domains
Q18H
the mutation alters the binding of monoclonal antibodies to the N domain of ACE and shedding of ACE domains
Q22A
the mutation alters the binding of monoclonal antibodies to the N domain of ACE and shedding of ACE domains
R1098Q
-
kcat/KM for angiotensin I is 7fold lower than wild-type value, kcat/KM for [Phe9]angiotensin I is 2.2fold higher than wild-type value, kcat/KM for [Arg10]angiotensin I is 23fold lower than wild-type value, kcat/KM for [Phe9,Arg10]angiotensin I is 1.4fold lower than wild-type value
S1270A
-
nonphosphorylatable signaling-dead ACE mutant
S516N
the S516N substitution results in a inhibitor binding affinity comparable to that of the wild type C domain
T282S
V379/V380T
the mutation displays small decrease in affinity for inhibitor (5S)-5-[(N-benzoyl)amino]-4-oxo-6-phenylhexanoyl-L-phenylalanine
V379S
V380T
V518T
Y1096F
-
kcat/KM for angiotensin I is 12fold lower than wild-type value, kcat/KM for [Phe9]angiotensin I is 8.9fold lower than wild-type value, kcat/KM for [Arg10]angiotensin I is 8.5fold lower than wild-type value, kcat/KM for [Phe9,Arg10]angiotensin I is 7fold lower than wild-type value
Y1096F/K1087A
-
no activity with angiotensin I, [Phe9]angiotensin I, [Arg10]angiotensin I, and [Phe9,Arg10]angiotensin I
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
-
rapid inactivation
81250
7 - 10
-
highest stability
81250
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
-
15 min, crude seminal plasma, stable
45
-
5-30 min, stable
55
-
10 min, 80% loss of activity
60
-
15 min, crude seminal plasma, stable
70
-
15 min, complete inactivation
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
lyophilized enzyme can be reconstituted but appears subsequently to be less stable
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 1 mg/ml enzyme in phosphate buffer, stable for 2 months
-
-20°C, 1 mg/ml enzyme, stable for several months
-
-20°C, pH 7.0, 0.01 M KH2PO4/K2HPO4, 0.5 M NaCl, stable for several months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
captopril affinity chromatography
-
large scale
-
N-catalytic domain (residues Ala361 to Gly468) of human somatic angiotensin-I converting enzyme expressed in Escherichia coli
Sepharose-lisinopril affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
ACE insertion/deletion genotyping
-
C-catalytic and N-catalytic domain is expressed in CHO cells
expressed in 3T3-L1 cells
-
expressed in Chinese hamster ovary cells
expression in Chinese hamster ovary cells
-
expression in CHO-K1 cells
expression of soluble wild-type and mutant enzymes in CHO and HEK-293 cells
expression of the N-catalytic domain (residues Ala361 to Gly468) of human somatic angiotensin-I converting enzyme in Escherichia coli. The overexpressed protein is exclusively localized to insoluble inclusion bodies
expression of wild-type enzyme and underglycosylated mutant enzymes in CHO cells
-
genotyping of ACE insertion and deletion polymorphisms in the Saudi population from Qassim region, genotyping, allele frequencies, overview
-
recombinantly expressed
-
regions of the testis ACE sequence are replaced with the corresponding N-domain sequence. The resultant chimeras C1-163Ndom-ACE, C417-579Ndom-ACE, and C583-623Ndom-ACE are processed to the cell surface of transfected Chinese hamster ovary cells, and are cleaved at the identical site as that of tACE
somatic enzyme form
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Soffer, R.L.
Angiotensin-converting enzyme and the regulation of vasoactive peptides
Annu. Rev. Biochem.
45
73-94
1976
Cavia porcellus, Oryctolagus cuniculus, Homo sapiens, Sus scrofa
Manually annotated by BRENDA team
Patchett, A.A.; Cordes, E.H.
The design and properties of N-carboxyalkyldipeptide inhibitors of angiotensin-converting enzyme
Adv. Enzymol. Relat. Areas Mol. Biol.
57
1-84
1985
Bos taurus, Canis lupus familiaris, Oryctolagus cuniculus, Homo sapiens, Mammalia, Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Ondetti, M.A.; Cushman, D.W.
Enzymes of the renin-angiotensin system and their inhibitors
Annu. Rev. Biochem.
51
283-308
1982
Bos taurus, Canis lupus familiaris, Cavia porcellus, Oryctolagus cuniculus, Equus caballus, Homo sapiens, Papio anubis, Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Wei, L.; Alhenc-Gelas, F.; Soubrier, F.; Michaud, A.; Corvol, P.; Clauser, E.
Expression and characterization of recombinant human angiotensin I-converting enzyme. Evidence for a C-terminal transmembrane anchor and for a proteolytic processing of the secreted recombinant and plasma enzymes
J. Biol. Chem.
266
5540-5546
1991
Homo sapiens
Manually annotated by BRENDA team
Stewart, T.A.; Weare, J.A.; Erds, E.G.
Human peptidyl dipeptidase (converting enzyme, kininase II)
Methods Enzymol.
80
450-460
1981
Homo sapiens
Manually annotated by BRENDA team
Cushman, D.W.; Cheung, H.S.; Sabo, E.F.; Rubin, B.; Ondetti, M.A.
Development of specific inhibitors of angiotensin I converting enzyme (kininase II)
Fed. Proc.
38
2778-2782
1979
Homo sapiens, Sus scrofa
Manually annotated by BRENDA team
Deddish, P.A.; Wang, L.X.; Jackman, H.L.; Michel, B.; Wang, J.; Skidgel, R.A.; Erds, E.G.
Single-domain angiotensin I converting enzyme (kininase II): characterization and properties
J. Pharmacol. Exp. Ther.
279
1582-1589
1996
Oryctolagus cuniculus, Homo sapiens
Manually annotated by BRENDA team
Ryan, J.W.
Angiotensin-converting enzyme, dipeptidyl carboxypeptidase I, and its inhibitors
Methods Enzymol.
163
194-210
1988
Homo sapiens
Manually annotated by BRENDA team
Takeuchi, K.; Shimizu, T.; Ohishi, N.; Seyama, Y.; Takaku, F.; Yotsumoto, H.
Purification of human lung angiotensin-converting enzyme by high-performance liquid chromatography: properties and N-terminal amino acid sequence
J. Biochem.
106
442-445
1989
Homo sapiens
Manually annotated by BRENDA team
Miska, W.; Croseck, H.; Schill, W.B.
Kininase II from human seminal plasma. Isolation and properties
Biol. Chem. Hoppe-Seyler
369
493-496
1988
Homo sapiens
Manually annotated by BRENDA team
Ehlers, M.R.W.; Kirsch, R.E.
Catalysis of angiotensin I hydrolysis by human angiotensin-converting enzyme: effect of chloride and pH
Biochemistry
27
5538-5544
1988
Homo sapiens
Manually annotated by BRENDA team
Sakharov, I.Y.; Danilov, S.M.; Sukhova, N.V.
Isolation of human liver angiotensin-converting enzyme by chromatofocusing
Anal. Biochem.
