Information on EC 3.4.15.1 - peptidyl-dipeptidase A

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY
3.4.15.1
-
RECOMMENDED NAME
GeneOntology No.
peptidyl-dipeptidase A
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
exopeptidase, C-terminus, dipeptide
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
ACE
-
-
-
-
ACE
-
-
ACE2
-
-
ACE2
Q9BYF1
-
ACE2
-
-
ACEI
-
-
angiotensin 1 converting enzyme
-
-
-
-
angiotensin converting enzyme
-
-
-
-
angiotensin converting enzyme
-
-
angiotensin converting enzyme
-
-
angiotensin converting enzyme
-
-
angiotensin converting enzyme
-
-
angiotensin converting enzyme
-
-
angiotensin converting enzyme 1
-
-
angiotensin converting enzyme I
-
-
angiotensin converting enzyme inhibitor
-
-
angiotensin I converting enzyme
-
-
angiotensin I converting enzyme
-
-
angiotensin I-converting enzyme
-
-
-
-
angiotensin I-converting enzyme
-
-
angiotensin I-converting enzyme
-
-
angiotensin I-converting enzyme
-
-
angiotensin I-converting enzyme
-
-
angiotensin-converting enzyme
-
-
-
-
angiotensin-converting enzyme
-
-
angiotensin-converting enzyme
-
-
angiotensin-converting enzyme
-
-
angiotensin-converting enzyme
Q50JE5
-
angiotensin-converting enzyme
-
-
angiotensin-converting enzyme
-
-
angiotensin-converting enzyme
-
-
angiotensin-converting enzyme
B0LJE2
-
angiotensin-converting enzyme 2
Q9BYF1
-
angiotensin-converting enzyme-2
-
-
angiotensin-converting-enzyme
-
-
angiotensin-I converting enzyme
-
-
angiotensin-I converting enzyme
-
-
angiotensin-I converting enzyme
-
-
angiotensin-I-converting enzyme
-
-
angiotensin-I-converting enzyme
-
-
carboxycathepsin
-
-
-
-
carboxypeptidase, dipeptidyl
-
-
-
-
CD143 antigen
-
-
-
-
DCP
-
-
-
-
Dipeptidyl carboxypeptidase
-
-
-
-
Dipeptidyl carboxypeptidase
-
-
dipeptidyl carboxypeptidase I
-
-
-
-
dipeptidylcarboxypeptidase
Q4KXL2
-
endothelial cell peptidyl dipeptidase
-
-
-
-
gACE
-
-
germinal ACE
-
-
kinases II peptidyldipeptide hydrolase
-
-
kininase II
-
-
-
-
kininase II
-
-
PDH
-
-
-
-
peptidase P
-
-
-
-
peptidyl dipeptidase
-
-
-
-
peptidyl dipeptidase
-
-
peptidyl dipeptidase A
-
-
-
-
peptidyl dipeptidase A
-
-
peptidyl dipeptidase I
-
-
-
-
peptidyl dipeptidase-4
-
-
-
-
peptidyl dipeptide hydrolase
-
-
-
-
peptidyl dipeptide hydrolase
-
-
peptidyl-dipeptide hydrolase
-
-
-
-
peptidyldipeptide hydrolase
-
-
-
-
peptidyldipeptide hydrolase
-
-
s-ACE
P12821
-
sACE
P12821
-
somatic ACE
P12821
-
somatic angiotensin I-converting enzyme
P12821
-
TACE
-
-
TACE
P12821
-
testicular ACE
-
-
testis ACE
P12821
-
mACE2
-
-
additional information
-
ACE is a M2 family metallopeptidase
CAS REGISTRY NUMBER
COMMENTARY
9015-82-1
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Bacillus pumilus HL721
HL721
-
-
Manually annotated by BRENDA team
dogs with degenerative mitral valve disease
-
-
Manually annotated by BRENDA team
mongrel dogs
-
-
Manually annotated by BRENDA team
recombinantly expressed in Pichia pastoris
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
4842 adult renal transplantation patients from Spain of different operation years
-
-
Manually annotated by BRENDA team
children and young people with IgA nephropathy and moderate proteinuria
-
-
Manually annotated by BRENDA team
hypertensive patients of African ancestry
-
-
Manually annotated by BRENDA team
individual biomechanical muscle properties correlate with ACE I/D gene polymorphism
-
-
Manually annotated by BRENDA team
patients taking angiotensin-converting enzyme inhibitor therapy
-
-
Manually annotated by BRENDA team
patients with congestive heart failure
-
-
Manually annotated by BRENDA team
patients with heart failure
-
-
Manually annotated by BRENDA team
precursor
SwissProt
Manually annotated by BRENDA team
precursor
SwissProt
Manually annotated by BRENDA team
recombinant
-
-
Manually annotated by BRENDA team
recombinant ACE construct tACEDELTA36NJ
SwissProt
Manually annotated by BRENDA team
Saudi population from Qassim region
-
-
Manually annotated by BRENDA team
somatic ACE isozyme
-
-
Manually annotated by BRENDA team
somatic and germinal isozymes, sACE and gACE
-
-
Manually annotated by BRENDA team
testis-specific isoform precursor
SwissProt
Manually annotated by BRENDA team
wild-type enzyme and mutants in which one active site has been inactivated by site-directed mutagenesis
-
-
Manually annotated by BRENDA team
-
Q4KXL2
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
two ACE forms: a somatic form of MW 150000-180000 Da and a smaller isoform of MW 90009-110000 Da in germinal cells
-
-
Manually annotated by BRENDA team
precursor
SwissProt
Manually annotated by BRENDA team
atherosclerosis-prone apolipoprotein E-deficient C57BL/6J mice
-
-
Manually annotated by BRENDA team
creation of mice with angiotensin converting enzyme expression limited to selected tissue types
-
-
Manually annotated by BRENDA team
male ob/ob, B6.V-Lepob/J mice and male ob/+ C57BL/6J mice
-
-
Manually annotated by BRENDA team
Swiss strain
-
-
Manually annotated by BRENDA team
Mus musculus Swiss
Swiss strain
-
-
Manually annotated by BRENDA team
expressed in a mouse epithelial cell line or in HeLa cells permanently transfected with gACE expression vector
-
-
Manually annotated by BRENDA team
New Zealand white rabbits
-
-
Manually annotated by BRENDA team
baboon
-
-
Manually annotated by BRENDA team
female Wistar rats
-
-
Manually annotated by BRENDA team
low molecular weight angiotensin I converting enzyme
-
-
Manually annotated by BRENDA team
male Sprague Dawley rats
-
-
Manually annotated by BRENDA team
male Wistar
-
-
Manually annotated by BRENDA team
male Wistar rats
-
-
Manually annotated by BRENDA team
spontaneous hypertension rats
-
-
