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Information on EC 3.4.15.1 - peptidyl-dipeptidase A and Organism(s) Rattus norvegicus and UniProt Accession P47820
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3.4.15.1 peptidyl-dipeptidase ASpecify your search results
Word Map
- 3.4.15.1
- hypertension
-
blocker
- cardiovascular
- arterial
-
antihypertensive
- cardiac
-
renin-angiotensin
- ventricular
- myocardial
- captopril
-
systolic
-
diuretic
- coronary
- renin
-
aceis
- infarction
-
beta-blockers
- enalapril
- glomerular
-
diastolic
-
ejection
- proteinuria
- mellitus
-
placebo
- hypertrophy
- aldosterone
- nephropathy
- creatinine
-
hemodynamic
- bradykinin
-
congestive
- ras
-
vasodilator
-
normotensive
- statin
-
renin-angiotensin-aldosterone
- hg
- sarcoidosis
- losartan
- aspirin
-
prescript
-
double-blind
- angiotensinogen
-
renoprotective
-
pressor
- digoxin
-
all-cause
-
renovascular
-
microalbuminuria
-
hypotensive
- drug development
- veterinary medicine
- medicine
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ACE
angiotensin 1 converting enzyme
-
-
-
-
angiotensin converting enzyme
angiotensin I-converting enzyme
angiotensin-converting enzyme
carboxycathepsin
-
-
-
-
carboxypeptidase, dipeptidyl
-
-
-
-
CD143 antigen
-
-
-
-
DCP
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
-
-
-
-
ACE
-
-
-
-
ACE
-
-
angiotensin converting enzyme
-
-
-
-
angiotensin I-converting enzyme
-
-
-
-
angiotensin-converting enzyme
-
-
-
-
DCP
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9015-82-1
-
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
angiotensin I + H2O
angiotensin II + L-His-L-Leu
-
-
-
-
?
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
bradykinin + H2O
L-Phe-L-Arg + L-Ser-L-Pro + L-Arg-L-Pro-L-Pro-Gly-L-Phe
-
-
-
-
?
hippuryl-His-Leu + H2O
hippuric acid + His-Leu
-
-
81211, 81219, 81220, 81241, 81244, 81252, 81254, 81283, 667885, 680293, 681562, 707783, 710160, 731569, 732968
-
-
?
hippuryl-L-His-L-Leu + H2O
hippuric acid + L-His-L-Leu
-
-
-
-
?
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
?
physalaemin + H2O
pGlu-Ala-Asp-Pro-Asn-Lys-Phe-Tyr-Gly + Leu-Met-NH2
-
degraded by striatal and by lung enzyme
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
-
i.e. DRVYIHPFHL
i.e. DRVYIHPF
-
?
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)
-
?
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
?
-
-
potential role of follicular enzyme in early stages of follicular maturation and atresia
-
-
?
additional information
?
-
-
ACE degrades bradykinin, other vasoactive peptides, and activates angiotensin
-
-
?
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
angiotensin I + H2O
angiotensin II + His-Leu
-
i.e. DRVYIHPFHL
i.e. DRVYIHPF
-
?
angiotensin I + H2O
angiotensin II + L-His-L-Leu
-
-
-
-
?
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
-
-
-
-
?
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
?
-
-
potential role of follicular enzyme in early stages of follicular maturation and atresia
-
-
?
additional information
?
-
-
ACE degrades bradykinin, other vasoactive peptides, and activates angiotensin
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
NaCl
Zinc
-
0.3 mM ZnCl2 completely reverses the inhibition caused by 0.1 mM EDTA
NaCl
-
stimulates hydrolysis of hippuryl-His-Leu in concentration-dependent manner between 0 and 300 mM
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
SPB1
Bacillus subtilis crude lipopeptide biosurfactant, the biosurfactant displays a potent inhibition of ACE activity in vitro, IC50 is 1.37 mg/ml
-
15B2
-
an inhibitor isolated from the culture broth of Actinomadura sp. No. 937ZE-1
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
-
D-mannitol
-
antihypertensive effect in spontaneously hypertensive rats by oral administration
dexamethasone
-
markedly inhibits the plasma extravasion in the tracheal mucosa produced by substance P. The simultanous inhibition of neutral endopeptidase and angiotensin converting enzyme completely reverses the effect of dexamethasone on substance P-induced extravasion
enalaprilat
-
inhibits ACE and the bradykinin degradation in vivo, which is reversed by insulin
ESIINF
-
the inhibitor produces an acute blood-pressure-lowering effect in spontaneously hypertensive rats upon a single oral administration
Gly-L-Ala-Hyp-Gly-L-Pro-L-Ala-Gly-L-Pro-Gly-Gly-L-Ile-Hyp-Gly-L-Glu-L-Arg-Gly
-
-
Gly-Phe-Hyp-Gly-Thr-Hyp-Gly-Leu-Hyp-Gly-Phe
-
inhibitory peptide derived from chicken breast muscle possesses hypotensive activity for spontaneously hypertensive rats
inhibitory peptides from rice dreg hydrolysate
-
significant antihypertensive action and no other side effects by oral administration in spontaneous hypertension rats
-
KRQKYDI
-
competitive inhibitor, the strongest inhibitor among reported troponin-originated peptides. The inhibhitor is slowly hydrolyzed by treatment with angiotensin I-converting enzyme. When KRQKYDI is administered orally to spontaneously hypertensive rats at a dose of 10 mg/kg, a temporary antihypertensive activity is observed at 3 and 6 h after administration
L-681,176
-
purification of the inhibitor found in the culture filtrate of Streptomyces sp. MA 5143
NaCl
-
concentration dependent inhibition of hippuryl-His-Leu between 0 and 100 mM
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
-
quercetin 3-O-alpha-(6''-p-coumaroylglucosyl-beta -1,2-rhamnoside)
-
IC50: 0.351 mM
quercetin-3-O-alpha-(6''-caffeoylglucosyl-beta-1,2-rhamnoside)
-
IC50: 0.1589 mM
sardine peptide
-
a protein hydrolysate derived from muscles of sardines, inhibits in vivo and reduces the blood glucose level, but not the plasma insulin level
-
trandolapril
-
the angiotensin-converting enzyme inhibitor has no significant effect on apoptosis induced via endotoxic shock with Escherichia coli lipopolysaccharides
Trp-Pro-Glu-Ala-Ala-Glu-Leu-Met-Met-Glu-Val-Asp-Pro
-
noncompetitive inhibitor.The peptide has an antihypertensive effect according to the time-course measurement after oral administration to spontaneously hypertensive rats. Maximal reduction is detected 3 h after oral administration at a dose of 10 mg/kg of body weight
Val-Lys-Lys-Val-Leu-Gly-Asn-Pro