166
14-17
1987
Homo sapiens
Manually annotated by BRENDA team
Sakharov, I.Y.; Danilov, S.M.; Dukhanina, E.A.
Affinity chromatography and some properties of the angiotensin-converting enzyme from human heart
Biochim. Biophys. Acta
923
143-149
1987
Homo sapiens
Manually annotated by BRENDA team
Ehlers, M.R.W.; Maeder, D.L.; Kirsch, R.E.
Rapid affinity chromatographic purification of human lung and kidney angiotensin-converting enzyme with the novel N-carboxyalkyl dipeptide inhibitor N-[1(S)-carboxy-5-aminopentyl]glycylglycine
Biochim. Biophys. Acta
883
361-372
1986
Homo sapiens
Manually annotated by BRENDA team
Erds, E.G.; Skidgel, R.A.
Structure and functions of human angiotensin I converting enzyme (kininase II)
Biochem. Soc. Trans.
13
42-44
1985
Homo sapiens
Manually annotated by BRENDA team
Lanzillo, J.J.; Stevens, J.; Dasarathy, Y.; Yotsumoto, H.; Fanburg, B.L.
Angiotensin-converting enzyme from human tissues. Physicochemical, catalytic, and immunological properties
J. Biol. Chem.
260
14938-14944
1985
Homo sapiens
Manually annotated by BRENDA team
Taira, H.; Mizutani, S.; Kurauchi, O.; Narita, O.; Tomoda, Y.
Rapid purification of human placental angiotensin I converting enzyme by captopril affinity chromatography
J. Chromatogr.
339
399-403
1985
Homo sapiens
Manually annotated by BRENDA team
Weare, J.A.; Gafford, J.T.; Lu, H.S.; Erds, E.G.
Purification of human kidney angiotensin I converting enzyme using reverse-immunoadsorption chromatography
Anal. Biochem.
123
310-319
1982
Homo sapiens
Manually annotated by BRENDA team
Corvol, P.; Williams, T.A.; Soubrier, F.
Peptidyl dipeptidase A: angiotensin I-converting enzyme
Methods Enzymol.
248
283-305
1995
Homo sapiens, Mammalia, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Takada, Y.; Hiwada, K.; Kokubu, T.
Isolation and characterization of angiotensin converting enzyme from human kidney
J. Biochem.
90
1309-1319
1981
Homo sapiens
Manually annotated by BRENDA team
Harris, R.B.; Ohlsson, J.T.; Wilson, I.B.
Purification of human serum angiotensin I-converting enzyme by affinity chromatography
Anal. Biochem.
111
227-234
1981
Homo sapiens
Manually annotated by BRENDA team
Nishimura, K.; Yoshida, N.; Hiwada, K.; Ueda, E.; Kokubu, T.
Properties of three different forms of angiotensin I-converting enzyme from human lung
Biochim. Biophys. Acta
522
229-237
1978
Homo sapiens
Manually annotated by BRENDA team
Lanzillo, J.J.; Fanburg, B.L.
Angiotensin I converting enzyme from human plasma
Biochemistry
16
5491-5495
1977
Homo sapiens
Manually annotated by BRENDA team
Nishimura, K.; Yoshida, N.; Hiwada, K.; Ueda, E.; Kokubu, T.
Purification of angiotensin I-converting enzyme from human lung
Biochim. Biophys. Acta
483
398-408
1977
Homo sapiens
Manually annotated by BRENDA team
Lanzillo, J.J.; Polsky-Cynkin, R.; Fanburg, B.L.
Large-scale purification of angiotensin I-converting enzyme from human plasma utilizing an immunoadsorbent affinity gel
Anal. Biochem.
103
400-407
1980
Homo sapiens, Papio anubis
Manually annotated by BRENDA team
Depierre, D.; Bargetzi, J.P.; Roth, M.
Dipeptidyl carboxypeptidase from human seminal plasma
Biochim. Biophys. Acta
523
469-476
1978
Homo sapiens
Manually annotated by BRENDA team
Bull, H.G.; Thornberry, N.A.; Cordes, E.H.
Purification of angiotensin-converting enzyme from rabbit lung and human plasma by affinity chromatography
J. Biol. Chem.
260
2963-2972
1985
Oryctolagus cuniculus, Homo sapiens
Manually annotated by BRENDA team
Wei, L.; Clauser, E.; Alhenc-Gelas, F.; Corvol, P.
The two homologous domains of human angiotensin I-converting enzyme interact differently with competitive inhibitors
J. Biol. Chem.
267
13398-13405
1992
Homo sapiens
Manually annotated by BRENDA team
Soubrier, F.; Alhenc-Gelas, F.; Hubert, C.; Allegrini, J.; John, M.; Tregear, G.; Corvol., P.
Two putative active centers in human angiotensin I-converting enzyme revealed by molecular cloning
Proc. Natl. Acad. Sci. USA
85
9386-9390
1988
Homo sapiens
Manually annotated by BRENDA team
Miska, W.; Croseck, H.; Schill, W.B.
Proteins of the kallikrein-kinin system in human semen. Isolation and properties of kininase II
Andrologia
22 Suppl 1
178-184
1990
Homo sapiens
Manually annotated by BRENDA team
Baudin, B.; Tahraoui, A.; Baumann, F.C.; Robic, D.; Drouet, L.; Legrand, Y.
Purification and analysis of lung and plasma angiotensin I-converting enzyme by high-performance liquid chromatography
Protein Expr. Purif.
2
412-419
1991
Homo sapiens, Sus scrofa
Manually annotated by BRENDA team
Jaspard, E.; Alhenc-Gelas, F.
Catalytic properties of the two active sites of angiotensin I-converting enzyme on the cell surface
Biochem. Biophys. Res. Commun.
211
528-534
1995
Homo sapiens
Manually annotated by BRENDA team
Mathey, A.; Reuter, G.
Microbial synthesis of metabolites with antihypertensive activity: aspects of fermentation derived inhibitors of angiotensin-converting enzyme (ACE)
J. Basic Microbiol.
29
623-639
1989
Homo sapiens
Manually annotated by BRENDA team
Gordon, K.; Redelinghuys, P.; Schwager, S.L.; Ehlers, M.R.; Papageorgiou, A.C.; Natesh, R.; Acharya, K.R.; Sturrock, E.D.
Deglycosylation, processing and crystallization of human testis angiotensin-converting enzyme
Biochem. J.
371
437-442
2003
Homo sapiens
Manually annotated by BRENDA team
Araujo, M.C.; Melo, R.L.; Cesari, M.H.; Juliano, M.A.; Juliano, L.; Carmona, A.K.
Peptidase specificity characterization of C- and N-terminal catalytic sites of angiotensin I-converting enzyme
Biochemistry
39
8519-8525
2000
Homo sapiens
Manually annotated by BRENDA team
Cotton, J.; Hayashi, M.A.F.; Cuniasse, P.; Vazeux, G.; Ianzer, D.; De Camargo, A.C.M.; Dive, V.
Selective inhibition of the C-domain of angiotensin I converting enzyme by bradykinin potentiating peptides
Biochemistry
41
6065-6071
2002
Homo sapiens
Manually annotated by BRENDA team
Hens, K.; Vandingenen, A.; Macours, N.; Baggerman, G.; Karaoglanovic, A.C.; Schoofs, L.; De Loof, A.; Huybrechts, R.