Manually annotated by BRENDA team
spontaneously hypertensive model rats
-
-
Manually annotated by BRENDA team
spontaneously hypertensive rats
-
-
Manually annotated by BRENDA team
spontaneously hypertensive rats
Uniprot
Manually annotated by BRENDA team
Sprague-Dawley
-
-
Manually annotated by BRENDA team
Wistar rats
-
-
Manually annotated by BRENDA team
with experimental chronic heart failure
-
-
Manually annotated by BRENDA team
Zucker rats and Sprague-Dawley rats
-
-
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
Sprague-Dawley
-
-
Manually annotated by BRENDA team
cotton leafworm
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
ACE induces angioedema, mainly mediated by bradykinin-induced activation of vascular bradykinin B2 receptors. Icatibant, a bradykinin B2 receptor antagonist, acts as therapeutic drug in treatment of ACE-induced angioedema
malfunction
-
ACE inhibitors can induce angioedema, overview. Polymorphism of ACE insertion/deletion and the bradykinin B2 receptor polymorphisms are not involved in the development of ACEi-induced angioedema, overview
malfunction
-
both angiotensin-converting enzyme inhibitors and angiotensin receptor blockers can slow the progression of diabetic nephropathy, overview
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
-
some genetic alleles predispose human individuals to hypertension and cardiac diseases, overview
malfunction
-
the enzyme is involved in hypertension, enzyme inhibition by flaxseed, Linum usitatissimum seeds, peptides reduces hypertension
malfunction
-
atherosclerosis-enhancing effects of angiotensin II
malfunction
-
polymorphisms in the neurokinin-2 receptor gene are associated with angiotensin-converting enzyme inhibitor-induced cough, overview
malfunction
-
clinical effects of calcium channel blocker and angiotensin converting enzyme inhibitor on endothelial function and arterial stiffness in patients with angina pectoris, overview
malfunction
-
ACE is involved in risk of GFR decrease, doubling of serum creatinine or progression to ESRD in renal disease
malfunction
-
use of ACE inhibitor is associated with a significant decrease in long-term mortality and cardiovascular events in the patients with diastolic heart failure
physiological function
-
angiotensin I-converting enzyme plays a pivotal role in blood pressure regulation
physiological function
-
ACE plays an important role in the renin-angiotensin system
physiological function
-
ACE is part of the renin-angiotensin system, RAS, that regulates blood pressure and electrolyte homeostasis, and is involved in regulating regeneration, cell growth, apoptosis, inflammation and angiogenesis, expression and function of the key RAS component ACE during fracture healing, overview. ACE is important in bone remodelling; key enzyme of the renin-angiotensin system, a circulating endocrine system regulating blood pressure and electrolyte homeostasis. Inhibition of angiotensin-converting enzyme stimulates fracture healing and periosteal callus formation in a murine femur fracture model, overview
physiological function
-
ACE limits the stimulation of bradykinin receptors by degrading bradykinin, functions of the bradykinin B2 receptor, B2R, signaling, overview. Interaction of B2R and ACE or allosteric transmission occurs on the plasma membrane surface
physiological function
-
angiotensin I-converting enzyme, ACE, catalyzes the formation of vasoconstrictor, angiotensin II, and the inactivation of vasodilator, bradykinin
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
-
ACE is involved in corneal angiogenesis
physiological function
-
ACE is responsible for degradation of bradykinin which is the most potent stimulus for tissue plasminogen activator secretion. The reaction product from angiotensin I cleavage, angiotensin II, has an important role on fibrinolytic balance causing release of plasminogen activator inhibitor 1 and consequently inhibits fibrinolysis
physiological function
-
enzyme inhibitors are useful in treatment of hypertension and heart failure, as well as for peritoneal dialysis patients, because inhibit the local tissue renin-angiotensin system, which results in less development of peritoneal fibrosis and a longer life for the peritoneal membrane, overview
physiological function
-
peptidases angiotensin-converting enzyme, together with neutral endopeptidase 24.11, mediates most of the kinin catabolism in normal cardiac tissue
metabolism
-
ACE is involved in the renin-angiotensin-aldosterone system, overview
additional information
-
the enzyme inhibition by angiotensin-converting enzyme inhibitors is inhibited by aspirin, which can cause therapeutic problems during application of both in treatment of heart failure patients. Angiotensin receptor blockers do not interfere with the bradykinin pathway, detailed overview
additional information
-
angiotensin-converting enzyme inhibitors treatment of myocardial infarction patients bears is asscoiated with increased mortality, the risk is also existent for renal failure patients, overview
additional information
-
renal failure risks of angiotensin-converting-enzyme inhibitors, angiotensin II-receptor blockers, and aspirin for patients with diabetes, overview
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(7-methoxycoumarin-2-acetic acid)-Ala-Ser-Asp-Lys-(N3-(2,4-dinitrophenyl)-L-2,3-diaminopropyl) + H2O
?
show the reaction diagram
-
-
-
?
(7-methoxycoumarin-2-acetic acid)-Ser-Asp-Lys-(N3-(2,4-dinitrophenyl)-L-2,3-diaminopropyl) + H2O
?
show the reaction diagram
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Ala-Ser-Asp-Lys-N3-(2,4-dinitrophenyl)-L-diaminopropionionate + H2O
?
show the reaction diagram
-
-
-
-
?