-
the angiotensin-I converting enzyme inhibitory peptide derived from porcine skeletal muscle myosin is a noncompetitive inhibitor that is slowly hydrolyzed by angiotensin-I converting enzyme. At the dose of 10 mg/kg, this peptide shows antihypertensive activity after a maximum of 3 h of administration
YRGGLEPINF
-
the inhibitor produces an acute blood-pressure-lowering effect in spontaneously hypertensive rats upon a single oral administration
captopril
-
-
captopril
-
lipophilic ACE inhibitors quinapril, enalapril, and captopril increase the survival and lifetime of rats with experimental chronic heart failure
captopril
-
the anngiotensin converting enzyme inhibitor captopril modifies conditioned place preference induced by morphine and morphine withdrawal signs in rats
captopril
-
ACE inhibition during pregnancy and lactation in adult offspring rats induces behavioural changes, e.g. in the open field test, overview
captopril
-
inhibits in vivo and reduces the blood glucose level, but not the plasma insulin level
enalapril
-
acute angiotensin-converting enzyme inhibition evokes bradykinin-induced sympathetic activation in diabetic rats
enalapril
-
lipophilic ACE inhibitors quinapril, enalapril, and captopril increase the survival and lifetime of rats with experimental chronic heart failure
enalapril
-
reduces the liver tissue transforming growth factor beta-1 and has an ameliorating effect on the fibrosis markers transforming growth factor beta-1 and matrix metalloproteinase-2. Enalapril does not affect the process of liver fibrosis at all (induced in rats by bile-duct ligation)
enalapril
-
the angiotensin-converting enzyme inhibitor has no significant effect on apoptosis induced via endotoxic shock with Escherichia coli lipopolysaccharides
genistein
-
0.003-0.3 mM genistein decreases the angiotensin-converting enzyme activity in blood plasma in a concentration-dependent manner
genistein
-
the isoflavone inhibits ACE in plasma and alters the vascular responses to angiotensin I and bradykinin, overview
lisinopril
-
angiotensin-converting enzyme inhibitor enhances the liver regeneration in rats after partial hepatectomy. Angiotensin-converting enzyme enhanced the hepatic regenerative response to PH by two independent mechanisms: an activation of B2 receptors and inhibition of angiotensin II production, both of which may stimulate production of hepatocyte growth factor, resulting in enhancement of the hepatic regeneration
lisinopril
-
therapeutic resistance to angiotensin converting enzyme inhibition is related to a difference in the combination of renal pharmacodynamic and pharmacokinetic characteristics in non-responders, primarily consisting of increased renal expression of angiotensin converting enzyme and higher angiotensin converting enzyme inhibitor clearance
lisinopril
-
treatment with 75 mg/l lisinopril significantly reduces renal ACE activity without affecting renal ACE2 activity
N-[(1S)-1-(ethoxycarbonyl)-3-phenylpropyl]-L-alanyl-L-proline
-
accelerated nitrotyrosine content in the renal cortex during high-glucose conditions is prevented by treatment with the angiotensin-converting enzyme inhibitor treatment. The suppressed degradation of nitrotyrosine in the renal cortex by the angiotensin-converting enzyme inhibitor enhances both superoxide anion degradation per se and antioxidative effects including activation of superoxide dismutase
N-[(1S)-1-(ethoxycarbonyl)-3-phenylpropyl]-L-alanyl-L-proline
-
independent of diet enalapril treatment decreases food intake, energetic gain and body weight in normotensive young rats, followed by reduced body fat mass and serum leptin
nicotianamine
-
mixed inhibition. The preferential inhibition of circulating and tissue angiotensin I-converting enzyme by nicotianamine can contribute to the suppression of hypertension
perindopril
-
chronic administration of perindopril results in a decrease in body adiposity
perindopril
-
chronic in vivo administration of the angiotensin-converting enzyme inhibitor reduces apoptosis induced via endotoxic shock with Escherichia coli lipopolysaccharides
perindopril
-
in growing spontaneously hypertensive rats, chronic treatment with perindopril enhances untrained exercise capacity, while it does no affect acquired exercise capacity as a result of exercise training. Perindopril promotes adaptive changes of skeletal muscle in response to exercise such as increases in capillary density and percentage of type I fibre
perindopril
-
decreases food intake and circulating insulin in both diet groups, and hepatic ACE activity in high fat fed animals only, while decreased plasma leptin concentration with ACE inhibition is only evident in chow fed animals
quinapril
-
lipophilic ACE inhibitors quinapril, enalapril, and captopril increase the survival and lifetime of rats with experimental chronic heart failure
quinapril
-
the angiotensin-converting enzyme inhibitor has no significant effect on apoptosis induced via endotoxic shock with Escherichia coli lipopolysaccharides
quinapril
-
18 mg/kg quinapril per day feeding for 3 days significantly reduces blood plasma ACE activity by 80%, quinapril administration for 16 days greatly decreases blood plasma ACE activity by 88% with 18 mg/kg per day, ACE activities in the heart, lung, and skeletal muscles of the 16-day ACE-inhibition with 18 mg/kg per day are 9%, 16%, and 22% of the controls, respectively
ramipril
-
in the early phase of diabetes, the angiotensin-converting enzyme inhibitor reverses glomerular overexpression and activation of some critical growth factor pathways and increases protection against oxidative stress. These effects involve B2-kinin receptor activation
ramipril
-
the angiotensin-converting enzyme inhibitor has no significant effect on apoptosis induced via endotoxic shock with Escherichia coli lipopolysaccharides
additional information