Characterization of four substrates emphasizes kinetic similarity between insect and human C-domain angiotensin-converting enzyme
Eur. J. Biochem.
269
3522-3530
2002
Homo sapiens, Locusta migratoria
Manually annotated by BRENDA team
Hu, J.; Igarashi, A.; Kamata, M.; Nakagawa, H.
Angiotensin-converting enzyme degrades Alzheimer amyloid beta-peptide (Abeta); retards Abeta aggregation, deposition, fibril formation; and inhibits cytotoxicity
J. Biol. Chem.
276
47863-47868
2001
Homo sapiens
Manually annotated by BRENDA team
Natesh, R.; Schwager, S.L.; Sturrock, E.D.; Acharya, K.R.
Crystal structure of the human angiotensin-converting enzyme-lisinopril complex
Nature
421
551-554
2003
Homo sapiens (P12821), Homo sapiens
Manually annotated by BRENDA team
Nikolaeva, M.A.; Balyasnikova, I.V.; Alexinskaya, M.A.; Metzger, R.; Franke, F.E.; Albrecht, R.F.2nd.; Kulakov, V.I.; Sukhikh, G.T.; Danilov, S.M.
Testicular isoform of angiotensin I-converting enzyme (ACE, CD143) on the surface of human spermatozoa: revelation and quantification using monoclonal antibodies
Am. J. Reprod. Immunol.
55
54-68
2006
Homo sapiens
Manually annotated by BRENDA team
Asci, R.; Sarikaya, S.; Buyukalpelli, R.; Yilmaz, A.; Bedir, A.
Somatic angiotensin converting enzyme in varicocele
Arch. Androl.
52
329-334
2006
Homo sapiens
Manually annotated by BRENDA team
Farias, S.L.; Sabatini, R.A.; Sampaio, T.C.; Hirata, I.Y.; Cezari, M.H.; Juliano, M.A.; Sturrock, E.D.; Carmona, A.K.; Juliano, L.
Angiotensin I-converting enzyme inhibitor peptides derived from the endostatin-containing NC1 fragment of human collagen XVIII
Biol. Chem.
387
611-616
2006
Homo sapiens
Manually annotated by BRENDA team
Levitt, D.G.; Schoemaker, R.C.
Human physiologically based pharmacokinetic model for ACE inhibitors: ramipril and ramiprilat
BMC Clin. Pharmacol.
6
1
2006
Homo sapiens
Manually annotated by BRENDA team
Brunner, D.B.; Desponds, G.; Biollaz, J.; Keller, I.; Ferber, F.; Gavras, H.; Brunner, H.R.; Schelling, J.L.
Effect of a new angiotensin converting enzyme inhibitor MK 421 and its lysine analogue on the components of the renin system in healthy subjects. (discussion S785-777) 1981
Br. J. Clin. Pharmacol.
58
S778-784
2004
Homo sapiens
Manually annotated by BRENDA team
Hayashi, K.; Miyagawa, K.; Sato, K.; Ueda, R.; Dohi, Y.
Temocapril, an angiotensin converting enzyme inhibitor, ameliorates age-related increase in carotid arterial stiffness in normotensive subjects
Cardiology
106
190-194
2006
Homo sapiens
Manually annotated by BRENDA team
Sturrock, E.D.; Natesh, R.; van Rooyen, J.M.; Acharya, K.R.
Structure of angiotensin I-converting enzyme
Cell. Mol. Life Sci.
61
2677-2686
2004
Homo sapiens
Manually annotated by BRENDA team
Fleming, I.
Signaling by the angiotensin-converting enzyme
Circ. Res.
98
887-896
2006
Homo sapiens
Manually annotated by BRENDA team
Chen, Z.; Tan, F.; Erdoes, E.G.; Deddish, P.A.
Hydrolysis of angiotensin peptides by human angiotensin I-converting enzyme and the resensitization of B2 kinin receptors
Hypertension
46
1368-1373
2005
Homo sapiens
Manually annotated by BRENDA team
Naqvi, N.; Liu, K.; Graham, R.M.; Husain, A.
Molecular basis of exopeptidase activity in the C-terminal domain of human angiotensin I-converting enzyme: insights into the origins of its exopeptidase activity
J. Biol. Chem.
280
6669-6675
2005
Homo sapiens
Manually annotated by BRENDA team
Nielsen, E.W.; Gramstad, S.
Angioedema from angiotensin-converting enzyme (ACE) inhibitor treated with complement 1 (C1) inhibitor concentrate
Acta Anaesthesiol. Scand.
50
120-122
2006
Homo sapiens
Manually annotated by BRENDA team
Rodrigues, A.M.; Hueb, M.; Nery, A.F.; Fontes, C.J.
Possible cardioprotective effect of angiotensin-converting enzyme inhibitors during treatment of American tegumentary leishmaniasis with meglumine antimoniate
Acta Trop.
102
113-118
2007
Homo sapiens
Manually annotated by BRENDA team
McMurray, J.J.; Young, J.B.; Dunlap, M.E.; Granger, C.B.; Hainer, J.; Michelson, E.L.; Earle, S.; Olofsson, B.; Ostergren, J.; Yusuf, S.; Swedberg, K.; Pfeffer, M.A.; Pfeffer, M.A.
Relationship of dose of background angiotensin-converting enzyme inhibitor to the benefits of candesartan in the Candesartan in heart failure: assessment of reduction in mortality and morbidity (CHARM)-added trial
Am. Heart J.
151
985-991
2006
Homo sapiens
Manually annotated by BRENDA team
Bowen, M.E.; Ray, W.A.; Arbogast, P.G.; Ding, H.; Cooper, W.O.
Increasing exposure to angiotensin-converting enzyme inhibitors in pregnancy
Am. J. Obstet. Gynecol.
198
291.e1-291.e5
2008
Homo sapiens
Manually annotated by BRENDA team
Lam, L.H.; Shimamura, T.; Sakaguchi, K.; Noguchi, K.; Ishiyama, M.; Fujimura, Y.; Ukeda, H.
Assay of angiotensin I-converting enzyme-inhibiting activity based on the detection of 3-hydroxybutyric acid
Anal. Biochem.
364
104-111
2007
Homo sapiens
Manually annotated by BRENDA team
Bubbar, C.D.; Blackburn, D.F.; Wilson, M.P.; Wilson, T.W.
Angiotensin-converting enzyme inhibitors and angiotensin receptor blockers in hypertension due to primary aldosteronism: a case for exclusion
Ann. Pharmacother.
41
129-132
2007
Homo sapiens
Manually annotated by BRENDA team
Molteni, A.; Heffelfinger, S.; Moulder, J.E.; Uhal, B.; Castellani, W.J.
Potential deployment of angiotensin I converting enzyme inhibitors and of angiotensin II type 1 and type 2 receptor blockers in cancer chemotherapy
Anticancer Agents Med. Chem.
6
451-460
2006
Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Corradi, H.R.; Chitapi, I.; Sewell, B.T.; Georgiadis, D.; Dive, V.; Sturrock, E.D.; Acharya, K.R.