1-dimethylaminonaphthalene-5-sulfonyl-Gly-Gly-Gly + H2O
1-dimethylaminonaphthalene-5-sulfonyl-Gly + Gly-Gly
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Ala-Ala-Leu-Ala-Gly-nitrobenzylamide + H2O
?
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Ala-Ala-Tyr-Leu-Ala-Gly-nitrobenzylamide + H2O
?
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Ala-Tyr-Leu-Ala-Gly-nitrobenzylamide + H2O
?
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-L-Phe-L-Arg-L-Lys-2,4-dinitrophenyl-L-Pro + H2O
?
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Val-Tyr-Leu-Ala-Gly-nitrobenzylamide + H2O
?
show the reaction diagram
-
-
-
-
?
2-furanacryloyl-1-Phe-Gly-Gly + H2O
?
show the reaction diagram
-
-
-
-
?
2-furanacryloyl-Phe-Gly-Gly + H2O
2-furanacryloyl-Phe + Gly-Gly
show the reaction diagram
-
-
-
-
?
2-furanacryloyl-Phe-Gly-Gly + H2O
2-furanacryloyl-Phe + Gly-Gly
show the reaction diagram
-
3-(2-furanacryloyl)-Phe-Gly-Gly
-
-
?
2-furylacryloyl-Phe-Gly-Gly + H2O
2-furylacrylic acid + Phe-Gly-Gly
show the reaction diagram
-
-
-
?
3-hydroxybutyryl-Gly-Gly-Gly + H2O
3-hydroxybutyryl-Gly + Gly-Gly
show the reaction diagram
-
-
-
-
?
3-hydroxybutyrylglycyl-glycyl-glycine + H2O
3-hydroxybutyrylglycine + Gly-Gly
show the reaction diagram
-
-
-
-
?
3-hydroxybutyrylglycyl-glycyl-glycine + H2O
3-hydroxybutyrate + glycyl-glycine
show the reaction diagram
-
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
-
-
?
7-amido-4-carboxymethylcoumarin-YVADAPK(Dnp)-OH + H2O
dinitrophenol + 7-amino-4-carbamoylmethylcoumarin-YVADAPK
show the reaction diagram
-
-
-
-
?
Abz-YRK(2,4-dinitrophenyl)P + H2O
?
show the reaction diagram
-
-
-
-
?
acetyl-His-Pro-(NO2)Phe-His-Leu + H2O
acetyl-His-Pro-(NO2)Phe + His-Leu
show the reaction diagram
-
-
-
-
?
Ala-Ala-Ala-Ala + H2O
Ala-Ala + Ala-Ala
show the reaction diagram
-
-
-
?
Ala-Ala-Ala-Ala + H2O
Ala-Ala + Ala-Ala
show the reaction diagram
-
-
-
-
?
Ala-Ala-Ala-Ala + H2O
Ala-Ala + Ala-Ala
show the reaction diagram
-
-
-
?
Ala-Ala-Ala-Pro + H2O
Ala-Ala-Ala + Pro
show the reaction diagram
-
-
-
?
Ala-Phe-Ala + H2O
Ala-Phe + Ala
show the reaction diagram
-
-
-
-
?
amyloid beta-peptide(1-40) + H2O
amyloid beta-peptide(1-7) + amyloid beta-peptide(8-40)
show the reaction diagram
-
cleavage at the Asp7-Ser9 bond, 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 Alzheimers disease
-
?
amyloid beta-protein 1-40 + H2O
amyloid beta-peptide(1-7) + amyloid beta-peptide(8-40)
show the reaction diagram
-
ACE cleaves amyloid beta-protein 1-40 between Asp7 and Ser8
-
-
?
amyloid beta-protein 1-42 + H2O
amyloid beta-protein 1-420 + ?
show the reaction diagram
-
angiotensin-converting enzyme converts amyloid beta-protein 1-42 to amyloid beta-protein1-40. ACE regulates Abeta1-42/Abeta1-40 ratio in vivo by converting secreted Abeta1-42 to Abeta1-40 and degrading Abetas.The upregulation of ACE activity can be a novel therapeutic strategy for Alzheimers disease
-
-
?
amyloid beta-protein 1-42 + H2O
amyloid beta-protein 1-420 + ?
show the reaction diagram
-
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 Alzheimers disease
-
-
?
amyloid beta-protein 1-42 + H2O
amyloid beta-peptide(1-40) + amyloid beta-peptide(41-42)
show the reaction diagram
-
ACE cleaves amyloid beta-protein 1-42 at multiple sites
-
-
?
angiotensin (1-9) + H2O
?
show the reaction diagram
-
-
-
-
?
Angiotensin I + H2O
?
show the reaction diagram
-
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
show the reaction diagram
-
-
-
-
-
angiotensin I + H2O
angiotensin II + His-Leu
show the reaction diagram
-
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
show the reaction diagram
-
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
show the reaction diagram
-
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
show the reaction diagram
-
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
show the reaction diagram
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
show the reaction diagram
-
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
show the reaction diagram
-
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
show the reaction diagram
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
show the reaction diagram
-
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
show the reaction diagram
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
show the reaction diagram
-
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
show the reaction diagram
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
show the reaction diagram
P47820
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
show the reaction diagram
-
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
show the reaction diagram
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
show the reaction diagram
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
show the reaction diagram
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
show the reaction diagram
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
show the reaction diagram
-
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
show the reaction diagram
-
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
show the reaction diagram
-
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
show the reaction diagram
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
show the reaction diagram
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
show the reaction diagram
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
show the reaction diagram
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
show the reaction diagram
-
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
show the reaction diagram
-
about 5% of the activity with hippury-Lys-Leu
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
show the reaction diagram
-
enzyme plays a major role in blood pressure regulation
-
?
angiotensin I + H2O
angiotensin II + His-Leu
show the reaction diagram
-
the enzyme plays an important role in blood pressure homeostasis
-
?
angiotensin I + H2O
angiotensin II + His-Leu
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
i.e. DRVYIHPFHL
i.e. DRVYIHPF
-
?
