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Information on EC 3.4.15.1 - peptidyl-dipeptidase A and Organism(s) Bos taurus and UniProt Accession P12820
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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: Bos taurus
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
-
-
-
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angiotensin I-converting enzyme
-
-
-
-
angiotensin-converting enzyme
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-
-
-
carboxycathepsin
-
-
-
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carboxypeptidase, dipeptidyl
-
-
-
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CD143 antigen
-
-
-
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DCP
-
-
-
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Dipeptidyl carboxypeptidase
-
-
-
-
dipeptidyl carboxypeptidase I
-
-
-
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endothelial cell peptidyl dipeptidase
-
-
-
-
kininase II
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-
-
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PDH
-
-
-
-
peptidase P
-
-
-
-
peptidyl dipeptidase
-
-
-
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peptidyl dipeptidase A
-
-
-
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peptidyl dipeptidase I
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-
-
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peptidyl dipeptidase-4
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-
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-
peptidyl dipeptide hydrolase
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-
-
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peptidyl-dipeptide hydrolase
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-
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peptidyldipeptide hydrolase
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-
-
-
ACE
-
-
-
-
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
benzyloxycarbonyl-Phe-His-Leu + H2O
benzyloxycarbonyl-Phe + His-Leu
-
-
-
-
?
hippuryl-His-Leu + H2O
hippuric acid + His-Leu
-
-
-
-
?
N-(3-(2-furyl)acryloyl)-L-Phe-Gly-Gly + H2O
2-furylacrylic acid + L-Phe-Gly-Gly
-
-
-
?
N-(3-(2-furyl)acryloyl)-L-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-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-benzyloxycarbonyl-L-Phe-L-His-L-Leu + H2O
N-benzyloxycarbonyl-L-Phe + L-His-L-Leu
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-
-
-
?
additional information
?
-
ACE is a key regulator of blood pressure homeostasis
-
-
?
additional information
?
-
-
ACE is a key regulator of blood pressure homeostasis
-
-
?
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
additional information
?
-
ACE is a key regulator of blood pressure homeostasis
-
-
?
additional information
?
-
-
ACE is a key regulator of blood pressure homeostasis
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Cl-
-
kcat increases with increasing KCl concentrations, reaches a maximum at about 300 mM KCl, and the begins to decrease. At relatively low concentrations chloride anions activate the C-domain of the enzyme, but at high concentrations chloride inhibits the enzyme activity. Presence of at least two chloride-binding sites in the C-domain of bovine enzyme: binding of chloride to one of the sites causes activation of the enzyme, whereas chloride binding to the second site results in inhibition of the enzymatic activity
captopril
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reduces the percentage of sperm with progressive motility and acrosome reactions after capacitation in vitro
additional information
-
design and properties of N-carboxyalkyldipeptide inhibitors
-
additional information
-
hot water extract of Tamogi-take mushroom, IC50: 6 mg/ml
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Cl-
-
kcat increases with increasing KCl concentrations, reaches a maximum at about 300 mM KCl, and the begins to decrease. At relatively low concentrations chloride anions activate the C-domain of the enzyme, but at high concentrations chloride inhibits the enzyme activity. Presence of at least two chloride-binding sites in the C-domain of bovine enzyme: binding of chloride to one of the sites causes activation of the enzyme, whereas chloride binding to the second site results in inhibition of the enzymatic activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
the two active sites within bovine lung enzyme exhibits strong negative cooperativity
-
0.14
N-(3-(2-furyl)acryloyl)-Phe-Ala-Lys
-
pH 7.5, 25°C, N-domain from lung enzyme
0.008
N-(3-(2-furyl)acryloyl)-Phe-Ala-Pro
-
pH 7.5, 25°C, N-domain from lung enzyme
0.05
N-(3-(2-furyl)acryloyl)-Phe-Phe-Arg
-
pH 7.5, 25°C, N-domain from lung enzyme
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
the two active sites within bovine lung enzyme exhibitsstrong negative cooperativity
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.3
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8.5
-
pH 6.0: about 40% of maximal activity, pH 8.5: about 35% of maximal activity, reaction with benzyloxycarbonyl-Phe-His-Leu
7 - 9.5
-
pH 7.0: about 40% of maximal activity, pH 9.5: about 50% of maximal activity, reaction with N-hippuryl-His-Leu
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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_BOVIN
1306
1
150097
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
126000
180000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, pH 7.2, in presence of 10% glycerol, activity remains unchanged for at least 3 months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
Adv. Enzymol. Relat. Areas Mol. Biol.
57
1-84
1985
Bos taurus, Canis lupus familiaris, Oryctolagus cuniculus, Homo sapiens, Mammalia, Rattus norvegicus, Sus scrofa
Ondetti, M.A.; Cushman, D.W.
Enzymes of the renin-angiotensin system and their inhibitors
Annu. Rev. Biochem.
51
283-308
1982
Bos taurus, Canis lupus familiaris, Cavia porcellus, Oryctolagus cuniculus, Equus caballus, Homo sapiens, Papio anubis, Rattus norvegicus, Sus scrofa
Kohama, Y.; Matsumoto, S.; Oka, H.; Teramoto, T.; Okabe, M.; Mimura, T.
Isolation of angiotensin-converting enzyme inhibitor from tuna muscle
Biochem. Biophys. Res. Commun.
155
332-337
1988
Bos taurus, Oryctolagus cuniculus
Sharma, M.; Singh, U.S.
Molecular and catalytic properties of angiotensin converting enzyme-I from bovine seminal plasma
J. Biochem.
104
57-61
1988
Bos taurus
Rohrbach, M.S.; Williams, E.B.; Rolstad, R.A.
Purification and substrate specificity of bovine angiotensin-converting enzyme
J. Biol. Chem.
256
225-230
1981
Bos taurus
Garats, E.V.; Nikolskaya, II; Binevski, P.V.; Pozdnev, V.F.; Kost, O.A.
Characterization of bovine atrial angiotensin-converting enzyme
Biochemistry (Moscow)
66
429-434
2001
Bos taurus
Binevski, P.V.; Sizova, E.A.; Pozdnev, V.F.; Kost, O.A.
Evidence for the negative cooperativity of the two active sites within bovine somatic angiotensin-converting enzyme
FEBS Lett.
550
84-88
2003
Bos taurus
Moiseeva, N.A.; Binevski, P.V.; Baskin, II; Palyulin, V.A.; Kost, O.A.
Role of two chloride-binding sites in functioning of testicular angiotensin-converting enzyme
Biochemistry (Moscow)
70
1167-1172
2005
Bos taurus
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
Katayama, K.; Tomatsu, M.; Kawahara, S.; Yamauchi, K.; Fuchu, H.; Kodama, Y.; Kawamura, Y.; Muguruma, M.
Inhibitory profile of nonapeptide derived from porcine troponin C against angiotensin I-converting enzyme
J. Agric. Food Chem.
52
771-775
2004
Bos taurus
Mungunsukh, O.; Marquez, A.P.; Lee, Y.H.; Thiel, G.; Day, R.M.
Characterization of the bovine angiotensin converting enzyme promoter: essential roles of Egr-1, ATF-2 and Ets-1 in the regulation by phorbol ester
Gene
421
81-88
2008
Bos taurus (P12820), Bos taurus
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