The structure of testis angiotensin-converting enzyme in complex with the C domain-specific inhibitor RXPA380
Biochemistry
46
5473-5478
2007
Homo sapiens (P12821)
Manually annotated by BRENDA team
Papakyriakou, A.; Spyroulias, G.A.; Sturrock, E.D.; Manessi-Zoupa, E.; Cordopatis, P.
Simulated interactions between angiotensin-converting enzyme and substrate gonadotropin-releasing hormone: novel insights into domain selectivity
Biochemistry
46
8753-8765
2007
Homo sapiens (P12821), Homo sapiens
Manually annotated by BRENDA team
Woodman, Z.L.; Schwager, S.L.; Redelinghuys, P.; Chubb, A.J.; van der Merwe, E.L.; Ehlers, M.R.; Sturrock, E.D.
Homologous substitution of ACE C-domain regions with N-domain sequences: effect on processing, shedding, and catalytic properties
Biol. Chem.
387
1043-1051
2006
Homo sapiens (P12821)
Manually annotated by BRENDA team
Redelinghuys, P.; Nchinda, A.T.; Chibale, K.; Sturrock, E.D.
Novel ketomethylene inhibitors of angiotensin I-converting enzyme (ACE): inhibition and molecular modelling
Biol. Chem.
387
461-466
2006
Homo sapiens (P12821)
Manually annotated by BRENDA team
Deaton, D.N.; Graham, K.P.; Gross, J.W.; Miller, A.B.
Thiol-based angiotensin-converting enzyme 2 inhibitors: P1 modifications for the exploration of the S1 subsite
Bioorg. Med. Chem. Lett.
18
1681-1687
2008
Homo sapiens, Homo sapiens (Q9BYF1)
Manually annotated by BRENDA team
Deaton, D.N.; Gao, E.N.; Graham, K.P.; Gross, J.W.; Miller, A.B.; Strelow, J.M.
Thiol-based angiotensin-converting enzyme 2 inhibitors: P1 modifications for the exploration of the S1 subsite
Bioorg. Med. Chem. Lett.
18
732-737
2008
Homo sapiens, Homo sapiens (Q9BYF1)
Manually annotated by BRENDA team
Garcia-Pavia, P.; Tomas, J.M.; Alonso-Pulpon, L.
Late-onset angioedema due to an angiotensin-converting enzyme inhibitor
Can. J. Cardiol.
23
315-316
2007
Homo sapiens
Manually annotated by BRENDA team
van der Knaap, R.; Siemes, C.; Coebergh, J.W.; van Duijn, C.M.; Hofman, A.; Stricker, B.H.
Renin-angiotensin system inhibitors, angiotensin I-converting enzyme gene insertion/deletion polymorphism, and cancer: the Rotterdam study
Cancer
112
748-757
2008
Homo sapiens
Manually annotated by BRENDA team
Ceconi, C.; Francolini, G.; Bastianon, D.; Gitti, G.L.; Comini, L.; Ferrari, R.
Differences in the effect of angiotensin-converting enzyme inhibitors on the rate of endothelial cell apoptosis: in vitro and in vivo studies
Cardiovasc. Drugs Ther.
21
423-429
2007
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Oyama, N.; Urasawa, K.; Kaneta, S.; Sakai, H.; Saito, T.; Takagi, C.; Yoshida, I.; Kitabatake, A.; Tsutsui, H.
Angiotensin converting enzyme inhibitors attenuated the expression of G-protein coupled receptor kinases in heart failure patients
Circ. J.
70
362-363
2006
Homo sapiens
Manually annotated by BRENDA team
Murray, B.A.; FitzGerald, R.J.
Angiotensin converting enzyme inhibitory peptides derived from food proteins: biochemistry, bioactivity and production
Curr. Pharm. Des.
13
773-791
2007
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Saha, S.A.; Molnar, J.; Arora, R.R.
Tissue angiotensin-converting enzyme inhibitors for the prevention of cardiovascular disease in patients with diabetes mellitus without left ventricular systolic dysfunction or clinical evidence of heart failure: a pooled meta-analysis of randomized place
Diabetes Obes. Metab.
10
41-52
2008
Homo sapiens
Manually annotated by BRENDA team
Goossens, G.H.; Blaak, E.E.; Schiffers, P.M.; Saris, W.H.; Baak, M.A.
Effect of short-term ACE inhibitor treatment on peripheral insulin sensitivity in obese insulin-resistant subjects
Diabetologia
49
3009-3016
2006
Homo sapiens
Manually annotated by BRENDA team
Lucas, C.; Christie, G.A.; Waring, W.S.
Rapid onset of haemodynamic effects after angiotensin converting enzyme-inhibitor overdose: implications for initial patient triage
Emerg. Med. J.
23
854-857
2006
Homo sapiens
Manually annotated by BRENDA team
Gislason, G.H.; Rasmussen, J.N.; Abildstrom, S.Z.; Gadsboll, N.; Buch, P.; Friberg, J.; Rasmussen, S.; Kober, L.; Stender, S.; Madsen, M.; Torp-Pedersen, C.
Long-term compliance with beta-blockers, angiotensin-converting enzyme inhibitors, and statins after acute myocardial infarction
Eur. Heart J.
27
1153-1158
2006
Homo sapiens
Manually annotated by BRENDA team
Wagner, H.; Thaller, S.; Dahse, R.; Sust, M.
Biomechanical muscle properties and angiotensin-converting enzyme gene polymorphism: a model-based study
Eur. J. Appl. Physiol.
98
507-515
2006
Homo sapiens
Manually annotated by BRENDA team
Morawietz, H.; Rohrbach, S.; Rueckschloss, U.; Schellenberger, E.; Hakim, K.; Zerkowski, H.R.; Kojda, G.; Darmer, D.; Holtz, J.
Increased cardiac endothelial nitric oxide synthase expression in patients taking angiotensin-converting enzyme inhibitor therapy
Eur. J. Clin. Invest.
36
705-712
2006
Homo sapiens
Manually annotated by BRENDA team
Symvoulakis, E.K.; Kyrmizakis, D.E.; Drivas, E.I.; Bizakis, J.; Velegrakis, G.A.; Lionis, C.
Angiotensin-converting enzyme inhibitor (ACE-I) - and angiotensin receptor blocker (ARB)-related angioedema: a neglected issue in daily practice in Greece
Eur. J. Gen. Pract.
13
239-241
2007
Homo sapiens
Manually annotated by BRENDA team
Ceconi, C.; Francolini, G.; Olivares, A.; Comini, L.; Bachetti, T.; Ferrari, R.
Angiotensin-converting enzyme (ACE) inhibitors have different selectivity for bradykinin binding sites of human somatic ACE
Eur. J. Pharmacol.
577
1-6
2007
Homo sapiens
Manually annotated by BRENDA team
Lew, R.A.; Warner, F.J.; Hanchapola, I.; Yarski, M.A.; Manohar, J.; Burrell, L.M.; Smith, A.I.
Angiotensin-converting enzyme 2 catalytic activity in human plasma is masked by an endogenous inhibitor
Exp. Physiol.
