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Information on EC 3.4.15.1 - peptidyl-dipeptidase A
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3.4.15.1 peptidyl-dipeptidase ASpecify your search results
Word Map
- 3.4.15.1
- hypertension
-
blocker
- arterial
- cardiovascular
-
antihypertensive
- cardiac
-
renin-angiotensin
- ventricular
- captopril
- myocardial
-
systolic
- coronary
-
diuretic
- infarction
- renin
-
aceis
-
beta-blockers
- enalapril
- glomerular
-
diastolic
- nephropathy
-
placebo
-
ejection
- proteinuria
- mellitus
- bradykinin
- creatinine
-
hemodynamic
- hypertrophy
-
congestive
- aldosterone
-
vasodilator
- statin
-
renin-angiotensin-aldosterone
- hg
-
normotensive
-
prescript
-
double-blind
- aspirin
- sarcoidosis
- angiotensinogen
- losartan
-
pressor
- cough
-
microalbuminuria
- digoxin
-
renovascular
-
all-cause
-
renoprotective
-
hypotensive
- drug development
- veterinary medicine
- medicine
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
ACE, ACE-1, ACE2, ACEI, ANCE, ANG I-converting enzyme, angiotensin 1 converting enzyme, angiotensin converting enzyme, angiotensin converting enzyme 1, angiotensin converting enzyme I, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ACE
ACE2
ACEI
ANCE
ANG I-converting enzyme
angiotensin 1 converting enzyme
-
-
-
-
angiotensin converting enzyme
angiotensin I converting enzyme
angiotensin I-converting enzyme
angiotensin-converting enzyme
angiotensin-I converting enzyme
angiotensin-I-converting enzyme
carboxycathepsin
-
-
-
-
carboxypeptidase, dipeptidyl
-
-
-
-
CD143
CD143 antigen
-
-
-
-
DCP
Dcp1
Dipeptidyl carboxypeptidase
dipeptidyl carboxypeptidase I
-
-
-
-
endothelial cell peptidyl dipeptidase
-
-
-
-
kininase II
PDH
-
-
-
-
peptidase P
-
-
-
-
peptidyl dipeptidase
peptidyl dipeptidase A
peptidyl dipeptidase I
-
-
-
-
peptidyl dipeptidase-4
-
-
-
-
peptidyl dipeptide hydrolase
peptidyl-dipeptide hydrolase
-
-
-
-
peptidyldipeptide hydrolase
sACE
somatic ACE
TACE
ACE
-
-
-
-
ACE
-
-
678698, 678710, 679008, 679070, 679511, 679708, 681184, 695587, 697020, 697516, 697714, 699475, 700299, 701190, 701430, 707023, 707024, 707026, 707029, 707286, 707904, 707939, 708183, 708199, 708590, 708687, 708782, 708800, 708830, 708834, 708844, 708845, 708848, 709266, 709279, 709411, 709470, 709786, 710054, 710060, 710062, 710213, 710222, 731532, 731953
ACE
-
-
ACE
-
-
angiotensin converting enzyme
-
-
-
-
angiotensin I converting enzyme
-
-
angiotensin I-converting enzyme
-
-
-
-
angiotensin I-converting enzyme
-
-
angiotensin I-converting enzyme
-
-
angiotensin-converting enzyme
-
-
-
-
angiotensin-converting enzyme
-
-
DCP
-
-
-
-
Dipeptidyl carboxypeptidase
-
-
-
-
kininase II
-
-
-
-
peptidyl dipeptidase
-
-
-
-
peptidyl dipeptidase A
-
-
-
-
peptidyl dipeptide hydrolase
-
-
-
-
peptidyldipeptide hydrolase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
exopeptidase, C-terminus, dipeptide
-
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CAS REGISTRY NUMBER
COMMENTARY
9015-82-1
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(7-methoxycoumarin-2-acetic acid)-Ala-Ser-Asp-Lys-(N3-(2,4-dinitrophenyl)-L-2,3-diaminopropyl) + H2O
?
-
-
-
?
(7-methoxycoumarin-2-acetic acid)-Ser-Asp-Lys-(N3-(2,4-dinitrophenyl)-L-2,3-diaminopropyl) + H2O
?
-
-
-
?
(7-methoxycoumarin-2-acetyl)-Tyr-Val-Ala-Asp-Ala-Phe-Lys-(2,4-dinitrophenyl)-OH + H2O
?
-
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Ala-Ser-Asp-Lys-N3-(2,4-dinitrophenyl)-L-diaminopropionionate + H2O
?
-
-
-
-
?
1-dimethylaminonaphthalene-5-sulfonyl-Gly-Gly-Gly + H2O
1-dimethylaminonaphthalene-5-sulfonyl-Gly + Gly-Gly
-
-
-
-
?
2-aminobenzoyl-L-Phe-L-Arg-L-Lys-2,4-dinitrophenyl-L-Pro + H2O
?
-
-
-
-
?
2-furylacryloyl-Phe-Gly-Gly + H2O
2-furylacrylic acid + Phe-Gly-Gly
-
-
-
?
3-hydroxybutyrylglycyl-glycyl-glycine + H2O
3-hydroxybutyrate + glycyl-glycine
-
synthetic substrate for use in an spectrophotometric assay of ACE inhibitory activity, method development involving automation of the measurement with immobilized aminoacylase and 3-hydroxybutyrate dehydrogenase, optimization, detailed overview. Application to the screening of ACE inhibitors
-
-
?
3-hydroxybutyrylglycyl-glycyl-glycine + H2O
3-hydroxybutyrylglycine + Gly-Gly
-
-
-
-
?
7-amido-4-carboxymethylcoumarin-YVADAPK(Dnp)-OH + H2O
dinitrophenol + 7-amino-4-carbamoylmethylcoumarin-YVADAPK
-
-
-
-
?
acetyl-His-Pro-(NO2)Phe-His-Leu + H2O
acetyl-His-Pro-(NO2)Phe + His-Leu
-
-
-
-
?
amyloid beta-protein 1-40 + H2O
amyloid beta-peptide(1-7) + amyloid beta-peptide(8-40)
-
ACE cleaves amyloid beta-protein 1-40 between Asp7 and Ser8
-
-
?
amyloid beta-protein 1-42 + H2O
amyloid beta-peptide(1-40) + amyloid beta-peptide(41-42)
-
ACE cleaves amyloid beta-protein 1-42 at multiple sites
-
-
?
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met + H2O
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly + Leu-Met
-
-
-
-
?