effects of metabolites produced from (-)-epigallocatechin gallate by rat intestinal bacteria on angiotensin I-converting enzyme activity and blood pressure in spontaneously hypertensive rats. All of the metabolites show ACE inhibitory activities and the order of IC50 is hydroxyphenyl valeric acids > 5-(3,4,5-trihydroxyphenyl)-gamma-valerolactone > 5-(3,4,5-trihydroxyphenyl) 4-hydroxyvaleric acid >> 5-(3,5-dihydroxyphenyl) 4-hydroxyvaleric acid >> 5-(3,5-dihydroxyphenyl)-gamma-valerolactone. Among the catechins, galloylated catechins exhibit stronger ACE inhibitory activity than nongalloylated catechins. Measurement of systolic blood pressure (SBP) after oral administration
-
additional information
-
endogenous inhibitor from rat heart may modulate the activity of the enzyme in the heart in response to alterations of the oxidation-reduction balance in the tissue, MW of the inhibitor is about 100000 Da
-
additional information
-
design and properties of N-carboxyalkyldipeptide inhibitors
-
additional information
-
the presence of verticione, verticine, peimisine may be responsible, at least in part, for the antihypertensive action of the bulbs of Fritillaria ussuriensis
-
additional information
-
hot water extract of Tamogi-take mushroom, antihypertensive effect in spontaneously hypertensive rats by oral administration
-
additional information
-
isolation of angiotensin converting enzyme (ACE) inhibitory flavonoids from Sedum sarmentosum
-
additional information
-
angiotensin I-converting enzyme inhibitory peptides from protein hydrolysates by a soybean protease D3
-
additional information
-
tissue angiotensin converting enzyme inhibitors exert more pronounced antithrombotic effect than plasma ACE-Is in experimental thrombosis
-
additional information
-
chicken collagen hydrolysates possess ACE-inhibitory activities, chicken collagen hydrolysates inhibit about 30% of the activity of ACE, whereas further enzymatic treatment doubles their activities
-
additional information
-
not inhibited by MLN4760, SCH39370, amastatin bestatin, chymostatin, and p-chloromercuribenzoate
-
additional information
-
2.7fold peptide-enriched soy sauce-like seasoning, termed Fermented Soybean Seasoning, FSS, shows ACE inhibitory activity with an IC50 of 0.454 mg/ml, fermentation method, overview. FSS shows antihypertensive effects, overview
-
additional information
-
ACE inhibitory peptides derived from marine organisms show a strong suppressive effect on systolic blood pressure of spontaneously hypertensive rats, and this antihypertensive activity is similar with captopril, a commercial antihypertensive drug. Hydrophobicity of the N-terminus is one of the common features of ACE inhibitory peptides, and may contribute to the inhibitory activity. No side effect observed on rats after administration of antihypertensive peptides. The peptides exhibit antihypertensive activity in vivo rather than in vitro. An antihypertensive peptide isolated from bonito fish hydrolysate product, is hydrolyzed by ACE to produce a smaller peptide than the initial one, which has 8fold increased ACE inhibitory activity compared with the initial peptide. Polyphenolic compounds inhibit ACE activity through sequestration of the enzyme metal factor, Zn2+ ion
-
additional information
-
metabolic effects of low dose angiotensin converting enzyme inhibitor in dietary obesity in the rat
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Cl-
-
activation, optimal NaCl concentration for the brain enzyme in hydrolysis of LVVYPWTQRY is 10 mM, optimal concentration for hydrolysis of angiotensin I is 200 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.351
quercetin 3-O-alpha-(6''-p-coumaroylglucosyl-beta -1,2-rhamnoside)
Rattus norvegicus
-
IC50: 0.351 mM
0.1589
quercetin-3-O-alpha-(6''-caffeoylglucosyl-beta-1,2-rhamnoside)
Rattus norvegicus
-
IC50: 0.1589 mM
additional information
additional information
Rattus norvegicus
-
IC50 values of nicotianamine, Val-Gly, Gly-Tyr, Ser-Tyr, Ala-Tyr, Ala-Ile, Val-Pro, Ala-Phe, Gly-Trp, and Ala-Trp are 0.442 mg/ml, 0.172 mg/ml, 0.132 mg/ml, 0.132 mg/ml, 0.132 mg/ml, 0.132 mg/ml, 0.172 mg/ml, 0.224 mg/ml, 0.199 mg/ml, and 0.199 mg/ml
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
during high-salt diets, activity of angiotensin-converting enzyme in the aorta progressively decreases to the minimal during week 1 and remains lower than control level for 1 month
additional information
-
rats exposed to a high-sodium diet show an enhanced ACE activity
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 9.5
-
pH 5.5: 55% of maximal acticity, pH 50°C: about 50% of maximal activity, enzyme from brain, hydrolysis of LVVYPWTQRY
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
wild-type Wistar and spontaneously hypertensive rats (SHR) derived thereof
Uniprot
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
-
-
follicular granulosa cells, corpora lutea, germinal epithelium, ovarian blood vessels, high levels of activity on the surface of granulosa cells
-
from aorta, extracellular ACE binds to smooth muscle cells, overview
additional information
-
the direct antioxidative and anti-inflammatory effects of peroxisome proliferator-activated receptors ligands are associated with the inhibition of angiotensin converting enzyme expression in streptozotocin-induced diabetic rat aorta
-
heart membrane, ACE activity is significantly higher in hearts of young Zucker rats than in those of Sprague-Dawley rats
-
ACE mRNA in the kidney is significantoly higher in the exercise rats than in the control rats
-
angiotensin-converting enzyme inhibitor enhances the liver regeneration in rats after partial hepatectomy
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
transcriptional regulation by exogenous ACE may involve its nuclear localization, nuclear localization of ACE is impaired by selective inhibitors of endocytosis
additional information
-
subcellular localization study, selective nuclear localization of ACE in smooth muscle cells and umbilical vein cells, HUVEC, may require the expression of specific protein receptors in these cells, overview. Mechanism of ACE endocytosis, overview
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
binding of captopril to angiotensin I-converting enzyme triggers activation of signaling pathways via JNK and ERK1/2 phosphorylation. Captopril leads to gene modulation trough binding to ACE causing a decrease of COX2 expression and an increase of AP2 expression. ACE interacts with beta-arrestin1, and this interaction seems to increase under captopril stimulation in CHO-ACE cells