93
685-693
2008
Homo sapiens
Manually annotated by BRENDA team
Andujar-Sanchez, M.; Jara-Perez, V.; Camara-Artigas, A.
Thermodynamic determination of the binding constants of angiotensin-converting enzyme inhibitors by a displacement method
FEBS Lett.
581
3449-3454
2007
Homo sapiens (P12821)
Manually annotated by BRENDA team
Lambert, D.W.; Clarke, N.E.; Hooper, N.M.; Turner, A.J.
Calmodulin interacts with angiotensin-converting enzyme-2 (ACE2) and inhibits shedding of its ectodomain
FEBS Lett.
582
385-390
2008
Homo sapiens
Manually annotated by BRENDA team
Hirota, T.; Ohki, K.; Kawagishi, R.; Kajimoto, Y.; Mizuno, S.; Nakamura, Y.; Kitakaze, M.
Casein hydrolysate containing the antihypertensive tripeptides Val-Pro-Pro and Ile-Pro-Pro improves vascular endothelial function independent of blood pressure-lowering effects: contribution of the inhibitory action of angiotensin-converting enzyme
Hypertens. Res.
30
489-496
2007
Homo sapiens
Manually annotated by BRENDA team
Furumatsu, Y.; Nagasawa, Y.; Tomida, K.; Mikami, S.; Kaneko, T.; Okada, N.; Tsubakihara, Y.; Imai, E.; Shoji, T.
Effect of renin-angiotensin-aldosterone system triple blockade on non-diabetic renal disease: addition of an aldosterone blocker, spironolactone, to combination treatment with an angiotensin-converting enzyme inhibitor and angiotensin II receptor blocker
Hypertens. Res.
31
59-67
2008
Homo sapiens
Manually annotated by BRENDA team
van Guilder, G.P.; Pretorius, M.; Luther, J.M.; Byrd, J.B.; Hill, K.; Gainer, J.V.; Brown, N.J.
Bradykinin type 2 receptor BE1 genotype influences bradykinin-dependent vasodilation during angiotensin-converting enzyme inhibition
Hypertension
51
454-459
2008
Homo sapiens
Manually annotated by BRENDA team
Khan, M.U.; Baig, M.A.; Javed, R.A.; Ali, S.; Qamar, U.R.; Vasavada, B.C.; Khan, I.A.
Benazepril induced isolated visceral angioedema: a rare and under diagnosed adverse effect of angiotensin converting enzyme inhibitors
Int. J. Cardiol.
118
e68-e69
2007
Homo sapiens
Manually annotated by BRENDA team
Kum, L.C.; Yip, G.W.; Lee, P.W.; Lam, Y.Y.; Wu, E.B.; Chan, A.K.; Fung, J.W.; Chan, J.Y.; Zhang, Q.; Kong, S.L.; Yu, C.M.
Comparison of angiotensin-converting enzyme inhibitor alone and in combination with irbesartan for the treatment of heart failure
Int. J. Cardiol.
125
16-21
2008
Homo sapiens
Manually annotated by BRENDA team
Coppo, R.; Peruzzi, L.; Amore, A.; Piccoli, A.; Cochat, P.; Stone, R.; Kirschstein, M.; Linne, T.
IgACE: a placebo-controlled, randomized trial of angiotensin-converting enzyme inhibitors in children and young people with IgA nephropathy and moderate proteinuria
J. Am. Soc. Nephrol.
18
1880-1888
2007
Homo sapiens
Manually annotated by BRENDA team
Lakhdar, R.; Al-Mallah, M.H.; Lanfear, D.E.
Safety and tolerability of angiotensin-converting enzyme inhibitor versus the combination of angiotensin-converting enzyme inhibitor and angiotensin receptor blocker in patients with left ventricular dysfunction: a systematic review and meta-analysis of randomized controled trials
J. Card. Fail.
14
181-188
2008
Homo sapiens
Manually annotated by BRENDA team
Kheterpal, S.; Khodaparast, O.; Shanks, A.; OReilly, M.; Tremper, K.K.
Chronic angiotensin-converting enzyme inhibitor or angiotensin receptor blocker therapy combined with diuretic therapy is associated with increased episodes of hypotension in noncardiac surgery
J. Cardiothorac. Vasc. Anesth.
22
180-186
2008
Homo sapiens
Manually annotated by BRENDA team
Egan, B.M.
Combination therapy with an angiotensin-converting enzyme inhibitor and a calcium channel blocker
J. Clin. Hypertens.
9
783-789
2007
Homo sapiens
Manually annotated by BRENDA team
White, W.B.
Angiotensin-converting enzyme inhibitors in the treatment of hypertension: an update
J. Clin. Hypertens.
9
876-882
2007
Homo sapiens
Manually annotated by BRENDA team
Dandona, P.; Dhindsa, S.; Ghanim, H.; Chaudhuri, A.
Angiotensin II and inflammation: the effect of angiotensin-converting enzyme inhibition and angiotensin II receptor blockade
J. Hum. Hypertens.
21
20-27
2007
Homo sapiens
Manually annotated by BRENDA team
Woodiwiss, A.J.; Nkeh, B.; Samani, N.J.; Badenhorst, D.; Maseko, M.; Tiago, A.D.; Candy, G.P.; Libhaber, E.; Sareli, P.; Brooksbank, R.; Norton, G.R.
Functional variants of the angiotensinogen gene determine antihypertensive responses to angiotensin-converting enzyme inhibitors in subjects of African origin
J. Hypertens.
24
1057-1064
2006
Homo sapiens
Manually annotated by BRENDA team
Doulton, T.W.; Saggar-Malik, A.K.; He, F.J.; Carney, C.; Markandu, N.D.; Sagnella, G.A.; MacGregor, G.A.
The effect of sodium and angiotensin-converting enzyme inhibition on the classic circulating renin-angiotensin system in autosomal-dominant polycystic kidney disease patients
J. Hypertens.
24
939-945
2006
Homo sapiens
Manually annotated by BRENDA team
Laggner, H.; Hermann, M.; Esterbauer, H.; Muellner, M.K.; Exner, M.; Gmeiner, B.M.; Kapiotis, S.
The novel gaseous vasorelaxant hydrogen sulfide inhibits angiotensin-converting enzyme activity of endothelial cells
J. Hypertens.
25
2100-2104
2007
Homo sapiens
Manually annotated by BRENDA team
van de Garde, E.M.; Souverein, P.C.; Hak, E.; Deneer, V.H.; van den Bosch, J.M.; Leufkens, H.G.
Angiotensin-converting enzyme inhibitor use and protection against pneumonia in patients with diabetes
J. Hypertens.
25
235-239
2007
Homo sapiens
Manually annotated by BRENDA team
Corradi, H.R.; Schwager, S.L.; Nchinda, A.T.; Sturrock, E.D.; Acharya, K.R.
Crystal structure of the N domain of human somatic angiotensin I-converting enzyme provides a structural basis for domain-specific inhibitor design
J. Mol. Biol.
357
964-974
2006
Homo sapiens (P12821), Homo sapiens
Manually annotated by BRENDA team
Zou, K.; Yamaguchi, H.; Akatsu, H.; Sakamoto, T.; Ko, M.; Mizoguchi, K.; Gong, J.S.; Yu, W.; Yamamoto, T.; Kosaka, K.; Yanagisawa, K.; Michikawa, M.