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met-NH2 + H2O
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly + Leu-Met-NH2
Asn-Arg-Val-Tyr-Ile-His-Pro-(NO2)Phe-His-Leu + H2O
Asn-Arg-Val-Tyr-Ile-His-Pro-(NO2)Phe + His-Leu
-
-
-
-
?
bradykinin + H2O
Arg-Pro-Pro-Gly-Phe + Ser-Pro + Phe-Arg
-
i.e. Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
-
-
?
bradykinin + H2O
L-Phe-L-Arg + L-Ser-L-Pro + L-Arg-L-Pro-L-Pro-Gly-L-Phe
-
-
-
-
?
Gly-Ile-His-Pro-(NO2)Phe-His-Leu + H2O
Gly-Ile-His-Pro-(NO2)Phe + His-Leu
-
-
-
-
?
gonadotropin-releasing hormone + H2O
?
a bridging interaction between Arg500 of the N-domain and Arg8 of gonadotropin-releasing hormone that involves a buried chloride ion may account for its role in the specificity of the N-domain for endoproteolytic cleavage of the substrate at the NH2-terminus in vitro
-
-
?
His-Lys-Thr-Asp-Ser-Phe-Val-Gly-Leu-Met-NH2 + H2O
His-Lys-Thr-Asp-Ser-Phe-Val-Gly + Leu-Met-NH2
-
i.e. substance K, degraded by striatal but not by lung enzyme
-
-
?
Luteinizing hormone-releasing hormone + H2O
?
-
degraded by striatal and by lung enzyme
-
-
?
LVVYPWTQRY + H2O
LVVYPWTQ + RY + LVVY + PW + LVVYPW + TQ
-
-
dipeptide TQ is unidentified. Sequential removal of dipeptides in three consecutive steps
?
N-(3-(2-furyl)acryloyl)-L-Phe-Gly-Gly + H2O
2-furylacrylic acid + L-Phe-Gly-Gly
-
-
-
?
N-(3-(2-furyl)acryloyl)-L-Phe-Gly-Gly + H2O
N-(3-(2-furyl)acrylic acid) + Phe-Gly-Gly
-
-
-
?
N-(3-(2-furyl)acryloyl)-L-Phe-Phe-Arg + H2O
2-furylacrylic acid + L-Phe-Phe-Arg
-
-
-
?
N-(3-(2-furyl)acryloyl)-Phe-Ala-Ala + H2O
2-furylacrylic acid + Phe-Ala-Ala
-
-
-
?
N-(3-(2-furyl)acryloyl)-Phe-Ala-Gly + H2O
2-furylacrylic acid + Phe-Ala-Gly
-
-
-
?
N-(3-(2-furyl)acryloyl)-Phe-Ala-Lys + H2O
2-furylacrylic acid + Phe-Ala-Lys
-
-
-
?
N-(3-(2-furyl)acryloyl)-Phe-Ala-Pro + H2O
2-furylacrylic acid + Phe-Ala-Pro
-
-
-
?
N-(3-(2-furyl)acryloyl)-Phe-Gly-Gly + H2O
2-furylacrylic acid + Phe-Gly-Gly
-
-
-
?
N-(3-(2-furyl)acryloyl)-Phe-Phe-Arg + H2O
2-furylacrylic acid + Phe-Phe-Arg
-
-
-
?
N-(3-[2-furyl]acryloyl)-L-phenylalanylglycylglycine + H2O
?
-
-
-
?
N-benzyloxycarbonyl-Phe-His-Leu + H2O
N-benzyloxycarbonyl-Phe + His-Leu
-
-
-
?
N-[3-(2-furyl)acryloyl]-L-Phe-Gly-Gly + H2O
2-furylacrylic acid + L-Phe-Gly-Gly
-
-
-
-
?
N-[3-(2-furyl)acryloyl]-L-phenylalanyl-glycyl-glycine + H2O
?
-
-
-
-
?
N-[3-(2-furyl)acryloyl]-L-phenylalanyl-glycyl-glycine + H2O
N-[3-(2-furyl)acryloyl]-L-phenylalanine + glycyl-glycine
N-[3-(2-furyl)acryloyl]-Phe-Gly-Gly + H2O
N-[3-(2-furyl)acryloyl]-Phe + Gly-Gly
-
-
-
-
?
o-aminobenzoyl-FDK-(dinitrophenyl)-P-OH + H2O
o-aminobenzoyl-FD + K-(dinitrophenyl)-P-OH
-
-
-
?
o-aminobenzoyl-FRK-(dinitrophenyl)-P-OH + H2O
o-aminobenzoyl-FR + K-(dinitrophenyl)-P-OH
-
-
-
?
o-aminobenzoyl-GFSPFAQ-(N-2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoyl-GFSPFA + Gln-(N-2,4-dinitrophenyl)ethylenediamine
-
-
-
?
o-aminobenzoyl-GFSPFEQ-(N-2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoyl-GFSPFE + Gln-(N-2,4-dinitrophenyl)ethylenediamine
-
-
-
?
o-aminobenzoyl-GFSPFFQ-(N-2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoyl-GFSPFF + Gln-(N-2,4-dinitrophenyl)ethylenediamine
-
-
-
?
o-aminobenzoyl-GFSPFLQ-(N-2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoyl-GFSPFL + Gln-(N-2,4-dinitrophenyl)ethylenediamine
-
-
-
?
o-aminobenzoyl-GFSPFQQ-(N-2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoyl-GFSPFQ + Gln-(N-2,4-dinitrophenyl)ethylenediamine
-
-
-
?
o-aminobenzoyl-GFSPFRA-(N-2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoyl-GFSPFR + Ala-(N-2,4-dinitrophenyl)ethylenediamine
-
-
-
?
o-aminobenzoyl-GFSPFRF-(N-2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoyl-GFSPFR + Phe-(N-2,4-dinitrophenyl)ethylenediamine
-
-
-
?
o-aminobenzoyl-GFSPFRI-(N-2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoyl-GFSPFR + Ile-(N-2,4-dinitrophenyl)ethylenediamine
-
-
-
?
o-aminobenzoyl-GFSPFRN-(N-2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoyl-GFSPFR + Asn-(N-2,4-dinitrophenyl)ethylenediamine
-
-
-
?
o-aminobenzoyl-GFSPFRQ-(N-2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoyl-GFSPFR + Gln-(N-2,4-dinitrophenyl)ethylenediamine
-
-
-
?
o-aminobenzoyl-GFSPFRR-(N-2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoyl-GFSPFR + Arg-(N-2,4-dinitrophenyl)ethylenediamine
-
-
-
?
o-aminobenzoyl-GFSPFRS-(N-2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoyl-GFSPFR + Ser-(N-2,4-dinitrophenyl)ethylenediamine
-
-
-
?
o-aminobenzoyl-GFSPFSQ-(N-2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoyl-GFSPFS + Gln-(N-2,4-dinitrophenyl)ethylenediamine
-
-
-
?
o-aminobenzoyl-Phe-Arg-Lys(2,4-dinitrophenyl)-Pro-hydroxide + H2O
?