angiotensin I + H2O
angiotensin II + His-Leu
show the reaction diagram
-
i.e. DRVYIHPFHL
i.e. DRVYIHPF
-
?
angiotensin I + H2O
angiotensin II + His-Leu
show the reaction diagram
-
i.e. DRVYIHPFHL
i.e. DRVYIHPF
-
?
angiotensin I + H2O
angiotensin II + His-Leu
show the reaction diagram
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
show the reaction diagram
Bacillus pumilus HL721
-
-
-
?
angiotensin I + H2O
angiotensin II + L-His-L-Leu
show the reaction diagram
-
-
-
-
?
angiotensin I + H2O
angiotensin II + L-His-L-Leu
show the reaction diagram
-
-
-
-
?
angiotensin I + H2O
angiotensin II + L-His-L-Leu
show the reaction diagram
P12820
-
-
-
?
angiotensin I + H2O
angiotensin II + L-His-L-Leu
show the reaction diagram
-
-
-
-
?
angiotensin I + H2O
angiotensin II + L-His-L-Leu
show the reaction diagram
-
-
-
-
?
angiotensin I + H2O
angiotensin II + L-His-L-Leu
show the reaction diagram
-
-
-
-
?
angiotensin I + H2O
angiotensin II + L-His-L-Leu
show the reaction diagram
-
-
-
-
?
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met-NH2 + H2O
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly + Leu-Met-NH2
show the reaction diagram
-
-
-
-
?
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met-NH2 + H2O
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly + Leu-Met-NH2
show the reaction diagram
-
-
-
-
?
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met-NH2 + H2O
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly + Leu-Met-NH2
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
primary cleavage of Phe8-Gly9
-
-
?
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met-NH2 + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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-Pro-Gly-Phe-Ser-Pro-Tyr-Arg + H2O
?
show the reaction diagram
-
-
-
-
?
Arg-Pro-Pro-Gly-Phe-Thr-Pro-Phe-Arg + H2O
?
show the reaction diagram
-
-
-
-
?
Asn-Arg-Val-Tyr-Ile-His-Pro-(NO2)Phe-His-Leu + H2O
Asn-Arg-Val-Tyr-Ile-His-Pro-(NO2)Phe + His-Leu
show the reaction diagram
-
-
-
-
?
benzoyl-Gly-Ala-His-Leu + H2O
benzoyl-Gly-Ala + His-Leu
show the reaction diagram
-
-
-
-
?
benzoyl-Gly-Ala-Leu + H2O
benzoyl-Gly + Ala-Leu
show the reaction diagram
-
-
-
-
?
benzoyl-Gly-Ala-Pro + H2O
benzoyl-Gly + Ala-Pro
show the reaction diagram
-
-
-
-
?
benzoyl-Gly-Ala-Pro + H2O
benzoyl-Gly + Ala-Pro
show the reaction diagram
-
-
-
?
benzoyl-Gly-Ala-Pro + H2O
benzoyl-Gly + Ala-Pro
show the reaction diagram
-
-
-
-
?
benzoyl-Gly-Ala-Pro + H2O
benzoyl-Gly + Ala-Pro
show the reaction diagram
-
-
-
-
?
benzoyl-Gly-Ala-Pro + H2O
benzoyl-Gly + Ala-Pro
show the reaction diagram
Bacillus pumilus HL721
-
-
-
?
benzoyl-Gly-Arg-His-Leu + H2O
benzoyl-Gly-Arg + His-Leu
show the reaction diagram
-
-
-
-
?
benzoyl-Gly-Arg-Leu + H2O
benzoyl-Gly + Arg-Leu
show the reaction diagram
-
-
-
-
?
benzoyl-Gly-Glu-Leu + H2O
benzoyl-Gly + Glu-Leu
show the reaction diagram
-
-
-
-
?
benzoyl-Gly-Gly-Gly + H2O
benzoyl-Gly + Gly-Gly
show the reaction diagram
-
-
-
-
?
benzoyl-Gly-Gly-Gly + H2O
benzoyl-Gly + Gly-Gly
show the reaction diagram
-
-
-
-
?
benzoyl-Gly-His-Ala + H2O
benzoyl-Gly + His-Ala
show the reaction diagram
-
-
-
-
?
benzoyl-Gly-His-Leu + H2O
benzoyl-Gly + His-Leu
show the reaction diagram
-
-
-
-
?
benzoyl-Gly-His-Leu + H2O
benzoyl-Gly + His-Leu
show the reaction diagram
-
-
-
-
?
benzoyl-Gly-His-Leu + H2O
benzoyl-Gly + His-Leu
show the reaction diagram
-
-
-
-
-
benzoyl-Gly-His-Leu + H2O
benzoyl-Gly + His-Leu
show the reaction diagram
-
-
-
-
?
benzoyl-Gly-His-Leu + H2O
benzoyl-Gly + His-Leu
show the reaction diagram
-
-
-
-
-
benzoyl-Gly-His-Leu + H2O
benzoyl-Gly + His-Leu
show the reaction diagram
-
-
-
?
benzoyl-Gly-His-Leu + H2O
benzoyl-Gly + His-Leu
show the reaction diagram
-
-
-
-
?
benzoyl-Gly-His-Leu + H2O
benzoyl-Gly + His-Leu
show the reaction diagram
Bacillus pumilus HL721
-
-
-
?
benzoyl-Gly-His-Phe + H2O
benzoyl-Gly + His-Phe
show the reaction diagram
-
-
-
-
?
benzoyl-Gly-Ile-His-Leu + H2O
benzoyl-Gly-Ile + His-Leu
show the reaction diagram
-
-
-
-
?
benzoyl-Gly-Phe-Arg + H2O
benzoyl-Gly + Phe-Arg
show the reaction diagram
-
-
-
-
?
benzoyl-Gly-Phe-Arg + H2O
benzoyl-Gly + Phe-Arg
show the reaction diagram
-
-
-
-
?