Angiotensin-converting enzyme converts amyloid beta-protein 1-42 (Abeta(1-42)) to Abeta(1-40), and its inhibition enhances brain Abeta deposition
J. Neurosci.
27
8628-8635
2007
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Vamvakas, S.S.; Leondiadis, L.; Pairas, G.; Manessi-Zoupa, E.; Spyroulias, G.A.; Cordopatis, P.
Expression, purification, and physicochemical characterization of the N-terminal active site of human angiotensin-I converting enzyme
J. Pept. Sci.
13
31-36
2007
Homo sapiens (P12821), Homo sapiens
Manually annotated by BRENDA team
Trasobares, E.; Corbaton, A.; Gonzalez-Estecha, M.; Lopez-Colon, J.L.; Prats, P.; Olivan, P.; Sanchez, J.A.; Arroyo, M.
Effects of angiotensin-converting enzyme inhibitors (ACE i) on zinc metabolism in patients with heart failure
J. Trace Elem. Med. Biol.
21 Suppl 1
53-55
2007
Homo sapiens
Manually annotated by BRENDA team
Kohlstedt, K.; Gershome, C.; Friedrich, M.; Mueller-Esterl, W.; Alhenc-Gelas, F.; Busse, R.; Fleming, I.
Angiotensin-converting enzyme (ACE) dimerization is the initial step in the ACE inhibitor-induced ACE signaling cascade in endothelial cells
Mol. Pharmacol.
69
1725-1732
2006
Homo sapiens (P12821)
Manually annotated by BRENDA team
Kraemer, H.H.; Schmidt, K.; Leis, S.; Schmelz, M.; Sommer, C.; Birklein, F.
Angiotensin converting enzyme has an inhibitory role in CGRP metabolism in human skin
Peptides
27
917-920
2006
Homo sapiens
Manually annotated by BRENDA team
Besancon, J.F.; Lagarce, L.; Diquet, B.; Laine-Cessac, P.
Study of the use of a spironolactone and angiotensin-converting enzyme inhibitor combination: a population-based analysis
Pharmacoepidemiol. Drug Saf.
17
172-179
2008
Homo sapiens
Manually annotated by BRENDA team
Woo, K.T.; Lau, Y.K.; Chan, C.M.; Wong, K.S.
Angiotensin-converting enzyme inhibitor versus angiotensin 2 receptor antagonist therapy and the influence of angiotensin-converting enzyme gene polymorphism in IgA nephritis
Ann. Acad. Med. Singap.
37
372-376
2008
Homo sapiens
Manually annotated by BRENDA team
Watermeyer, J.M.; Kroeger, W.L.; O'Neill, H.G.; Sewell, B.T.; Sturrock, E.D.
Probing the basis of domain-dependent inhibition using novel ketone inhibitors of angiotensin-converting enzyme
Biochemistry
47
5942-5950
2008
Homo sapiens (P12821), Homo sapiens
Manually annotated by BRENDA team
Liu, H.W.; Cheng, B.; Li, J.F.; Wu, H.J.; Li, K.Y.; Sun, T.Z.; Fu, X.B.
Characterization of angiotensin-converting enzyme expression during epidermis morphogenesis in humans: a potential marker for epidermal stem cells
Br. J. Dermatol.
160
250-258
2009
Homo sapiens
Manually annotated by BRENDA team
Brugts, J.J.; Danser, A.H.; de Maat, M.P.; den Uil, C.A.; Boersma, E.; Ferrari, R.; Simoons, M.L.
Pharmacogenetics of ACE inhibition in stable coronary artery disease: steps towards tailored drug therapy
Curr. Opin. Cardiol.
23
296-301
2008
Homo sapiens
Manually annotated by BRENDA team
Rafailidis, P.I.; Matthaiou, D.K.; Varbobitis, I.; Falagas, M.E.
Use of ACE inhibitors and risk of community-acquired pneumonia: a review
Eur. J. Clin. Pharmacol.
64
565-573
2008
Homo sapiens
Manually annotated by BRENDA team
Ramesar, S.; Baijnath, H.; Govender, T.; Mackraj, I.
Angiotensin I-converting enzyme inhibitor activity of nutritive plants in KwaZulu-Natal
J. Med. Food
11
331-336
2008
Homo sapiens
Manually annotated by BRENDA team
Kohlstedt, K.; Gershome, C.; Trouvain, C.; Hofmann, W.K.; Fichtlscherer, S.; Fleming, I.
Angiotensin-converting enzyme (ACE) inhibitors modulate cellular retinol-binding protein 1 and adiponectin expression in adipocytes via the ACE-dependent signaling cascade
Mol. Pharmacol.
75
685-692
2009
Homo sapiens
Manually annotated by BRENDA team
Zou, K.; Michikawa, M.
Angiotensin-converting enzyme as a potential target for treatment of Alzheimer's disease: inhibition or activation?
Rev. Neurosci.
19
203-212
2008
Homo sapiens
Manually annotated by BRENDA team
Pentzien, A.K.; Meisel, H.
Transepithelial transport and stability in blood serum of angiotensin-I-converting enzyme inhibitory dipeptides
Z. Naturforsch. C
63
451-459
2008
Oryctolagus cuniculus, Homo sapiens
Manually annotated by BRENDA team
Cesari, M.; Kritchevsky, S.B.; Atkinson, H.H.; Penninx, B.W.; Di Bari, M.; Tracy, R.P.; Pahor, M.
Angiotensin-converting enzyme inhibition and novel cardiovascular risk biomarkers: results from the trial of angiotensin converting enzyme inhibition and novel cardiovascular risk factors (TRAIN) study
Am. Heart J.
157
334e1-334e8
2009
Homo sapiens
Manually annotated by BRENDA team
Levy, P.D.; Nandyal, D.; Welch, R.D.; Sun, J.L.; Pieper, K.; Ghali, J.K.; Fonarow, G.C.; Gheorgiade, M.; OConnor, C.M.
Does aspirin use adversely influence intermediate-term postdischarge outcomes for hospitalized patients who are treated with angiotensin-converting enzyme inhibitors or angiotensin receptor blockers? Organized Program to Facilitate Life-Saving Treatment in Hospitalized Patients with Heart Failure (OPTIMIZE-HF)
Am. Heart J.
159
222-230.e2
2010
Homo sapiens
Manually annotated by BRENDA team
Milonas, C.; Jernberg, T.; Lindbaeck, J.; Agewall, S.; Wallentin, L.; Stenestrand, U.; Stenestrand, U.
Effect of angiotensin-converting enzyme inhibition on one-year mortality and frequency of repeat acute myocardial infarction in patients with acute myocardial infarction
Am. J. Cardiol.
105
1229-1234
2010
Homo sapiens
Manually annotated by BRENDA team
LaMarr, B.; Valdez, C.; Driscoll, K.; Ryan, M.
Influence of pharmacist intervention on prescribing of angiotensin-converting-enzyme inhibitors, angiotensin II-receptor blockers, and aspirin for diabetic patients
Am. J. Health Syst. Pharm.