-
-
-
?
o-aminobenzoyl-SDK-(dinitrophenyl)-P-OH + H2O
o-aminobenzoyl-SD + K-(dinitrophenyl)-P-OH
-
-
-
?
o-aminobenzoyl-SRK-(dinitrophenyl)-P-OH + H2O
o-aminobenzoyl-SR + K-(dinitrophenyl)-P-OH
-
-
-
?
o-aminobenzoyl-TDK-(dinitrophenyl)-P-OH + H2O
o-aminobenzoyl-TD + K-(dinitrophenyl)-P-OH
-
-
-
?
o-aminobenzoyl-TRK-(dinitrophenyl)-P-OH + H2O
o-aminobenzoyl-TR + K-(dinitrophenyl)-P-OH
-
-
-
?
o-aminobenzoyl-YDK-(dinitrophenyl)-P-OH + H2O
o-aminobenzoyl-YD + K-(dinitrophenyl)-P-OH
-
-
-
?
o-aminobenzoyl-YRK-(dinitrophenyl)-P-OH + H2O
o-aminobenzoyl-YR + K-(dinitrophenyl)-P-OH
-
-
-
?
physalaemin + H2O
pGlu-Ala-Asp-Pro-Asn-Lys-Phe-Tyr-Gly + Leu-Met-NH2
-
degraded by striatal and by lung enzyme
-
-
?
tert-butoxycarbonyl-Phe-Ala-Pro + H2O
tert-butoxycarbonyl-Phe + Ala-Pro
-
-
-
-
?
Tyr-Gly-Gly-Phe-Met-Arg-Gly-Leu + H2O
Tyr-Gly-Gly-Phe-Met-Arg + Gly-Leu
-
-
-
-
?
Tyr-Ile-His-Pro-(NO2)Phe-His-Leu + H2O
Tyr-Ile-His-Pro-(NO2)Phe + His-Leu
-
-
-
-
?
Z-phenylalanyl-histidyl-leucine + H2O
Z-phenylalanine + histidyl-leucine
-
-
-
?
2-furanacryloyl-Phe-Gly-Gly + H2O
2-furanacryloyl-Phe + Gly-Gly
-
3-(2-furanacryloyl)-Phe-Gly-Gly
-
-
?
amyloid beta-peptide(1-40) + H2O
amyloid beta-peptide(1-7) + amyloid beta-peptide(8-40)
-
cleavage at the Asp7-Ser9 bond
-
?
amyloid beta-peptide(1-40) + H2O
amyloid beta-peptide(1-7) + amyloid beta-peptide(8-40)
-
cleavage at the Asp7-Ser9 bond. Compared with amyloid beta-peptide(1-40), aggregation and cytotoxic effects of the degradation products amyloid beta-peptide(1-7) and amyloid beta-peptide(8-40) are reduced ot virtually absent. The enzyme inhibits aggregation, deposition, and cytotoxicity of amyloid beta-peptide in vitro may affect susceptibility to Alzheimer‘s disease
-
?
amyloid beta-protein 1-42 + H2O
amyloid beta-protein 1-420 + ?
-
angiotensin-converting enzyme converts amyloid beta-protein 1-42 to amyloid beta-protein1-40. ACE regulates Abeta1-42/Abeta1-40 ratio in vivo by converting secreted Abeta1-42 to Abeta1-40 and degrading Abetas.The upregulation of ACE activity can be a novel therapeutic strategy for Alzheimer’s disease
-
-
?
amyloid beta-protein 1-42 + H2O
amyloid beta-protein 1-420 + ?
-
angiotensin-converting enzyme converts amyloid beta-protein1-42 to amyloid beta-protein1-40. ACE regulates Abeta1-42/Abeta1-40 ratio in vivo by converting secreted Abeta1-42 to Abeta1-40 and degrading Abetas. The upregulation of ACE activity can be a novel therapeutic strategy for Alzheimer’s disease
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
-
the enzyme plays an important role in blood pressure homeostasis
-
?
angiotensin I + H2O
angiotensin II + His-Leu
-
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
-
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
-
i.e. DRVYIHPFHL
i.e. DRVYIHPF
-
?
angiotensin I + H2O
angiotensin II + His-Leu
-
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
-
about 5% of the activity with hippury-Lys-Leu
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
-
the effect on angiotensin I containing the paramagnetic 2,2,6,6-tetramethylpiperidine-1-oxyl-4-amino-4-carboxylic acid (TOAC) at positions 1, 3, 8, and 9 is studied. TOAC1-Ang I and TOAC3-Ang I are cleaved by ACE. TOAC8-Ang I and TOAC9-Ang I are not cleaved
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
-
angiotensin II is a vasoconstrictor that raises blood pressure and is formed from angiotensin I by the angiotensin I converting enzyme in the reninangiotensin system
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
-
i.e. DRVYIHPFHL
i.e. DRVYIHPF
-
?
angiotensin I + H2O
angiotensin II + His-Leu
-
i.e. DRVYIHPFHL
i.e. DRVYIHPF
-
?
angiotensin I + H2O
angiotensin II + His-Leu
-
enzyme plays a major role in blood pressure regulation
-
?
angiotensin I + H2O
angiotensin II + L-His-L-Leu
-
-
-
-
?
angiotensin I + H2O
angiotensin II + L-His-L-Leu
-
-
-
-
?
angiotensin I + H2O
angiotensin II + L-His-L-Leu
-
-
-
-
?
angiotensin I + H2O
angiotensin II + L-His-L-Leu
-
-
-
?
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met-NH2 + H2O
?
-
cleavage sites: Arg-Pro-/-Lys-Pro-/-Gln-Gln-/-Phe-Phe-/-Gly-Leu-Met-NH2
-
?
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met-NH2 + H2O
?
-
i.e. substance P, lung and brain ACE cleave substance P via two pathways. In one pathway ACE first releases Gly-Leu-Met-NH2 and then dipeptides sequentially from the carboxyl terminus. The other first produces Leu-Met-NH2 and then releases dipeptides to leave substance P(1-5)
-
-
?