benzoyl-Gly-Phe-His-Leu + H2O
benzoyl-Gly-Phe + His-Leu
show the reaction diagram
-
-
-
-
?
benzoyl-Gly-Phe-Leu + H2O
benzoyl-Gly + Phe-Leu
show the reaction diagram
-
-
-
-
?
benzoyl-Gly-Pro-His-Leu + H2O
benzoyl-Gly-Pro + His-Leu
show the reaction diagram
-
-
-
-
?
benzoyl-Gly-Ser-His-Leu + H2O
benzoyl-Gly-Ser + His-Leu
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-(NO2)Phe-His-Leu + H2O
benzyloxycarbonyl-(NO2)Phe + His-Leu
show the reaction diagram
-
-
-
-
-
benzyloxycarbonyl-(NO2)Phe-His-Leu + H2O
benzyloxycarbonyl-(NO2)Phe + His-Leu
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Gly-Gly-Gly + H2O
benzyloxycarbonyl-Gly + Gly-Gly
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Leu-Gly-Gly + H2O
benzyloxycarbonyl-Leu + Gly-Gly
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Phe-His-Leu + H2O
benzyloxycarbonyl-Phe + His-Leu
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Phe-His-Leu + H2O
benzyloxycarbonyl-Phe + His-Leu
show the reaction diagram
P12821
-
-
-
?
benzyloxycarbonyl-Phe-His-Leu + H2O
benzyloxycarbonyl-Phe + His-Leu
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Phe-His-Leu + H2O
?
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Phe-His-Leu + H2O
?
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Phe-His-Leu + H2O
?
show the reaction diagram
P12821
-
-
-
?
benzyloxycarbonyl-Phe-Tyr-Leu
benzyloxycarbonyl-Phe + Tyr-Leu
show the reaction diagram
-
-
-
-
?
beta-neoendorphin + H2O
?
show the reaction diagram
-
-
-
-
?
Bradykinin + H2O
?
show the reaction diagram
-
-
-
-
?
Bradykinin + H2O
?
show the reaction diagram
-
-
-
-
?
Bradykinin + H2O
?
show the reaction diagram
P12820
-
-
-
?
Bradykinin + H2O
?
show the reaction diagram
-
-
-
-
?
Bradykinin + H2O
?
show the reaction diagram
-
degradation
-
-
?
Bradykinin + H2O
?
show the reaction diagram
-
inactivation
-
-
?
Bradykinin + H2O
?
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
?
bradykinin + H2O
Phe-Arg + Ser-Pro + Arg-Pro-Pro-Gly-Phe
show the reaction diagram
-
-
-
-
?
bradykinin + H2O
Phe-Arg + Ser-Pro + Arg-Pro-Pro-Gly-Phe
show the reaction diagram
-
-
-
-
?
bradykinin + H2O
Phe-Arg + Ser-Pro + Arg-Pro-Pro-Gly-Phe
show the reaction diagram
-
-
-
-
?
bradykinin + H2O
Phe-Arg + Ser-Pro + Arg-Pro-Pro-Gly-Phe
show the reaction diagram
-
-
-
-
?
bradykinin + H2O
Phe-Arg + Ser-Pro + Arg-Pro-Pro-Gly-Phe
show the reaction diagram
-
-
-
?
bradykinin + H2O
Phe-Arg + Ser-Pro + Arg-Pro-Pro-Gly-Phe
show the reaction diagram
-
-
-
-
?
bradykinin + H2O
Phe-Arg + Ser-Pro + Arg-Pro-Pro-Gly-Phe
show the reaction diagram
-
-
-
?
bradykinin + H2O
Phe-Arg + Ser-Pro + Arg-Pro-Pro-Gly-Phe
show the reaction diagram
-
-
-
-
?
bradykinin + H2O
Phe-Arg + Ser-Pro + Arg-Pro-Pro-Gly-Phe
show the reaction diagram
-
-
-
?
bradykinin + H2O
Phe-Arg + Ser-Pro + Arg-Pro-Pro-Gly-Phe
show the reaction diagram
-
-
Phe-Arg + Ser-Pro -Arg-Pro-Pro-Gly-Phe
?
bradykinin + H2O
Phe-Arg + Ser-Pro + Arg-Pro-Pro-Gly-Phe
show the reaction diagram
-
-
Arg-Pro-Pro + Gly-Phe + Ser-Pro + Phe-Arg
?
bradykinin + H2O
Phe-Arg + Ser-Pro + Arg-Pro-Pro-Gly-Phe
show the reaction diagram
-
-
hydrolyzes Phe-Arg + Ser-Pro from the C-terminus of bradykinin
?
bradykinin + H2O
Phe-Arg + Ser-Pro + Arg-Pro-Pro-Gly-Phe
show the reaction diagram
-
about 3.5% of the activity with hippury-Lys-Leu
-
?
bradykinin + H2O
Phe-Arg + Ser-Pro + Arg-Pro-Pro-Gly-Phe
show the reaction diagram
-
-
hydrolyzes Phe-Arg + Ser-Pro from the C-terminus of bradykinin
?
bradykinin + H2O
Phe-Arg + Ser-Pro + Arg-Pro-Pro-Gly-Phe
show the reaction diagram
Bacillus pumilus HL721
-
-
Arg-Pro-Pro + Gly-Phe + Ser-Pro + Phe-Arg
?
bradykinin + H2O
Arg-Pro-Pro-Gly-Phe + Ser-Pro + Phe-Arg
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
?
cholecystokinin-8 + H2O
?
show the reaction diagram
-
-
-
-
?
dansyltriglycine + H2O
?
show the reaction diagram
-
-
-
-
?
dynorphin + H2O
?
show the reaction diagram
-
-
-
-
?
furanacryloyl-L-Phe-Gly-Gly + H2O
furanacryloyl-L-Phe + Gly-Gly
show the reaction diagram
-
-
-
-
?
furanacryloyl-L-Phe-Gly-Gly + H2O
furanacryloyl-L-Phe + Gly-Gly
show the reaction diagram
-
-
-
-
?