malfunction
physiological function
additional information
malfunction
inhibition of ACE leads to amelioration of endothelial function, vascular remodeling, and reduction in atherosclerosis progression
malfunction
protective and the curative effects of Bacillus subtilis SPB1 crude lipopeptide biosurfactant in alleviating induced obesity complications in rats fed on high-fat-high-fructose diet (HFFD) via inhibition of ACE activity. Administration of SPB1 biosurfactant reduced significantly (34%) the peak of blood glucose concentration 60 min after glucose administration, as compared with untreated rats fed on HFFD. SPB1 lipopeptides treatments improves some of serum electrolytes such as Na+, K+, Ca2+, and Mg2+
malfunction
-
effect of chronic pre-treatment with angiotensin converting enzyme inhibition on skeletal muscle mitochondrial recovery after ischemia/reperfusion. Chronic ACE inhibition reduced blood pressure and might reduce ischemia-induced mitochondrial respiratory chain dysfunction in the frequent setting of hindlimb ischemia-reperfusion, overview
malfunction
-
ACE2 gene transfer to the rostral ventrolateral medulla in spontaneously hypertensive rats attenuates the increased tonically active glutamatergic inputs to the rostral ventrolateral medulla in spontaneously hypertensive rats
physiological function
-
ACE catalyzes the extracellular formation of angiotensin II, and degradation of bradykinin, thus regulating blood pressure and renal handling of electrolytes. ACE added to smooth muscle cells resultes in transcriptional stimulation of the genes of bradykinin receptors B1 and B2. ACE enhances the activation of platelet-derived growth factor receptor beta signaling pathway
physiological function
-
peptidases angiotensin-converting enzyme, together with neutral endopeptidase 24.11, mediates most of the kinin catabolism in normal cardiac tissue
additional information
-
ACE inhibition during pregnancy and lactation in adult offspring rats induces behavioural changes, e.g. in the open field test, overview
additional information
-
metabolic effects of low dose angiotensin converting enzyme inhibitor in dietary obesity in the rat
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ACE_RAT
1313
1
150908
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
ACE contains transactivation domains in its sequence
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
side-chain modification
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55
-
lung enzyme looses 50% of the activity after 1.5 min, testicular enzyme looses 50% loss of activity
additional information
-
chelators and Co2+ markedly potentiate the thermal denaturation
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
zinc may contribute to the structural integrity and thermal stability of angiotensin-converting enzyme in each tissue
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
stable recombinant expression of ACE in CHO cells and quantitative real-time RT-PCR expression analysis
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
alpha-linolenic acid downregulates ACE expression in the aorta of spontaneously hypertensive rats, but not in other organs, via feeding of 10% alpha-linolenic acid-rich flaxseed oil, control is feeding of high oleic safflower oil
ACE activity is significantly decreased in heart membranes 4-8 weeks post-streptozotocin injection
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
hypertension is a global health problem, and angiotensin I (ANG I)-converting enzyme (ACE) inhibitors are largely used to control this pathology
drug development
-
ACE is the molecular targets of inhibitory drugs that favorably influence diabetic complications
medicine
medicine
-
genistein has a potentially preventive role against cardiovascular diseases. Genistein inhibits the expression of angiotensin-converting enzyme via estrogen receptor and subsequently ERK1/2 signaling pathway in rat aortic endothelial cells. Down-regulation of the angiotensin-convering enzyme with a consequent change in circulating levels of angiotensin II, vasorelaxant angiotensin(1-7) and bradykinin plays an important role in cardiovascular effects of genistein through the ERK1/2 pathway
medicine
-
angiotensin-converting enzyme inhibition (lisinopril) and AT1 receptor blockade reduce the tubular damage and apoptosis in the contralateral testes after unilateral testicular torsion. The beneficial effect of these drugs may arise from inhibition of ischemic process resulting from increased sympathetic activity and elimination of insults subsequent to dysregulation of the renin-angiotensin system
medicine
-
antihypertensive effect of angiotensin I-converting enzyme inhibitory peptides from a sesame protein hydrolysate in spontaneously hypertensive rats. Sesam peptide powder would be a beneficial ingredient for preventing and providing therapy against hypertension and its related diseases
medicine
-
chronic inhibition of angiotensin II synthesis from birth specifically reduces the development of adiposity in the rat
medicine
-
combination therapy with an angiotensin-converting enzyme inhibitor and beta-adrenoceptor blocker without intrinsic sympathomimetic activity should be used in the therapy of chronic heart failure
medicine
-
in the early phase of diabetes, the angiotensin-converting enzyme inhibitorramipril reverses glomerular overexpression and activation of some critical growth factor pathways and increases protection against oxidative stress. These effects involve B2-kinin receptor activation
medicine
-
modulation of the renin-angiotensin system by enalapril is important for body weight regulation and can be of beneficial effect in the treatment of obesity and related diseases
medicine
-
peptide derived from tuna dark muscle would be a beneficial ingredient for functional food or pharmaceuticals against hypertension and its related diseases
medicine
-
ACE inhibition is a therapeutic target in treating peripheral occlusive arterial disease
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Patchett, A.A.; Cordes, E.H.