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met-NH2 + H2O
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly + Leu-Met-NH2
-
-
-
-
?
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met-NH2 + H2O
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly + Leu-Met-NH2
-
-
-
-
?
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met-NH2 + H2O
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly + Leu-Met-NH2
-
i.e. substance P
-
?
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met-NH2 + H2O
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly + Leu-Met-NH2
-
lung and brain ACE cleave substance P via two pathways. In one pathway ACE first releases Gly-Leu-Met-NH2 and then dipeptides sequentially from the carboxyl terminus. The other first produces Leu-Met-NH2 and then releases dipeptides to leave substance P(1-5)
-
?
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met-NH2 + H2O
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly + Leu-Met-NH2
-
primary cleavage at the Phe8-Gly9 bond followed by succesive dipeptide cleavages from the newly formed C-terminus, cleavage of the Gly9-Leu10 bond is relatively minor
-
-
?
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met-NH2 + H2O
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly + Leu-Met-NH2
-
primary cleavage of Phe8-Gly9
-
-
?
benzyloxycarbonyl-(NO2)Phe-His-Leu + H2O
benzyloxycarbonyl-(NO2)Phe + His-Leu
-
-
-
-
?
benzyloxycarbonyl-(NO2)Phe-His-Leu + H2O
benzyloxycarbonyl-(NO2)Phe + His-Leu
-
-
-
-
?
benzyloxycarbonyl-Phe-His-Leu + H2O
benzyloxycarbonyl-Phe + His-Leu
-
-
-
-
?
benzyloxycarbonyl-Phe-His-Leu + H2O
benzyloxycarbonyl-Phe + His-Leu
-
-
-
?
bradykinin + H2O
?
-
bradykinin is a nonapeptide released from high molecular weight kininogen, it exerts its vasodilatory effect mainly by stimulation of B2 receptors
-
-
?
bradykinin + H2O
Phe-Arg + Ser-Pro + Arg-Pro-Pro-Gly-Phe
-
-
Arg-Pro-Pro + Gly-Phe + Ser-Pro + Phe-Arg
?
bradykinin + H2O
Phe-Arg + Ser-Pro + Arg-Pro-Pro-Gly-Phe
-
-
Arg-Pro-Pro + Gly-Phe + Ser-Pro + Phe-Arg
?
bradykinin + H2O
Phe-Arg + Ser-Pro + Arg-Pro-Pro-Gly-Phe
-
-
-
-
?
bradykinin + H2O
Phe-Arg + Ser-Pro + Arg-Pro-Pro-Gly-Phe
-
-
Phe-Arg + Ser-Pro -Arg-Pro-Pro-Gly-Phe
?
bradykinin + H2O
Phe-Arg + Ser-Pro + Arg-Pro-Pro-Gly-Phe
-
about 3.5% of the activity with hippury-Lys-Leu
-
?
bradykinin + H2O
Phe-Arg + Ser-Pro + Arg-Pro-Pro-Gly-Phe
-
-
hydrolyzes Phe-Arg + Ser-Pro from the C-terminus of bradykinin
?
bradykinin + H2O
Phe-Arg + Ser-Pro + Arg-Pro-Pro-Gly-Phe
-
-
hydrolyzes Phe-Arg + Ser-Pro from the C-terminus of bradykinin
?
bradykinin + H2O
Phe-Arg + Ser-Pro + Arg-Pro-Pro-Gly-Phe
-
-
-
-
?
furanacryloyl-L-Phe-Gly-Gly + H2O
furanacryloyl-L-Phe + Gly-Gly
-
-
-
-
?
hippuryl-His-Leu + H2O
hippuric acid + His-Leu
-
-
-
-
?
hippuryl-His-Leu + H2O
hippuric acid + His-Leu
-
-
81211, 81212, 81225, 81231, 81234, 81236, 81238, 81239, 81240, 81241, 81242, 81245, 81246, 81247, 81248, 81277, 81282, 81288
-
-
?
hippuryl-His-Leu + H2O
hippuric acid + His-Leu
-
colorimetric assay method
-
-
?
hippuryl-His-Leu + H2O
hippuric acid + His-Leu
-
-
-
-
?
hippuryl-His-Leu + H2O
hippuric acid + His-Leu
-
-
668985, 669020, 669023, 669026, 669033, 678863, 680284, 680316, 680317, 681160, 681163, 681562, 682248, 707653, 707763, 707764, 708537, 708837, 708857, 710252
-
-
?
hippuryl-His-Leu + H2O
hippuric acid + His-Leu
-
-
81211, 81219, 81220, 81241, 81244, 81252, 81254, 81283, 667885, 680293, 681562, 707783, 710160, 731569, 732968
-
-
?
hippuryl-His-Leu + H2O
hippuric acid + His-Leu
-
-
-
-
?
hippuryl-His-Leu + H2O
hippuric acid + His-Leu
-
colorimetric quantification of released hippuric acid, using pyridine and benzene sulfonyl chloride, assay method evaluation, overview
-
-
?
hippuryl-L-His-L-Leu + H2O
hippuric acid + L-His-L-Leu
-
-
-
-
?
hippuryl-L-His-L-Leu + H2O
hippuric acid + L-His-L-Leu
-
-
-
-
?
hippuryl-L-His-L-Leu + H2O
hippuric acid + L-His-L-Leu
-
-
-
-
?
MCA-Ala-Ser-Asp-Lys-Dap(DNP)-OH + H2O
?
angiotensin-converting enzyme
-
-
?
MCA-Ala-Ser-Asp-Lys-Dap(DNP)-OH + H2O
?
angiotensin-converting enzyme
-
-
?
MCA-Tyr-Val-Ala-Asp-Ala-Pro-Lys(DNP)-OH + H2O
?
angiotensin-converting enzyme 2
-
-
?
MCA-Tyr-Val-Ala-Asp-Ala-Pro-Lys(DNP)-OH + H2O
?
angiotensin-converting enzyme 2
-
-
?
N-benzyloxycarbonyl-L-Phe-L-His-L-Leu + H2O
N-benzyloxycarbonyl-L-Phe + L-His-L-Leu
-
-
-
-
?
N-benzyloxycarbonyl-L-Phe-L-His-L-Leu + H2O
N-benzyloxycarbonyl-L-Phe + L-His-L-Leu
-
-
-
-
?
N-[3-(2-furyl)acryloyl]-L-phenylalanyl-glycyl-glycine + H2O
N-[3-(2-furyl)acryloyl]-L-phenylalanine + glycyl-glycine
-
-
-
-
?