67
290-294
2010
Homo sapiens
Manually annotated by BRENDA team
Bas, M.; Greve, J.; Stelter, K.; Bier, H.; Stark, T.; Hoffmann, T.K.; Kojda, G.
Therapeutic efficacy of icatibant in angioedema induced by angiotensin-converting enzyme inhibitors: a case series
Ann. Emerg. Med.
56
278-282
2010
Homo sapiens
Manually annotated by BRENDA team
Bertrand, M.E.; Fox, K.M.; Remme, W.J.; Ferrari, R.; Simoons, M.L.
Angiotensin-converting enzyme inhibition with perindopril in patients with prior myocardial infarction and/or revascularization: a subgroup analysis of the EUROPA trial
Arch. Cardiovasc. Dis.
102
89-96
2009
Homo sapiens
Manually annotated by BRENDA team
Watermeyer, J.M.; Kroeger, W.L.; ONeill, H.G.; Sewell, B.T.; Sturrock, E.D.
Characterization of domain-selective inhibitor binding in angiotensin-converting enzyme using a novel derivative of lisinopril
Biochem. J.
428
67-74
2010
Homo sapiens (P12821), Homo sapiens
Manually annotated by BRENDA team
Bas, M.; Hoffmann, T.K.; Tiemann, B.; Dao, V.T.; Bantis, C.; Balz, V.; Schultz-Coulon, H.J.; Stark, T.; Schuler, P.; Greve, J.; Ivens, K.; Bier, H.; Kojda, G.
Potential genetic risk factors in angiotensin-converting enzyme-inhibitor-induced angio-oedema
Br. J. Clin. Pharmacol.
69
179-186
2010
Homo sapiens
Manually annotated by BRENDA team
Blaes, A.H.; Gaillard, P.; Peterson, B.A.; Yee, D.; Virnig, B.
Angiotensin converting enzyme inhibitors may be protective against cardiac complications following anthracycline chemotherapy
Breast Cancer Res. Treat.
122
585-593
2010
Homo sapiens
Manually annotated by BRENDA team
Hoover, T.; Lippmann, M.; Grouzmann, E.; Marceau, F.; Herscu, P.
Angiotensin converting enzyme inhibitor induced angio-oedema: a review of the pathophysiology and risk factors
Clin. Exp. Allergy
40
50-61
2010
Homo sapiens
Manually annotated by BRENDA team
Fried, L.F.; Duckworth, W.; Zhang, J.H.; OConnor, T.; Brophy, M.; Emanuele, N.; Huang, G.D.; McCullough, P.A.; Palevsky, P.M.; Seliger, S.; Warren, S.R.; Peduzzi, P.; Peduzzi, P.
Design of combination angiotensin receptor blocker and angiotensin-converting enzyme inhibitor for treatment of diabetic nephropathy (VA NEPHRON-D)
Clin. J. Am. Soc. Nephrol.
4
361-368
2009
Homo sapiens
Manually annotated by BRENDA team
Algasham, A.; Ismail, H.; Dewaidar, M.; Settin, A.A.
Methylenetetrahydrofolate reductase and angiotensin-converting enzyme gene polymorphisms among Saudi population from Qassim region
Genet. Test. Mol. Biomarkers
13
817-820
2009
Homo sapiens
Manually annotated by BRENDA team
Erdoes, E.G.; Tan, F.; Skidgel, R.A.
Angiotensin I-converting enzyme inhibitors are allosteric enhancers of kinin B1 and B2 receptor function
Hypertension
55
214-220
2010
Homo sapiens
Manually annotated by BRENDA team
Yeo, S.K.; Liong, M.T.
Angiotensin I-converting enzyme inhibitory activity and bioconversion of isoflavones by probiotics in soymilk supplemented with prebiotics
Int. J. Food Sci. Nutr.
61
161-181
2010
Homo sapiens
Manually annotated by BRENDA team
Adarkwah, C.C.; Gandjour, A.
Cost-effectiveness of angiotensin-converting enzyme inhibitors and angiotensin II receptor blockers in newly diagnosed type 2 diabetes in Germany
Int. J. Technol. Assess. Health Care
26
62-70
2010
Homo sapiens
Manually annotated by BRENDA team
Guang, C.; Phillips, R.D.
Plant food-derived angiotensin I converting enzyme inhibitory peptides
J. Agric. Food Chem.
57
5113-5120
2009
Homo sapiens
Manually annotated by BRENDA team
Nogata, Y.; Nagamine, T.; Yanaka, M.; Ohta, H.
Angiotensin I converting enzyme inhibitory peptides produced by autolysis reactions from wheat bran
J. Agric. Food Chem.
57
6618-6622
2009
Homo sapiens
Manually annotated by BRENDA team
Escudero, E.; Sentandreu, M.A.; Arihara, K.; Toldra, F.
Angiotensin I-converting enzyme inhibitory peptides generated from in vitro gastrointestinal digestion of pork meat
J. Agric. Food Chem.
58
2895-2901
2010
Homo sapiens
Manually annotated by BRENDA team
Balti, R.; Nedjar-Arroume, N.; Adje, E.Y.; Guillochon, D.; Nasri, M.
Analysis of novel angiotensin I-converting enzyme inhibitory peptides from enzymatic hydrolysates of cuttlefish (Sepia officinalis) muscle proteins
J. Agric. Food Chem.
58
3840-3846
2010
Homo sapiens
Manually annotated by BRENDA team
Udenigwe, C.C.; Aluko, R.E.
Antioxidant and angiotensin converting enzyme-inhibitory properties of a flaxseed protein-derived high Fischer ratio peptide mixture
J. Agric. Food Chem.
58
4762-4768
2010
Homo sapiens
Manually annotated by BRENDA team
Wang, S.R.; Chen, C.; Xiong, M.J.; Wu, L.P.; Ye, L.M.
Quantitative retention-activity relationship models of angiotensin converting enzyme inhibitors using biopartitioning micellar chromatography
J. Chromatogr. Sci.
48
134-139
2010
Homo sapiens
Manually annotated by BRENDA team
Kim, T.B.; Oh, S.Y.; Park, H.K.; Jeon, S.G.; Chang, Y.S.; Lee, K.Y.; Cho, Y.S.; Chae, I.H.; Kim, Y.K.; Cho, S.H.; Moon, H.B.; Min, K.U.; Kim, Y.Y.
Polymorphisms in the neurokinin-2 receptor gene are associated with angiotensin-converting enzyme inhibitor-induced cough
J. Clin. Pharm. Ther.
34
457-464
2009
Homo sapiens
Manually annotated by BRENDA team
Kim, K.H.; Jeong, M.H.; Cho, S.H.; Moon, J.Y.; Hong, Y.J.; Park, H.W.; Kim, J.H.; Ahn, Y.; Cho, J.G.; Park, J.C.; Kang, J.C.
Clinical effects of calcium channel blocker and Angiotensin converting enzyme inhibitor on endothelial function and arterial stiffness in patients with angina pectoris
J. Korean Med. Sci.
24
223-231
2009
Homo sapiens
Manually annotated by BRENDA team
Jullien, N.; Makritis, A.; Georgiadis, D.; Beau, F.; Yiotakis, A.; Dive, V.