Gly-Ala-Ala + H2O
Gly + Ala-Ala
show the reaction diagram
-
-
-
?
Gly-Gly-Tyr-Arg + H2O
Gly-Gly + Tyr-Arg
show the reaction diagram
-
-
-
?
Gly-His-Gly + H2O
Gly + His-Gly
show the reaction diagram
-
-
-
?
Gly-Ile-His-Pro-(NO2)Phe-His-Leu + H2O
Gly-Ile-His-Pro-(NO2)Phe + His-Leu
show the reaction diagram
-
-
-
-
?
Gly-Pro-(NO2)Phe-His-Leu + H2O
Gly-Pro-(NO2)Phe + His-Leu
show the reaction diagram
-
-
-
-
?
gonadotropin-releasing hormone + H2O
?
show the reaction diagram
-
a bridging interaction between Arg500 of the N-domain and Arg8 of gonadotropin-releasing hormone that involves a buried chloride ion may account for its role in the specificity of the N-domain for endoproteolytic cleavage of the substrate at the NH2-terminus in vitro
-
-
?
hippuryl-Gly-Gly + H2O
hippuric acid + Gly-Gly
show the reaction diagram
-
-
-
-
?
hippuryl-Gly-Gly + H2O
hippuric acid + Gly-Gly
show the reaction diagram
-
-
-
-
?
hippuryl-Gly-Gly + H2O
hippuric acid + Gly-Gly
show the reaction diagram
-
-
-
-
?
hippuryl-Gly-His-Leu + H2O
hippuric acid + His-Leu
show the reaction diagram
-
-
-
?
hippuryl-His-Leu + H2O
hippuric acid + His-Leu
show the reaction diagram
-
-
-
-
?
hippuryl-His-Leu + H2O
hippuric acid + His-Leu
show the reaction diagram
-
-
-
-
?
hippuryl-His-Leu + H2O
hippuric acid + His-Leu
show the reaction diagram
-
-
-
-
?
hippuryl-His-Leu + H2O
hippuric acid + His-Leu
show the reaction diagram
-
-
-
?
hippuryl-His-Leu + H2O
hippuric acid + His-Leu
show the reaction diagram
-
-
-
-
?
hippuryl-His-Leu + H2O
hippuric acid + His-Leu
show the reaction diagram
-
-
-
-
?
hippuryl-His-Leu + H2O
hippuric acid + His-Leu
show the reaction diagram
P47820
-
-
-
?
hippuryl-His-Leu + H2O
hippuric acid + His-Leu
show the reaction diagram
-
-
-
-
?
hippuryl-His-Leu + H2O
hippuric acid + His-Leu
show the reaction diagram
-
-
-
-
?
hippuryl-His-Leu + H2O
hippuric acid + His-Leu
show the reaction diagram
-
-
-
-
?
hippuryl-His-Leu + H2O
hippuric acid + His-Leu
show the reaction diagram
-
-
-
-
?
hippuryl-His-Leu + H2O
hippuric acid + His-Leu
show the reaction diagram
-
-
-
?
hippuryl-His-Leu + H2O
hippuric acid + His-Leu
show the reaction diagram
-
-
-
-
?
hippuryl-His-Leu + H2O
hippuric acid + His-Leu
show the reaction diagram
-
-
-
-
?
hippuryl-His-Leu + H2O
hippuric acid + His-Leu
show the reaction diagram
-
-
-
-
?
hippuryl-His-Leu + H2O
hippuric acid + His-Leu
show the reaction diagram
-
-
-
-
-
hippuryl-His-Leu + H2O
hippuric acid + His-Leu
show the reaction diagram
-
-
-
?
hippuryl-His-Leu + H2O
hippuric acid + His-Leu
show the reaction diagram
-
-
-
?
hippuryl-His-Leu + H2O
hippuric acid + His-Leu
show the reaction diagram
-
-
-
-
?
hippuryl-His-Leu + H2O
hippuric acid + His-Leu
show the reaction diagram
-, Q4KXL2
-
-
-
?
hippuryl-His-Leu + H2O
hippuric acid + His-Leu
show the reaction diagram
P12821
-
-
-
?
hippuryl-His-Leu + H2O
hippuric acid + His-Leu
show the reaction diagram
-
colorimetric assay method
-
-
?
hippuryl-His-Leu + H2O
hippuric acid + His-Leu
show the reaction diagram
-
colorimetric quantification of released hippuric acid, using pyridine and benzene sulfonyl chloride, assay method evaluation, overview
-
-
?
hippuryl-histidyl-leucine + H2O
?
show the reaction diagram
-
-
-
-
?
hippuryl-L-His-L-Leu + H2O
hippuric acid + L-His-L-Leu
show the reaction diagram
-
-
-
-
?
hippuryl-L-His-L-Leu + H2O
hippuric acid + L-His-L-Leu
show the reaction diagram
-
-
-
-
?
hippuryl-L-His-L-Leu + H2O
hippuric acid + L-His-L-Leu
show the reaction diagram
-
-
-
-
?
hippuryl-L-His-L-Leu + H2O
hippuric acid + L-His-L-Leu
show the reaction diagram
-
-
-
-
?
hippuryl-Lys-Leu + H2O
hippuric acid + Lys-Leu
show the reaction diagram
-
-
-
-
?
hippuryl-Phe-Arg + H2O
hippuric acid + Phe-Arg
show the reaction diagram
-
-
-
-
?
hippuryl-Phe-Arg + H2O
hippuric acid + Phe-Arg
show the reaction diagram
-
-
-
-
?
His-Lys-Thr-Asp-Ser-Phe-Val-Gly-Leu-Met-NH2 + H2O
His-Lys-Thr-Asp-Ser-Phe-Val-Gly + Leu-Met-NH2
show the reaction diagram
-
i.e. substance K, degraded by striatal but not by lung enzyme
-
-
?
His-Pro-(NO2)Phe-His-Leu + H2O
His-Pro-(NO2)Phe + His-Leu
show the reaction diagram
-
-
-
-
?
Ile-Ser-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
?
show the reaction diagram
-
-
-
-
?