N-[3-(2-furyl)acryloyl]-L-phenylalanyl-glycyl-glycine + H2O
N-[3-(2-furyl)acryloyl]-L-phenylalanine + glycyl-glycine
-
-
-
-
?
N-[3-(2-furyl)acryloyl]-L-phenylalanylglycylglycine + H2O
?
-
-
-
?
neurotensin + H2O
pGlu-Leu-Tyr-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Tyr + Ile-Leu
-
-
-
-
?
additional information
?
-
-
no cleavage of imido-bonds. No hydrolysis of angiotensin II and angiotensin III
-
?
additional information
?
-
ACE is a key regulator of blood pressure homeostasis
-
-
?
additional information
?
-
-
ACE is a key regulator of blood pressure homeostasis
-
-
?
additional information
?
-
-
the enzyme may play a role not only in the angiotensin-bradykinin system but also in the metabolism of circulating enkephalins and other bioactive peptides
-
-
?
additional information
?
-
AnCE is a single domain protein with ACE activity, an ACE homologue
-
-
?
additional information
?
-
-
AnCE is a single domain protein with ACE activity, an ACE homologue
-
-
?
additional information
?
-
-
may contribute to elevated blood pressure in hypertensive disease via conversion of angiotensin I to angiotensin II or inactivation of bradykinin
-
-
?
additional information
?
-
-
angiotensin-converting enzyme-2 is a regulatory protein of the renin-angiotensin system. ACE2 interacts with calmodulin and this association down-regulates shedding of the ACE2 ectodomain
-
-
?
additional information
?
-
-
neutral endopeptidase and angiotensin converting enzyme do not have additive effects regarding neuropeptide degradation
-
-
?
additional information
?
-
somatic angiotensin I-converting enzyme plays a central role in blood pressure regulation
-
-
?
additional information
?
-
-
ACE may play a role in human epidermis morphogenesis during fetal life and serve as an unrecognized marker for keratinocyte progenitor cells
-
-
?
additional information
?
-
-
complex formation witht e bradykinin B2 receptor
-
-
?
additional information
?
-
ACE comprises two homologous domains, that differ in their substrate preferences, overview
-
-
?
additional information
?
-
-
ACE comprises two homologous domains, that differ in their substrate preferences, overview
-
-
?
additional information
?
-
-
the enzyme enhances presentation of certain endogenously synthesized peptides to major histocompatibility complex class-I-restricted cytotoxic T-lymphocytes
-
-
?
additional information
?
-
-
primary enzyme that is involved in the degradation of Tyr-Gly-Gly-Phe-Met-Arg-Gly-Leu in brain
-
-
?
additional information
?
-
-
ACE structure-activity relationship, overview
-
-
?
additional information
?
-
-
potential role of follicular enzyme in early stages of follicular maturation and atresia
-
-
?
additional information
?
-
-
ACE degrades bradykinin, other vasoactive peptides, and activates angiotensin
-
-
?
additional information
?
-
ACE interacts with beta-arrestin1
-
-
?
additional information
?
-
-
ACE may influence trypsin biosynthesis in the larval gut by interacting with a trypsin-modulating oostatic factor
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
amyloid beta-peptide(1-40) + H2O
amyloid beta-peptide(1-7) + amyloid beta-peptide(8-40)
-
cleavage at the Asp7-Ser9 bond. Compared with amyloid beta-peptide(1-40), aggregation and cytotoxic effects of the degradation products amyloid beta-peptide(1-7) and amyloid beta-peptide(8-40) are reduced ot virtually absent. The enzyme inhibits aggregation, deposition, and cytotoxicity of amyloid beta-peptide in vitro may affect susceptibility to Alzheimer‘s disease
-
?
amyloid beta-protein 1-40 + H2O
amyloid beta-peptide(1-7) + amyloid beta-peptide(8-40)
-
ACE cleaves amyloid beta-protein 1-40 between Asp7 and Ser8
-
-
?
amyloid beta-protein 1-42 + H2O
amyloid beta-peptide(1-40) + amyloid beta-peptide(41-42)
-
ACE cleaves amyloid beta-protein 1-42 at multiple sites
-
-
?
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met-NH2 + H2O
?
-
i.e. substance P, lung and brain ACE cleave substance P via two pathways. In one pathway ACE first releases Gly-Leu-Met-NH2 and then dipeptides sequentially from the carboxyl terminus. The other first produces Leu-Met-NH2 and then releases dipeptides to leave substance P(1-5)
-
-
?
bradykinin + H2O
L-Phe-L-Arg + L-Ser-L-Pro + L-Arg-L-Pro-L-Pro-Gly-L-Phe
-
-
-
-
?
amyloid beta-protein 1-42 + H2O
amyloid beta-protein 1-420 + ?
-
angiotensin-converting enzyme converts amyloid beta-protein 1-42 to amyloid beta-protein1-40. ACE regulates Abeta1-42/Abeta1-40 ratio in vivo by converting secreted Abeta1-42 to Abeta1-40 and degrading Abetas.The upregulation of ACE activity can be a novel therapeutic strategy for Alzheimer’s disease
-
-
?
amyloid beta-protein 1-42 + H2O
amyloid beta-protein 1-420 + ?
-
angiotensin-converting enzyme converts amyloid beta-protein1-42 to amyloid beta-protein1-40. ACE regulates Abeta1-42/Abeta1-40 ratio in vivo by converting secreted Abeta1-42 to Abeta1-40 and degrading Abetas. The upregulation of ACE activity can be a novel therapeutic strategy for Alzheimer’s disease
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
-
the enzyme plays an important role in blood pressure homeostasis
-
?
angiotensin I + H2O
angiotensin II + His-Leu
-
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
-
i.e. DRVYIHPFHL
i.e. DRVYIHPF
-
?
angiotensin I + H2O
angiotensin II + His-Leu
-
angiotensin II is a vasoconstrictor that raises blood pressure and is formed from angiotensin I by the angiotensin I converting enzyme in the reninangiotensin system
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
-
i.e. DRVYIHPFHL
i.e. DRVYIHPF
-
?
angiotensin I + H2O
angiotensin II + His-Leu
-
enzyme plays a major role in blood pressure regulation
-
?
angiotensin I + H2O
angiotensin II + L-His-L-Leu
-
-
-
-
?
angiotensin I + H2O
angiotensin II + L-His-L-Leu
-
-
-
-
?
angiotensin I + H2O
angiotensin II + L-His-L-Leu
-
-
-
-
?
angiotensin I + H2O
angiotensin II + L-His-L-Leu
-
-
-
?
bradykinin + H2O
?