The design and properties of N-carboxyalkyldipeptide inhibitors of angiotensin-converting enzyme
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Bos taurus, Canis lupus familiaris, Oryctolagus cuniculus, Homo sapiens, Mammalia, Rattus norvegicus, Sus scrofa
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Enzymes of the renin-angiotensin system and their inhibitors
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Bos taurus, Canis lupus familiaris, Cavia porcellus, Oryctolagus cuniculus, Equus caballus, Homo sapiens, Papio anubis, Rattus norvegicus, Sus scrofa
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Pharmacological properties of the converting enzyme inhibitor, enalapril maleate (MK-421)
Fed. Proc.
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Canis lupus familiaris, Rattus norvegicus, Sus scrofa
Huang, L.; Rowin, G.; Dunn, J.; Sykes, R.; Dobna, R.; Mayles, B.A.; Gross, D.M.; Burg, R.W.
Discovery, purification and characterization of the angiotensin converting enzyme inhibitor, L-681,176, produced by Streptomyces sp. MA 5143a
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Rattus norvegicus
Kido, Y.; Hamakado, T.; Anno, M.; Miyagawa, E.; Motoki, Y.
Isolation and characterization of I5B2, a new phosphorus containing inhibitor of angiotensin I converting enzyme produced by Actinomadura sp
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37
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Rattus norvegicus
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Endogenous inhibitor of angiotensin converting enzyme in the rat heart
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159
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Oryctolagus cuniculus, Rattus norvegicus
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Peptidyl dipeptidase A: angiotensin I-converting enzyme
Methods Enzymol.
248
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1995
Homo sapiens, Mammalia, Mus musculus, Rattus norvegicus
Piedimonte, G.; McDonald, D.M.; Nadel, J.A.
Neutral endopeptidase and kininase II mediate glucocorticoid inhibition of neurogenic inflammation in the rat trachea
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88
40-44
1991
Rattus norvegicus
Yoshida, T.; Nosaka, S.
Some characteristics of a peptidyl dipeptidase (kininase II) from rat CSF: differential effects of NaCl on the sequential degradation steps of bradykinin
J. Neurochem.
55
1861-1869
1990
Rattus norvegicus
Yokosawa, H.; Endo, S.; Ohgaki, Y.; Maeyama, J.; Ishii, S.
Hydrolysis of substance P and its analogs by angiotensin-converting enzyme from rat lung. Characterization of endopeptidase activity of the enzyme
J. Biochem.
98
1293-1299
1985
Rattus norvegicus
Strittmatter, S.M.; Thiele, E.A.; Kapiloff, M.S.; Snyder, S.H.
A rat brain isozyme of angiotensin-converting enzyme. Unique specificity for amidated peptide substrates
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260
9825-9832
1985
Rattus norvegicus
Ward, P.E.; Sheridan, M.A.
Angiotensin I converting enzyme of rat intestinal and vascular surface membrane
Biochim. Biophys. Acta
716
208-216
1982
Rattus norvegicus
Velletri, P.A.; Billingsley, M.L.; Lovenberg, W.
Thermal denaturation of rat pulmonary and testicular angiotensin-converting enzyme isozymes. Effects of chelators and CoCl2
Biochim. Biophys. Acta
839
71-82
1985
Rattus norvegicus
Lanzillo, J.J.; Fanburg, B.L.
Low molecular weight angiotensin I converting enzyme from rat lung
Biochim. Biophys. Acta
491
339-344
1977
Rattus norvegicus
Daud, A.I.; Bumpus, F.M.; Husain, A.
Characterization of angiotensin I-converting enzyme (ACE)-containing follicles in the rat ovary during the estrous cycle and effects of ACE inhibitor on ovulation
Endocrinology
126
2927-2934
1990
Rattus norvegicus
Kalinina, E.V.; Posdnev, V.F.; Komissarova, N.V.; Gomazkov, O.A.
Effect of new peptide inhibitors on the ratio of angiotensin I-converting and kinin-degrading activities of dipeptidyl carboxypeptidase (angiotensin-converting enzyme)
Biochemistry
62
247-250
1997
Rattus norvegicus
Hayakari, M.; Satoh, K.; Izumi, H.; Kudoh, T.; Asano, J.; Yamazaki, T.; Tsuchida, S.
Kinetic-controlled hydrolysis of Leu-Val-Val-hemorphin-7 catalyzed by angiotensin-converting enzyme from rat brain
Peptides
24
1075-1082
2003
Rattus norvegicus
Oh, H.; Kang, D.G.; Lee, S.; Lee, Y.; Lee, H.S.
Angiotensin converting enzyme (ACE) inhibitory alkaloids from Fritillaria ussuriensis
Planta Med.
69
564-565
2003
Rattus norvegicus
Maeda, S.; Iemitsu, M.; Jesmin, S.; Miyauchi, T.
Acute exercise causes an enhancement of tissue renin-angiotensin system in the kidney in rats
Acta Physiol. Scand.
185
79-86
2005
Rattus norvegicus
Oh, H.; Kang, D.G.; Kwon, J.W.; Kwon, T.O.; Lee, S.Y.; Lee, D.B.; Lee, H.S.
Isolation of angiotensin converting enzyme (ACE) inhibitory flavonoids from Sedum sarmentosum
Biol. Pharm. Bull.
27
2035-2037
2004
Rattus norvegicus
Hagiwara, S.Y.; Takahashi, M.; Shen, Y.; Kaihou, S.; Tomiyama, T.; Yazawa, M.; Tamai, Y.; Sin, Y.; Kazusaka, A.; Terazawa, M.
A phytochemical in the edible Tamogi-take mushroom (Pleurotus cornucopiae), D-mannitol, inhibits ACE activity and lowers the blood pressure of spontaneously hypertensive rats
Biosci. Biotechnol. Biochem.
69
1603-1605
2005
Bos taurus, Rattus norvegicus
Saiga, A.; Okumura, T.; Makihara, T.; Katsuda, S.; Morimatsu, F.; Nishimura, T.