LEQIYHL + H2O
?
show the reaction diagram
-
-
-
?
Leu5-enkephalin + H2O
Tyr-Gly-Gly + Phe-Leu
show the reaction diagram
-
-
-
-
?
Leu5-enkephalin + H2O
Tyr-Gly-Gly + Phe-Leu
show the reaction diagram
-
-
-
-
?
Luteinizing hormone-releasing hormone + H2O
?
show the reaction diagram
-
degraded by striatal and by lung enzyme
-
-
?
LVVYPWTQRY + H2O
LVVYPWTQ + RY + LVVY + PW + LVVYPW + TQ
show the reaction diagram
-
-
dipeptide TQ is unidentified. Sequential removal of dipeptides in three consecutive steps
?
MCA-Ala-Ser-Asp-Lys-Dap(DNP)-OH + H2O
?
show the reaction diagram
Q9BYF1
angiotensin-converting enzyme
-
-
?
MCA-Tyr-Val-Ala-Asp-Ala-Pro-Lys(DNP)-OH + H2O
?
show the reaction diagram
Q9BYF1
angiotensin-converting enzyme 2
-
-
?
Met5-enkephalin + H2O
Tyr-Gly-Gly + Phe-Met
show the reaction diagram
-
-
-
-
?
Met5-enkephalin + H2O
Tyr-Gly-Gly + Phe-Met
show the reaction diagram
-
-
-
-
?
Met5-enkephalin + H2O
Tyr-Gly-Gly + Phe-Met
show the reaction diagram
-
-
-
-
?
Met5-enkephalin-Arg6-Gly7-Leu8 + H2O
Tyr-Gly-Gly-Phe-met-Arg + Gly-Leu
show the reaction diagram
-
-
-
-
?
N-(1-(S)-carboxy-3-phenylpropyl)-L-Ala-L-Pro + H2O
?
show the reaction diagram
-
i.e. MK-422
-
-
?
N-(1-(S)-carboxy-3-phenylpropyl)-L-Lys-L-Pro + H2O
?
show the reaction diagram
-
i.e. MK-522
-
-
?
N-(3-(2-furyl)acryloyl)-L-Phe-Gly-Gly + H2O
2-furylacrylic acid + L-Phe-Gly-Gly
show the reaction diagram
-
-
-
?
N-(3-(2-furyl)acryloyl)-L-Phe-Gly-Gly + H2O
N-(3-(2-furyl)acrylic acid) + Phe-Gly-Gly
show the reaction diagram
-
-
-
?
N-(3-(2-furyl)acryloyl)-L-Phe-Phe-Arg + H2O
2-furylacrylic acid + L-Phe-Phe-Arg
show the reaction diagram
-
-
-
?
N-(3-(2-furyl)acryloyl)-Phe-Ala-Ala + H2O
2-furylacrylic acid + Phe-Ala-Ala
show the reaction diagram
-
-
-
?
N-(3-(2-furyl)acryloyl)-Phe-Ala-Gly + H2O
2-furylacrylic acid + Phe-Ala-Gly
show the reaction diagram
-
-
-
?
N-(3-(2-furyl)acryloyl)-Phe-Ala-Lys + H2O
2-furylacrylic acid + Phe-Ala-Lys
show the reaction diagram
-
-
-
?
N-(3-(2-furyl)acryloyl)-Phe-Ala-Pro + H2O
2-furylacrylic acid + Phe-Ala-Pro
show the reaction diagram
-
-
-
?
N-(3-(2-furyl)acryloyl)-Phe-Gly-Gly + H2O
2-furylacrylic acid + Phe-Gly-Gly
show the reaction diagram
-
-
-
?
N-(3-(2-furyl)acryloyl)-Phe-Phe-Arg + H2O
2-furylacrylic acid + Phe-Phe-Arg
show the reaction diagram
-
-
-
?
N-acetyl-Ala-Ala-Ala + H2O
N-acetyl-Ala + Ala-Ala
show the reaction diagram
-
-
-
?
N-hippuryl-His-Leu + H2O
hippuric acid + His + Leu
show the reaction diagram
-
-
-
?
N-hippuryl-His-Leu + H2O
hippuric acid + His-Leu
show the reaction diagram
-
-
-
?
N-hippuryl-His-Leu + H2O
hippuric acid + His-Leu
show the reaction diagram
-
-
-
?
N-hippuryl-His-Leu + H2O
N-hippuric acid + His-Leu
show the reaction diagram
-
-
-
-
?
N-[3-(2-furyl)acryloyl]-L-Phe-Gly-Gly + H2O
2-furylacrylic acid + L-Phe-Gly-Gly
show the reaction diagram
-
-
-
-
?
N-[3-(2-furyl)acryloyl]-L-phenylalanyl-glycyl-glycine + H2O
N-[3-(2-furyl)acryloyl]-L-phenylalanine + glycyl-glycine
show the reaction diagram
-
-
-
-
?
N-[3-(2-furyl)acryloyl]-L-phenylalanyl-glycyl-glycine + H2O
?
show the reaction diagram
-
-
-
-
?
N-[3-(2-furyl)acryloyl]-Phe-Gly-Gly + H2O
N-[3-(2-furyl)acryloyl]-Phe + Gly-Gly
show the reaction diagram
-
-
-
-
?
neurotensin + H2O
pGlu-Leu-Tyr-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Tyr + Ile-Leu
show the reaction diagram
-
-
-
-
?
neurotensin + H2O
pGlu-Leu-Tyr-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Tyr + Ile-Leu
show the reaction diagram
-
-
-
-
?
NKLKPSQ + H2O
?
show the reaction diagram
-
-
-
?
NKLKPSQWI + H2O
?
show the reaction diagram
-
-
-
?
NKLKPSQWISL + H2O
?
show the reaction diagram
-
-
-
?