-
bradykinin is a nonapeptide released from high molecular weight kininogen, it exerts its vasodilatory effect mainly by stimulation of B2 receptors
-
-
?
additional information
?
-
ACE is a key regulator of blood pressure homeostasis
-
-
?
additional information
?
-
-
ACE is a key regulator of blood pressure homeostasis
-
-
?
additional information
?
-
-
the enzyme may play a role not only in the angiotensin-bradykinin system but also in the metabolism of circulating enkephalins and other bioactive peptides
-
-
?
additional information
?
-
AnCE is a single domain protein with ACE activity, an ACE homologue
-
-
?
additional information
?
-
-
AnCE is a single domain protein with ACE activity, an ACE homologue
-
-
?
additional information
?
-
-
may contribute to elevated blood pressure in hypertensive disease via conversion of angiotensin I to angiotensin II or inactivation of bradykinin
-
-
?
additional information
?
-
-
angiotensin-converting enzyme-2 is a regulatory protein of the renin-angiotensin system. ACE2 interacts with calmodulin and this association down-regulates shedding of the ACE2 ectodomain
-
-
?
additional information
?
-
-
neutral endopeptidase and angiotensin converting enzyme do not have additive effects regarding neuropeptide degradation
-
-
?
additional information
?
-
somatic angiotensin I-converting enzyme plays a central role in blood pressure regulation
-
-
?
additional information
?
-
-
ACE may play a role in human epidermis morphogenesis during fetal life and serve as an unrecognized marker for keratinocyte progenitor cells
-
-
?
additional information
?
-
-
complex formation witht e bradykinin B2 receptor
-
-
?
additional information
?
-
-
the enzyme enhances presentation of certain endogenously synthesized peptides to major histocompatibility complex class-I-restricted cytotoxic T-lymphocytes
-
-
?
additional information
?
-
-
primary enzyme that is involved in the degradation of Tyr-Gly-Gly-Phe-Met-Arg-Gly-Leu in brain
-
-
?
additional information
?
-
-
potential role of follicular enzyme in early stages of follicular maturation and atresia
-
-
?
additional information
?
-
-
ACE degrades bradykinin, other vasoactive peptides, and activates angiotensin
-
-
?
additional information
?
-
ACE interacts with beta-arrestin1
-
-
?
additional information
?
-
-
ACE may influence trypsin biosynthesis in the larval gut by interacting with a trypsin-modulating oostatic factor
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
Co2+
Na+
NaCl
Zinc
Zn2+
additional information
-
enzyme is not affected by addition of 0.1-1.0 mM CaCl2, Mn2Cl2, MgCl2 or 0.1 mM ZnCl2
Na+
-
at pH 7 increasing concentrations of NaCl result in a faster rate of conversion which reaches a plateau at 150-200 mM NaCl. The activation by NaCl at pH 7 is the result of a 330% increase in kcat/Km which is solely attributable to a lowering of the Km. At pH 8, maximal activity is achieved in absence of NaCl, weak inhibitory effect on hydrolysis of angiotensin I as salt concentrations increase from 0 to 200 mM
NaCl
-
stimulates hydrolysis of hippuryl-His-Leu in concentration-dependent manner between 0 and 300 mM
Zinc
-
0.3 mM ZnCl2 completely reverses the inhibition caused by 0.1 mM EDTA
Zinc
-
XcACE activity depends on zinc binding. Hydrolysis of 7-methoxycoumarin-4-yl-diacetyl-SDKP-N3 (2,4-dinitrophenyl)L-2,3-diaminopropionyl-OH is abolished after zinc chelation with EDTA and dialysis but is restored by zinc addition
Zn2+
-
ACE is a metallopeptidase. An activated water molecule complexed to Zn2+ acts as the nucleophile to attack the carbonyl group of the targeted peptide bond
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2E)-3-(3-amino-4-methoxyphenyl)-1-(3,4,5-trimethoxyphenyl)prop-2-en-1-one
-
-
(2E)-3-(3-fluoro-4-methoxyphenyl)-1-(3,4,5-trimethoxyphenyl)prop-2-en-1-one
-
-
(2E)-3-(3-hydroxy-4-methoxyphenyl)-1-(3,4,5-trimethoxyphenyl)prop-2-en-1-one
-
-
(2E)-3-(3-hydroxy-4-nitrophenyl)-1-(3,4,5-trimethoxyphenyl)prop-2-en-1-one
-
-
(2E)-3-(4-hydroxy-3-methoxyphenyl)-1-(3,4,5-trimethoxyphenyl)prop-2-en-1-one
-
-
(2E)-3-(4-methoxy-3-nitrophenyl)-1-(3,4,5-trimethoxyphenyl)prop-2-en-1-one
-
-
(2R)-2-((3-[hydroxyl (2-phenyl-(1R)-1-([(benzyloxy) carbonyl]-amino)ethyl)phosphinyl]-2-[(3-phenylisoxazol-5-yl)methyl]-1-oxopropyl)amino)-3-(4-hydroxy-phenyl) propanoic acid
(2S)-1-((3S)-3-amino-3-carboxypropyl)azetidine-2-carboxylic acid
-
IC50: 0.0033 mM
(2S)-2-((3-[hydroxyl (2-phenyl-(1R)-1-([(benzyloxy) carbonyl]-amino)ethyl)phosphinyl]-2-[(3-phenylisoxazol-5-yl)methyl]-1-oxopropyl)amino)-3-(4-hydroxy-phenyl) propanoic acid
(2S)-2-((3-[hydroxyl(2-phenyl-(1R)-1([(benzyloxy)carbonyl]amino)ethyl)phosphinyl]-(2R)-2-[(3-phenylisoxazol-5-yl)methyl]-1-oxopropyl)amino)-3-phenyl propanoic acid
-
-
(2S)-2-((3-[hydroxyl(2-phenyl-(1R)-1-([(benzyloxy)carbonyl]-amino)ethyl)phosphinyl]-(2R)-2-[(3-phenylisoxazol-5-yl)methyl]-1-oxopropyl)amino) 1H-Indole-3-propanoic acid
-
-
(2S)-2-((3-[hydroxyl(2-phenyl-(1R)-1-([(benzyloxy)carbonyl]-amino)ethyl)phosphinyl]-(2R)-2-[(3-phenylisoxazol-5-yl)methyl]-1-oxopropyl)amino)-3-(4-hydroxy-phenyl) propanoic acid
-
-
(2S)-2-((3-[hydroxyl(2-phenyl-(1R)-1-([(benzyloxy)carbonyl]-amino)ethyl)phosphinyl]-(2S)-2-[(3-phenylisoxazol-5-yl)methyl]-1-oxopropyl)amino) 1H-indole-3-propanoic acid
-
-
(2S)-2-((3-[hydroxyl(2-phenyl-(1R)-1-([(benzyloxy)carbonyl]-amino)ethyl)phosphinyl]-(2S)-2-[(3-phenylisoxazol-5-yl)methyl]-1-oxopropyl)amino)-3-(4-hydroxy-phenyl) propanoic acid
-
-
(2S)-2-([3-(1,1'-biphenyl)-2-([hydroxyl(2-phenyl-(1R)-1-([(benzyloxy)carbonyl]amino)ethyl)phosphinyl]methyl)-1-oxopropyl]-amino) 1H-indole-3-propanoic acid
-
-
(2S)-2-([3-(3'-[1,1'-biphenyl]-4''-yl-4',5'-dihydro-5'-isoxazolyl)-2-([hydroxyl(2-phenyl-(1R)-1-([(benzyloxy)carbonyl]amino)ethyl)-phosphinyl]methyl)-1-oxopropyl]amino) 1H-indole-3-propanoic acid
-
-
(2S)-2-[[(2S)-2-mercapto-3-methylpentanoyl]amino]-3-(1-naphthyl)propanoic acid