Phosphinic tripeptides as dual angiotensin-converting enzyme C-domain and endothelin-converting enzyme-1 inhibitors
J. Med. Chem.
53
208-220
2010
Homo sapiens
Manually annotated by BRENDA team
Wijesekara, I.; Kim, S.K.
Angiotensin-I-converting enzyme (ACE) inhibitors from marine resources: prospects in the pharmaceutical industry
Mar. Drugs
8
1080-1093
2010
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Hernandez, A.A.; Moreso, F.; Bayes, B.; Lauzurica, R.; Sanz-Guajardo, D.; Gomez-Huertas, E.; Pereira, P.; Paul, J.; Crespo, J.; Amenabar, J.J.; Oliver, J.; Seron, D.
Angiotensin-converting enzyme inhibitors and angiotensin receptor blockers in renal transplantation between 1990 and 2002 in Spain
NDT plus
3
ii21-ii25
2010
Homo sapiens
Manually annotated by BRENDA team
Tiryaki, O.; Usalan, C.; Buyukhatipoglu, H.
Effect of combined angiotensin-converting enzyme and aldosterone inhibition on plasma plasminogen activator inhibitor type 1 levels in chronic hypertensive patients
Nephrology
15
211-215
2010
Homo sapiens
Manually annotated by BRENDA team
Kolesnyk, I.; Struijk, D.G.; Dekker, F.W.; Krediet, R.T.
Effects of angiotensin-converting enzyme inhibitors and angiotensin II receptor blockers in patients with chronic kidney disease
Neth. J. Med.
68
15-23
2010
Homo sapiens
Manually annotated by BRENDA team
Jimsheena, V.K.; Gowda, L.R.
Arachin derived peptides as selective angiotensin I-converting enzyme (ACE) inhibitors: structure-activity relationship
Peptides
31
1165-1176
2010
Homo sapiens, Sus scrofa
Manually annotated by BRENDA team
Wu, C.K.; Luo, J.L.; Tsai, C.T.; Huang, Y.T.; Cheng, C.L.; Lee, J.K.; Lin, L.Y.; Lin, J.W.; Hwang, J.J.; Chiang, F.T.
Demonstrating the pharmacogenetic effects of angiotensin-converting enzyme inhibitors on long-term prognosis of diastolic heart failure
Pharmacogenomics J.
10
46-53
2010
Homo sapiens
Manually annotated by BRENDA team
Gordon, K.; Balyasnikova, I.V.; Nesterovitch, A.B.; Schwartz, D.E.; Sturrock, E.D.; Danilov, S.M.
Fine epitope mapping of monoclonal antibodies 9B9 and 3G8 to the N domain of angiotensin-converting enzyme (CD143) defines a region involved in regulating angiotensin-converting enzyme dimerization and shedding
Tissue Antigens
75
136-150
2010
Homo sapiens (P12821)
Manually annotated by BRENDA team
Sinka, L.; Biasch, K.; Khazaal, I.; Peault, B.; Tavian, M.
Angiotensin-converting enzyme (CD143) specifies emerging lympho-hematopoietic progenitors in the human embryo
Blood
119
3712-3723
2012
Homo sapiens
Manually annotated by BRENDA team
Namazi, M.; Ashraf, A.; Handjani, F.; Eftekhar, E.; Kalafi, A.
Angiotensin converting enzyme activity in alopecia areata
Enzyme Res.
2014
694148
2014
Homo sapiens
Manually annotated by BRENDA team
Lo, J.; Patel, V.B.; Wang, Z.; Levasseur, J.; Kaufman, S.; Penninger, J.M.; Oudit, G.Y.
Angiotensin-converting enzyme 2 antagonizes angiotensin II-induced pressor response and NADPH oxidase activation in Wistar-Kyoto rats and spontaneously hypertensive rats
Exp. Physiol.
98
109-122
2013
Homo sapiens
Manually annotated by BRENDA team
Masuyer, G.; Akif, M.; Czarny, B.; Beau, F.; Schwager, S.L.; Sturrock, E.D.; Isaac, R.E.; Dive, V.; Acharya, K.R.
Crystal structures of highly specific phosphinic tripeptide enantiomers in complex with the angiotensin-I converting enzyme
FEBS J.
281
943-956
2014
Homo sapiens (P12821), Homo sapiens, Drosophila melanogaster (Q10714)
Manually annotated by BRENDA team
Darewicz, M.; Borawska, J.; Vegarud, G.E.; Minkiewicz, P.; Iwaniak, A.
Angiotensin I-converting enzyme (ACE) inhibitory activity and ACE inhibitory peptides of salmon (Salmo salar) protein hydrolysates obtained by human and porcine gastrointestinal enzymes
Int. J. Mol. Sci.
15
14077-14101
2014
Homo sapiens
Manually annotated by BRENDA team
Hocharoen, L.; Joyner, J.C.; Cowan, J.A.
N- versus C-domain selectivity of catalytic inactivation of human angiotensin converting enzyme by lisinopril-coupled transition metal chelates
J. Med. Chem.
56
9826-9836
2013
Homo sapiens
Manually annotated by BRENDA team
Masuyer, G.; Schwager, S.L.; Sturrock, E.D.; Isaac, R.E.; Acharya, K.R.
Molecular recognition and regulation of human angiotensin-I converting enzyme (ACE) activity by natural inhibitory peptides
Sci. Rep.
2
717
2012
Homo sapiens (P12821), Homo sapiens
Manually annotated by BRENDA team
Rutkowska-Zapala, M.; Suski, M.; Szatanek, R.; Lenart, M.; Weglarczyk, K.; Olszanecki, R.; Grodzicki, T.; Strach, M.; Gasowski, J.; Siedlar, M.
Human monocyte subsets exhibit divergent angiotensin I-converting activity
Clin. Exp. Immunol.
181
126-132
2015
Homo sapiens (P12821), Homo sapiens
Manually annotated by BRENDA team
Bhaskar, B.; Ananthanarayan, L.; Jamdar, S.N.
Effect of enzymatic hydrolysis on the functional, antioxidant, and angiotensin I-converting enzyme (ACE) inhibitory properties of whole horse gram flour
Food Sci. Biotechnol.
28
43-52
2019
Homo sapiens (P12821)
Manually annotated by BRENDA team
Kryukova, O.V.; Tikhomirova, V.E.; Golukhova, E.Z.; Evdokimov, V.V.; Kalantarov, G.F.; Trakht, I.N.; Schwartz, D.E.; Dull, R.O.; Gusakov, A.V.; Uporov, I.V.; Kost, O.A.; Danilov, S.M.
Tissue specificity of human angiotensin I-converting enzyme
PLoS ONE
10
e0143455
2015
Homo sapiens (P12821), Homo sapiens
Manually annotated by BRENDA team
Lubbe, L.; Sewell, B.T.; Woodward, J.D.; Sturrock, E.D.
Cryo-EM reveals mechanisms of angiotensin I-converting enzyme allostery and dimerization
EMBO J.
41
e110550
2022
Homo sapiens (P12821)
Manually annotated by BRENDA team