Action mechanism of an angiotensin I-converting enzyme inhibitory peptide derived from chicken breast muscle
J. Agric. Food Chem.
54
942-945
2006
Oryctolagus cuniculus, Rattus norvegicus
Xu, Y.Y.; Yang, C.; Li, S.N.
Effects of genistein on angiotensin-converting enzyme in rats
Life Sci.
79
828-837
2006
Rattus norvegicus
Augustyniak, R.A.; Maliszewska-Scislo, M.; Chen, H.; Fallucca, J.; Rossi, N.F.
Acute angiotensin-converting enzyme inhibition evokes bradykinin-induced sympathetic activation in diabetic rats
Am. J. Physiol. Regul. Integr. Comp. Physiol.
293
R2260-R2266
2007
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
Allard, J.; Buleon, M.; Cellier, E.; Renaud, I.; Pecher, C.; Praddaude, F.; Conti, M.; Tack, I.; Girolami, J.P.
ACE inhibitor reduces growth factor receptor expression and signaling but also albuminuria through B2-kinin glomerular receptor activation in diabetic rats
Am. J. Physiol. Renal Physiol.
293
F1083-F1092
2007
Rattus norvegicus
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
Chen, Q.; Xuan, G.; Fu, M.; He, G.; Wang, W.; Zhang, H.; Ruan, H.
Effect of angiotensin I-converting enzyme inhibitory peptide from rice dregs protein on antihypertensive activity in spontaneously hypertensive rats
Asia Pac. J. Clin. Nutr.
16 Suppl 1
281-285
2007
Rattus norvegicus
Yayama, K.; Sugiyama, K.; Miyagi, R.; Okamoto, H.
Angiotensin-converting enzyme inhibitor enhances liver regeneration following partial hepatectomy: involvement of bradykinin B2 and angiotensin AT1 receptors
Biol. Pharm. Bull.
30
591-594
2007
Rattus norvegicus
Nakano, D.; Ogura, K.; Miyakoshi, M.; Ishii, F.; Kawanishi, H.; Kurumazuka, D.; Kwak, C.J.; Ikemura, K.; Takaoka, M.; Moriguchi, S.; Iino, T.; Kusumoto, A.; Asami, S.; Shibata, H.; Kiso, Y.; Matsumura, Y.
Antihypertensive effect of angiotensin I-converting enzyme inhibitory peptides from a sesame protein hydrolysate in spontaneously hypertensive rats
Biosci. Biotechnol. Biochem.
70
1118-1126
2006
Rattus norvegicus
Fedorov, V.N.; Salnikov, E.V.; Sidorov, A.V.; Bogatushin, A.V.; Fateev, M.M.
Survival of rats with experimental chronic heart failure depending on pharmacodynamic and pharmacokinetic parameters of angiotensin-converting enzyme inhibitors and beta-adrenoceptor blockers
Bull. Exp. Biol. Med.
141
40-43
2006
Rattus norvegicus
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
Ishii, N.; Ikenaga, H.; Carmines, P.K.; Takada, N.; Okazaki, T.; Nagai, T.; Maeda, T.; Aoki, Y.; Saruta, T.; Katagiri, M.
Impact of angiotensin-converting enzyme inhibition on renal cortical nitrotyrosine content during increased extracellular glucose concentration
Clin. Biochem.
39
633-639
2006
Rattus norvegicus
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
Tuerkay, C.; Yoenem, O.; Arici, S.; Koyuncu, A.; Kanbay, M.
Effect of angiotensin-converting enzyme inhibition on experimental hepatic fibrogenesis
Digest. Dis. Sci.
53
789-793
2008
Rattus norvegicus
Toba, H.; Miki, S.; Shimizu, T.; Yoshimura, A.; Inoue, R.; Sawai, N.; Tsukamoto, R.; Murakami, M.; Morita, Y.; Nakayama, Y.; Kobara, M.; Nakata, T.
The direct antioxidative and anti-inflammatory effects of peroxisome proliferator-activated receptors ligands are associated with the inhibition of angiotensin converting enzyme expression in streptozotocin-induced diabetic rat aorta
Eur. J. Pharmacol.
549
124-132
2006
Rattus norvegicus
Takai, S.; Yamamoto, D.; Jin, D.; Inagaki, S.; Yoshikawa, K.; Tanaka, K.; Miyazaki, M.
Inhibition of matrix metalloproteinase-9 activity by lisinopril after myocardial infarction in hamsters
Eur. J. Pharmacol.
568
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2007
Rattus norvegicus
Windt, W.A.; van Dokkum, R.P.; Kluppel, C.A.; Jeronimus-Stratingh, C.M.; Hut, F.; de Zeeuw, D.; Henning, R.H.
Therapeutic resistance to angiotensin converting enzyme (ACE) inhibition is related to pharmacodynamic and -kinetic factors in 5/6 nephrectomized rats
Eur. J. Pharmacol.
580
231-240
2008
Rattus norvegicus
Santos, E.L.; de Picoli Souza, K.; Guimaraes, P.B.; Reis, F.C.; Silva, S.M.; Costa-Neto, C.M.; Luz, J.; Pesquero, J.B.
Effect of angiotensin converting enzyme inhibitor enalapril on body weight and composition in young rats
Int. Immunopharmacol.
8
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2008
Rattus norvegicus
Gokce, G.; Karboga, H.; Yildiz, E.; Ayan, S.; Gultekin, Y.
Effect of angiotensin-converting enzyme inhibition and angiotensin II type 1 receptor blockade on apoptotic changes in contralateral testis following unilateral testicular torsion
Int. Urol. Nephrol.
40
989-995
2008
Rattus norvegicus
Miguel, M.; Manso, M.; Aleixandre, A.; Alonso, M.J.; Salaices, M.; Lopez-Fandino, R.
Vascular effects, angiotensin I-converting enzyme (ACE)-inhibitory activity, and antihypertensive properties of peptides derived from egg white
J. Agric. Food Chem.
55
10615-10621
2007
Rattus norvegicus
Qian, Z.J.; Je, J.Y.; Kim, S.K.