-
(2S)-2-[[(2S)-2-mercapto-3-methylpentanoyl]amino]-3-phenylpropanoic acid
-
(2S)-3-(4-hydroxyphenyl)-2-[[(2S)-2-mercapto-3-methylpentanoyl]amino]propanoic acid
-
(2S)-3-biphenyl-4-yl-2-[(2-mercapto-2-methylpropanoyl)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
1-cyclohexyl-3-(2-morpholinoethyl)carbodiimide metho-p-toluene sulfonate
-
20 mM, 99.6% inhibition
1-methyl-5-phenyl-3-(3,4,5-trimethoxyphenyl)-4,5-dihydro-1H-pyrazole
-
-
1-[(5S)-5-[(tert-butoxycarbonyl)amino]-4-oxo-6-phenylhexanoyl]-L-proline
-
15B2
-
an inhibitor isolated from the culture broth of Actinomadura sp. No. 937ZE-1
2''-hydroxynicotianamide
-
angiotensin-I converting enzyme inhibitor from buckwheat (Fagopyrum esculentum Moench) flour, IC50: 0.00008 mM
2-methoxy-4-[1-methyl-3-(3,4,5-trimethoxyphenyl)-4,5-dihydro-1H-pyrazol-5-yl]phenol
-
-
2-methoxy-5-[1-methyl-3-(3,4,5-trimethoxyphenyl)-4,5-dihydro-1H-pyrazol-5-yl]aniline
-
-
2-methoxy-5-[1-methyl-3-(3,4,5-trimethoxyphenyl)-4,5-dihydro-1H-pyrazol-5-yl]phenol
-
-
2-[([2-[(1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]cyclopentyl]carbonyl)amino]-3-(2,3-dihydro-1H-indol-3-yl)propanoate
-
3,6-Dihydroxy-1-phenazinecarboxylic acid
-
i.e. phenacein, competitive, reversed by Zn2+, isolated from a member of Streptomyces tanashiensis-zaomyceticus
5-(3,4,5-trihydroxyphenyl)-gamma-valerolactone
the metabolite has a hypotensive effect in vivo
5-(3,5-dihydroxyphenyl)-gamma-valerolactone
the metabolite has a hypotensive effect in vivo
5-(3-fluoro-4-methoxyphenyl)-1-methyl-3-(3,4,5-trimethoxyphenyl)-4,5-dihydro-1H-pyrazole
-
-
5-(3-methoxyphenyl)-1-methyl-3-(3,4,5-trimethoxyphenyl)-4,5-dihydro-1H-pyrazole
-
-
5-(4-methoxy-3-nitrophenyl)-1-methyl-3-(3,4,5-trimethoxyphenyl)-4,5-dihydro-1H-pyrazole
-
-
5-(4-methoxyphenyl)-1-methyl-3-(3,4,5-trimethoxyphenyl)-4,5-dihydro-1H-pyrazole
-
-
5-[1-methyl-3-(3,4,5-trimethoxyphenyl)-4,5-dihydro-1H-pyrazol-5-yl]-2-nitrophenol
-
-
9-[1-carboxy-3-(4-hydroxyphenyl)propylamino]octahydro-10-oxo-6H-pyridazo[1,2-a][1,2]diazepine-1-carboxylic acid
-
-
Ac-FKCRRWQWRMKKLGA-NH2
-
0.02 mM, 38% loss of activity with hippuryl-His-Leu, 41% loss of activity with angiotensin I
Ac-RKWHFW-NH2
-
0.02 mM, 42% loss of activity with hippuryl-His-Leu, 55% loss of activity with angiotensin I; 0.02 mM, 48% loss of activity with hippuryl-His-Leu
Ac-RKWLFW-NH2
-
0.02 mM, 26% loss of activity with hippuryl-His-Leu, 71% loss of activity with angiotensin I; 0.02 mM, 32% loss of activity with hippuryl-His-Leu
Ac-RRWQWR-NH2
-
0.02 mM, 29% loss of activity with hippuryl-His-Leu, 34% loss of activity with angiotensin I
acteoside
-
a phenylpropanoid glycoside isolated from ethanolic extracts of seeds of Plantago asiatica, collected from Jiang Xi Province in China. The compound shows ACE inhibitory activity in vitro, structure analysis by NMR, UV, IR and MS
Ala-His-Ser-Tyr
-
a noncompetitive inhibitor, the peptide is resistant to further degenration by pepsin, trypsin, and chymotrypsin
aliphatic monocarboxylates
-
degree of inhibition increases in proportion to their chain length up to C14
-
angiotensin converting enzyme inhibitor
-
ACE-I, inhibition is impacting both the renin-angiotensin cascade and the degradation metabolism of bradykinin, inhibition mechanism, overview. ACE-I is used as therapeutic agent in congestive heart failure, diabetic nephropathy, hypertension, and coronary artery disease. ACE-I medications can induce chronic cough, hypotension, hyperkalemia, bone marrow depression, angioedema, and rarely, hepatic failure. Angioedema involves a subcutaneous swelling reaction that evolves over several hours and is not associated with itching or pain, pathomechanism, detailed overview
-
angiotensin I converting enzyme inhibitory peptides
-
from wheat milling byproducts by proteolysis through aspartic proteases, optimally produced at pH 3.2. Milled whole grain, bran, shorts, and red dog acquire ACE inhibitory activity though water soaking treatment, preparation of shorts exhibits the strongest inhibitory activity with an IC50 value of 0.08 mg/ml, overview
-
angiotensin I-converting enzyme inhibitory peptides
-
i.e. ACE-Is, from enzymatic hydrolysates of cuttlefish, Sepia officinalis, muscle proteins, generated by the crude enzyme from Bacillus mojavensis A21, show 87.11% inhibition at 2 mg/ml, mass spectrometric analysis, overview
-
angiotensin-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
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angiotensin-I converting enzyme inhibitory peptides
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activity of hydrolysates, using diverse proteases, from Avena sativa proteins by in silico and in vitro analyses, peptide sequencing, overview
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Asp-Asp-Thr-Gly-His-Asp-Phe-Glu-Asp-Thr-Gly-Glu-Ala-Met
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an inhibitory peptide from the marine rotifer, Brachionus rotundiformis
bradykinin potentiating peptide
i.e. BPP1 or pGlu-Trp-Pro-Arg-Pro-Gln-Ile-Pro-Pro
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bradykinin potentiating peptide b
interaction with sACE in a Zn-dependent manner
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Cl-
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kcat increases with increasing KCl concentrations, reaches a maximum at about 300 mM KCl, and the begins to decrease. At relatively low concentrations chloride anions activate the C-domain of the enzyme, but at high concentrations chloride inhibits the enzyme activity. Presence of at least two chloride-binding sites in the C-domain of bovine enzyme: binding of chloride to one of the sites causes activation of the enzyme, whereas chloride binding to the second site results in inhibition of the enzymatic activity
cyanidin-3-O-beta-D-glucoside
