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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
- 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 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
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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
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-
-
-
CD143
CD143 antigen
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-
-
-
DCP
Dcp1
Dipeptidyl carboxypeptidase
dipeptidyl carboxypeptidase I
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-
-
-
endothelial cell peptidyl dipeptidase
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-
-
-
kininase II
PDH
-
-
-
-
peptidase P
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-
-
-
peptidyl dipeptidase
peptidyl dipeptidase A
peptidyl dipeptidase I
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-
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-
peptidyl dipeptidase-4
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-
-
-
peptidyl dipeptide hydrolase
peptidyl-dipeptide hydrolase
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-
-
-
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
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-
ACE
-
-
angiotensin converting enzyme
-
-
-
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angiotensin I converting enzyme
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-
angiotensin I-converting enzyme
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-
-
-
angiotensin I-converting enzyme
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-
angiotensin I-converting enzyme
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-
angiotensin-converting enzyme
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-
-
-
angiotensin-converting enzyme
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-
DCP
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-
-
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Dipeptidyl carboxypeptidase
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-
-
-
kininase II
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-
-
-
peptidyl dipeptidase
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-
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peptidyl dipeptidase A
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-
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-
peptidyl dipeptide hydrolase
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-
-
-
peptidyldipeptide hydrolase
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-
-
-
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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
-
-
-
?
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
Drosophila sp. (in: flies)
-
i.e. Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
-
-
?
bradykinin + H2O
L-Phe-L-Arg + L-Ser-L-Pro + L-Arg-L-Pro-L-Pro-Gly-L-Phe
-
-
-
-
?
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-L-Phe-L-His-L-Leu + H2O
N-benzyloxycarbonyl-L-Phe + L-His-L-Leu