Antihypertensive effect of angiotensin i converting enzyme-inhibitory peptide from hydrolysates of Bigeye tuna dark muscle, Thunnus obesus
J. Agric. Food Chem.
55
8398-8403
2007
Oryctolagus cuniculus, Rattus norvegicus
Katayama, K.; Anggraeni, H.E.; Mori, T.; Ahhmed, A.M.; Kawahara, S.; Sugiyama, M.; Nakayama, T.; Maruyama, M.; Muguruma, M.
Porcine skeletal muscle troponin is a good source of peptides with Angiotensin-I converting enzyme inhibitory activity and antihypertensive effects in spontaneously hypertensive rats
J. Agric. Food Chem.
56
355-360
2008
Rattus norvegicus
Kodera, T.; Nio, N.
Identification of an angiotensin I-converting enzyme inhibitory peptides from protein hydrolysates by a soybean protease and the antihypertensive effects of hydrolysates in spontaneously hypertensive model rats
J. Food Sci.
71
C164-C173
2006
Rattus norvegicus
Katayama, K.; Katayama, K.; Mori, T.; Kawahara, S.; Miake, K.; Kodama, Y.; Sugiyama, M.; Kawamura, Y.; Nakayama, T.; Maruyama, M.; Muguruma, M.
Angiotensin-I converting enzyme inhibitory peptide derived from porcine skeletal muscle myosin and its antihypertensive activity in spontaneously hypertensive rats
J. Food Sci.
72
S702-S706
2007
Rattus norvegicus
Minami, N.; Li, Y.; Guo, Q.; Kawamura, T.; Mori, N.; Nagasaka, M.; Ogawa, M.; Ito, O.; Kurosawa, H.; Kanazawa, M.; Kohzuki, M.
Effects of angiotensin-converting enzyme inhibitor and exercise training on exercise capacity and skeletal muscle
J. Hypertens.
25
1241-1248
2007
Rattus norvegicus
Hayashi, A.; Kimoto, K.
Nicotianamine preferentially inhibits angiotensin I-converting enzyme
J. Nutr. Sci. Vitaminol.
53
331-336
2007
Oryctolagus cuniculus, Rattus norvegicus
Alaei, H.; Hosseini, M.
Angiotensin converting enzyme inhibitor captopril modifies conditioned place preference induced by morphine and morphine withdrawal signs in rats
Pathophysiology
14
55-60
2007
Rattus norvegicus
Weisinger, H.S.; Begg, D.P.; Egan, G.F.; Jayasooriya, A.P.; Lie, F.; Mathai, M.L.; Sinclair, A.J.; Wark, J.D.; Weisinger, R.S.
Angiotensin converting enzyme inhibition from birth reduces body weight and body fat in Sprague-Dawley rats
Physiol. Behav.
93
820-825
2008
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
Ren, J.; Li, H.; Prior, B.M.; Yang, H.T.
Angiotensin converting enzyme inhibition enhances collateral artery remodeling in rats with femoral artery occlusion
Am. J. Med. Sci.
335
177-187
2008
Rattus norvegicus
Diaz-Sylvester, P.L.; Fiori, M.C.; Dieguez, S.M.; Mueller, A.C.; Lopardo, M.L.; Amorena, C.E.
Effect of chronic inhibition of converting enzyme on proximal tubule acidification
Am. J. Physiol. Regul. Integr. Comp. Physiol.
294
R2014-R2020
2008
Rattus norvegicus
Montenegro, M.F.; Pessa, L.R.; Tanus-Santos, J.E.
Isoflavone genistein inhibits the angiotensin-converting enzyme and alters the vascular responses to angiotensin I and bradykinin
Eur. J. Pharmacol.
607
173-177
2009
Rattus norvegicus
Hamming, I.; van Goor, H.; Turner, A.J.; Rushworth, C.A.; Michaud, A.A.; Corvol, P.; Navis, G.
Differential regulation of renal angiotensin-converting enzyme (ACE) and ACE2 during ACE inhibition and dietary sodium restriction in healthy rats
Exp. Physiol.
93
631-638
2008
Rattus norvegicus
Diz, D.I.; Garcia-Espinosa, M.A.; Gegick, S.; Tommasi, E.N.; Ferrario, C.M.; Ann Tallant, E.; Chappell, M.C.; Gallagher, P.E.
Injections of angiotensin-converting enzyme 2 inhibitor MLN4760 into nucleus tractus solitarii reduce baroreceptor reflex sensitivity for heart rate control in rats
Exp. Physiol.
93
694-700
2008
Rattus norvegicus
Saiga, A.; Iwai, K.; Hayakawa, T.; Takahata, Y.; Kitamura, S.; Nishimura, T.; Morimatsu, F.
Angiotensin I-converting enzyme-inhibitory peptides obtained from chicken collagen hydrolysate
J. Agric. Food Chem.
56
9586-9591
2008
Oryctolagus cuniculus, Rattus norvegicus
Kim, M.Y.; Baik, S.K.; Park, D.H.; Jang, Y.O.; Suk, K.T.; Yea, C.J.; Lee, I.Y.; Kim, J.W.; Kim, H.S.; Kwon, S.O.; Cho, M.Y.; Ko, S.B.; Chang, S.J.; Um, S.H.; Han, K.H.
Angiotensin receptor blockers are superior to angiotensin-converting enzyme inhibitors in the suppression of hepatic fibrosis in a bile duct-ligated rat model
J. Gastroenterol.
43
889-896
2008
Rattus norvegicus
Richardson, M.A.; Gupta, A.; OBrien, L.A.; Berg, D.T.; Gerlitz, B.; Syed, S.; Sharma, G.R.; Cramer, M.S.; Heuer, J.G.; Galbreath, E.J.; Grinnell, B.W.
Treatment of sepsis-induced acquired protein C deficiency reverses angiotensin-converting enzyme-2 inhibition and decreases pulmonary inflammatory response
J. Pharmacol. Exp. Ther.
325
17-26
2008
Rattus norvegicus
Olszanecki, R.; Bujak-Gizycka, B.; Madej, J.; Suski, M.; Wolkow, P.P.; Jawien, J.; Korbut, R.