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isolated from flower buds of Rosa damascena. Metal ions might be involved in the inhibition
cyanidin-3-O-sambubioside
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an anthocyanin isolated from Hibiscus sabdariffa calyces, competitive ACE inhibition reducing blood pressure in humans, IC50 is 0.0684 mg/ml
delphinidin-3-O-sambubioside
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an anthocyanin isolated from Hibiscus sabdariffa calyces, competitive ACE inhibition reducing blood pressure in humans, IC50 is 0.0845 mg/ml
dexamethasone
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markedly inhibits the plasma extravasion in the tracheal mucosa produced by substance P. The simultanous inhibition of neutral endopeptidase and angiotensin converting enzyme completely reverses the effect of dexamethasone on substance P-induced extravasion
ESIINF
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the inhibitor produces an acute blood-pressure-lowering effect in spontaneously hypertensive rats upon a single oral administration
EtOAc extract of Rabdosia coetsa
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angiotensin-converting enzyme inhibitory activity
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flavanol
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flavanols either isolated or present in foods can inhibit enzyme activity
genistein
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0.003-0.3 mM genistein decreases the angiotensin-converting enzyme activity in blood plasma in a concentration-dependent manner; the isoflavone inhibits ACE in plasma and alters the vascular responses to angiotensin I and bradykinin, overview
gluco-aurantioobtusin
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competitive inhibitor, 137.62% inhibition at 1.63 ng/ml
GQGGP
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extraction and characterization of an ACE inhibitor from the fruiting body of Pholiota adiposa ASI 24012, which can be used as an antihypertensive drug
inhibitory peptides from rice dreg hydrolysate
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significant antihypertensive action and no other side effects by oral administration in spontaneous hypertension rats
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isoacteoside
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a phenylpropanoid glycoside isolated from ethanolic extracts of seeds of Plantago asiatica, collected from Jiang Xi Province in China. The compound shows ACE inhibitory activity in vitro, structure analysis by NMR, UV, IR and MS
KRQKYDI
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competitive inhibitor, the strongest inhibitor among reported troponin-originated peptides. The inhibhitor is slowly hydrolyzed by treatment with angiotensin I-converting enzyme. When KRQKYDI is administered orally to spontaneously hypertensive rats at a dose of 10 mg/kg, a temporary antihypertensive activity is observed at 3 and 6 h after administration
Leu-Ile-Tyr
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i.e. acein-2, isolated from tryptic hydrolysate of human plasma, non-competitive inhibitor, IC50: 0.00082 mM.
Lys-Ala-Phe-Arg
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ACE inhibitory peptide derived from Arachis hypogaea protein hydrolysate using digestion by Alcalase, mass spectrometric sequence determination, overview. IC50 value is 0.085 mg/ml
melanoidin
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melanoidins obtained from coffee (three roasting degrees), beer, and sweet-wine show in-vitro angiotensin-converting enzyme-inhibitory activity. The activity in coffee melanoidinsis significantly higher at more severe heating conditions
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MLN-4760
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conversion of Ang II to Ang(1-7) is blocked by MLN-4760 but not by DX600
Monascus-fermented soybean extract
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butanol, ethyl acetate, 50% ethanol-soluble extract and water-soluble extract
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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
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N-[(5S)-4-oxo-6-phenyl-5-[(phenylcarbonyl)amino]hexanoyl]-L-phenylalanine
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N-[(5S)-5-[(tert-butoxycarbonyl)amino]-4-oxo-6-phenylhexanoyl]-L-phenylalanine
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N-[(5S)-5-[(tert-butoxycarbonyl)amino]-4-oxo-6-phenylhexanoyl]-L-tryptophan
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N-[(S)-1-(ethoxycarbonyl)-3-phenylpropyl]-L-alanyl-L-proline
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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-[3-{[(1R)-1-{[(benzyloxy)carbonyl]amino}-2-phenylethyl](hydroxy)phosphoryl}-2-(biphenyl-4-ylmethyl)propanoyl]-L-tryptophan
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N-{(2R)-3-{[(1R)-1-{[(benzyloxy)carbonyl]amino}-2-phenylethyl](hydroxy)phosphoryl}-2-[(3-phenyl-1,2-oxazol-5-yl)methyl]propanoyl}-L-tyrosine
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N-{(2S)-3-{[(1R)-1-{[(benzyloxy)carbonyl]amino}-2-phenylethyl](hydroxy)phosphoryl}-2-[(3-phenyl-1,2-oxazol-5-yl)methyl]propanoyl}-L-tryptophan
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N2-[(S)-1-carboxy-3-phenylpropyl]-L-lysyl-L-proline
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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-[3,5-bis(trifluoromethyl)benzyl]-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-tyrosine
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peptide
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more angiotensin I converting enzyme-inhibitory peptides are present in hydrolyzed wet-milled corn germ compared to hydrolyzed dry-milled germ