Kaempferol, but not resveratrol inhibits angiotensin converting enzyme
J. Physiol. Pharmacol.
59
387-392
2008
Rattus norvegicus
Otani, L.; Ninomiya, T.; Murakami, M.; Osajima, K.; Kato, H.; Murakami, T.
Sardine peptide with angiotensin I-converting enzyme inhibitory activity improves glucose tolerance in stroke-prone spontaneously hypertensive rats
Biosci. Biotechnol. Biochem.
73
2203-2209
2009
Rattus norvegicus
Mecawi, A.S.; Araujo, I.G.; Fonseca, F.V.; Almeida-Pereira, G.; Cortes, W.S.; Rocha, F.F.; Reis, L.C.
Behavioural changes induced by angiotensin-converting enzyme inhibition during pregnancy and lactation in adult offspring rats
Clin. Exp. Pharmacol. Physiol.
36
495-500
2009
Rattus norvegicus
Thaveau, F.; Zoll, J.; Bouitbir, J.; Nguessan, B.; Plobner, P.; Chakfe, N.; Kretz, J.G.; Richard, R.; Piquard, F.; Geny, B.
Effect of chronic pre-treatment with angiotensin converting enzyme inhibition on skeletal muscle mitochondrial recovery after ischemia/reperfusion
Fundam. Clin. Pharmacol.
24
333-340
2010
Rattus norvegicus
Nakahara, T.; Sano, A.; Yamaguchi, H.; Sugimoto, K.; Chikata, H.; Kinoshita, E.; Uchida, R.
Antihypertensive effect of peptide-enriched soy sauce-like seasoning and identification of its angiotensin I-converting enzyme inhibitory substances
J. Agric. Food Chem.
58
821-827
2010
Rattus norvegicus
Lucero, H.A.; Kintsurashvili, E.; Marketou, M.E.; Gavras, H.
Cell signaling, internalization, and nuclear localization of the angiotensin converting enzyme in smooth muscle and endothelial cells
J. Biol. Chem.
285
5555-5568
2010
Rattus norvegicus
Ogawa, A.; Suzuki, Y.; Aoyama, T.; Takeuchi, H.
Dietary alpha-linolenic acid inhibits angiotensin-converting enzyme activity and mRNA expression levels in the aorta of spontaneously hypertensive rats
J. Oleo Sci.
58
355-360
2009
Rattus norvegicus (P47820)
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
Adam, A.; Leclair, P.; Montpas, N.; Koumbadinga, G.A.; Bachelard, H.; Marceau, F.
Altered cardiac bradykinin metabolism in experimental diabetes caused by the variations of angiotensin-converting enzyme and other peptidases
Neuropeptides
44
69-75
2010
Rattus norvegicus
Velkoska, E.; Warner, F.J.; Cole, T.J.; Smith, I.; Morris, M.J.
Metabolic effects of low dose angiotensin converting enzyme inhibitor in dietary obesity in the rat
Nutr. Metab. Cardiovasc. Dis.
20
49-55
2010
Rattus norvegicus
Wang, Y.K.; Shen, D.; Hao, Q.; Yu, Q.; Wu, Z.T.; Deng, Y.; Chen, Y.F.; Yuan, W.J.; Hu, Q.K.; Su, D.F.; Wang, W.Z.
Overexpression of angiotensin-converting enzyme 2 attenuates tonically active glutamatergic input to the rostral ventrolateral medulla in hypertensive rats
Am. J. Physiol. Heart Circ. Physiol.
307
H182-H190
2014
Rattus norvegicus
Arutyunyan, T.; Korystova, A.; Kublik, L.; Levitman, M.; Shaposhnikova, V.; Appazov, N.; Narmanova, R.; Ibadullayeva, S.; Korystov, Y.
Camel thorn extract reduces activity of angiotensin-converting enzyme in rat aorta increased during aging and treatment with NO-Synthase inhibitor
Bull. Exp. Biol. Med.
158
222-224
2014
Rattus norvegicus
Crestani, S.; Gasparotto Junior, A.; Marques, M.C.; Sullivan, J.C.; Webb, R.C.; da Silva-Santos, J.E.
Enhanced angiotensin-converting enzyme activity and systemic reactivity to angiotensin II in normotensive rats exposed to a high-sodium diet
Vascul. Pharmacol.
60
67-74
2014
Rattus norvegicus
Reis, R.I.; Nogueira, M.D.; Campanha-Rodrigues, A.L.; Pereira, L.M.; Andrade, M.C.C.; Parreiras-E-Silva, L.T.; Costa-Neto, C.M.; Mortara, R.A.; Casarini, D.E.
The binding of captopril to angiotensin I-converting enzyme triggers activation of signaling pathways
Am. J. Physiol. Cell Physiol.
315
C367-C379
2018
Rattus norvegicus (P47820), Rattus norvegicus, Rattus norvegicus Wistar (P47820)
Zouari, R.; Hamden, K.; El Feki, A.; Chaabouni, K.; Makni-Ayadi, F.; Sallemi, F.; Ellouze-Chaabouni, S.; Ghribi-Aydi, D.
Evaluation of Bacillus subtilis SPB1 biosurfactant effects on hyperglycemia, angiotensin I-converting enzyme (ACE) activity and kidney function in rats fed on high-fat-high-fructose diet
Arch. Physiol. Biochem.
123
112-120
2017
Rattus norvegicus (P47820), Rattus norvegicus, Rattus norvegicus Wistar (P47820)
Takagaki, A.; Nanjo, F.
Effects of metabolites produced from (-)-epigallocatechin gallate by rat intestinal bacteria on angiotensin I-converting enzyme activity and blood pressure in spontaneously hypertensive rats
J. Agric. Food Chem.
63
8262-8266
2015
Rattus norvegicus (P47820), Rattus norvegicus Wistar (P47820)
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Release 2023.1 (January 2023)
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