NKLKPSQWISLSD + H2O
?
show the reaction diagram
-
-
-
?
o-aminobenzoyl-FDK-(dinitrophenyl)-P-OH + H2O
o-aminobenzoyl-FD + K-(dinitrophenyl)-P-OH
show the reaction diagram
-
-
-
?
o-aminobenzoyl-FRK-(dinitrophenyl)-P-OH + H2O
o-aminobenzoyl-FR + K-(dinitrophenyl)-P-OH
show the reaction diagram
-
-
-
?
o-aminobenzoyl-GFSPFAQ-(N-2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoyl-GFSPFA + Gln-(N-2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
o-aminobenzoyl-GFSPFEQ-(N-2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoyl-GFSPFE + Gln-(N-2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
o-aminobenzoyl-GFSPFFQ-(N-2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoyl-GFSPFF + Gln-(N-2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
o-aminobenzoyl-GFSPFLQ-(N-2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoyl-GFSPFL + Gln-(N-2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
o-aminobenzoyl-GFSPFQQ-(N-2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoyl-GFSPFQ + Gln-(N-2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
o-aminobenzoyl-GFSPFRA-(N-2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoyl-GFSPFR + Ala-(N-2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
o-aminobenzoyl-GFSPFRF-(N-2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoyl-GFSPFR + Phe-(N-2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
o-aminobenzoyl-GFSPFRI-(N-2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoyl-GFSPFR + Ile-(N-2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
o-aminobenzoyl-GFSPFRN-(N-2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoyl-GFSPFR + Asn-(N-2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
o-aminobenzoyl-GFSPFRQ-(N-2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoyl-GFSPFR + Gln-(N-2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
o-aminobenzoyl-GFSPFRR-(N-2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoyl-GFSPFR + Arg-(N-2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
o-aminobenzoyl-GFSPFRS-(N-2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoyl-GFSPFR + Ser-(N-2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
o-aminobenzoyl-GFSPFSQ-(N-2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoyl-GFSPFS + Gln-(N-2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
-
-
?
o-aminobenzoyl-Phe-Arg-Lys(2,4-dinitrophenyl)-Pro-hydroxide + H2O
?
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-SDK-(dinitrophenyl)-P-OH + H2O
o-aminobenzoyl-SD + K-(dinitrophenyl)-P-OH
show the reaction diagram
-
-
-
?
o-aminobenzoyl-SRK-(dinitrophenyl)-P-OH + H2O
o-aminobenzoyl-SR + K-(dinitrophenyl)-P-OH
show the reaction diagram
-
-
-
?
o-aminobenzoyl-TDK-(dinitrophenyl)-P-OH + H2O
o-aminobenzoyl-TD + K-(dinitrophenyl)-P-OH
show the reaction diagram
-
-
-
?
o-aminobenzoyl-TRK-(dinitrophenyl)-P-OH + H2O
o-aminobenzoyl-TR + K-(dinitrophenyl)-P-OH
show the reaction diagram
-
-
-
?
o-aminobenzoyl-YDK-(dinitrophenyl)-P-OH + H2O
o-aminobenzoyl-YD + K-(dinitrophenyl)-P-OH
show the reaction diagram
-
-
-
?
o-aminobenzoyl-YRK-(dinitrophenyl)-P-OH + H2O
o-aminobenzoyl-YR + K-(dinitrophenyl)-P-OH
show the reaction diagram
-
-
-
?
p-hydroxyhippuryl-His-Leu + H2O
?
show the reaction diagram
-
-
-
?
p-nitrobenzyloxycarbonyl-Gly + H2O
?
show the reaction diagram
-
-
-
-
?
p-nitrobenzyloxycarbonyl-Gly-Gly-Gly + H2O
?
show the reaction diagram
-
-
-
-
?
Phe-Gly-Gly-Phe + H2O
Phe-Gly + Gly-Phe
show the reaction diagram
-
-
-
?
physalaemin + H2O
pGlu-Ala-Asp-Pro-Asn-Lys-Phe-Tyr-Gly + Leu-Met-NH2
show the reaction diagram
-
degraded by striatal and by lung enzyme
-
-
?
Pro-(NO2)Phe-His-Leu + H2O
Pro-(NO2)Phe + His-Leu
show the reaction diagram
-
-
-
-
?
SLKPSNWLTPSE + H2O
?
show the reaction diagram
-
-
-
?
tert-butoxycarbonyl-Phe-Ala-Pro + H2O
tert-butoxycarbonyl-Phe + Ala-Pro
show the reaction diagram
-
-
-
-
?
tert-butoxycarbonyl-Phe-Phe-Gly + H2O
tert-butoxycarbonyl-Phe + Phe-Gly
show the reaction diagram
-
-
-
-
?
Tyr-Gly-Gly + H2O
Tyr + Gly-Gly
show the reaction diagram
-
-
-
-
?
Tyr-Gly-Gly-Phe-Leu + H2O
Tyr-Gly-Gly + Phe-Leu
show the reaction diagram
-
-
-
?
Tyr-Gly-Gly-Phe-Met + H2O
Tyr-Gly-Gly + Phe-Met
show the reaction diagram
-
-
-
?
Tyr-Gly-Gly-Phe-Met-Arg-Gly-Leu + H2O
Tyr-Gly-Gly-Phe-Met-Arg + Gly-Leu
show the reaction diagram
-
-
-
-
?
Tyr-Ile-His-Pro-(NO2)Phe-His-Leu + H2O
Tyr-Ile-His-Pro-(NO2)Phe + His-Leu
show the reaction diagram
-
-
-
-
?
Z-Phe-His-Leu + H2O
Z-Phe + His-Leu
show the reaction diagram
-
-
-
-
?
Z-phenylalanyl-histidyl-leucine + H2O
Z-phenylalanine + histidyl-leucine
show the reaction diagram
-
-
-
-
?
[Arg10]angiotensin I + H2O
?
show the reaction diagram
-
-
-
-
?
[D-Ala2,Leu5]enkephalin + H2O
Tyr-D-Ala-Gly + Phe-Leu
show the reaction diagram
-
-
-
-
?
[Leu5]enkephalin + H2O
?
show the reaction diagram
-
-
-
-
?
[Leu5]enkephalinamide + H2O
?
show the reaction diagram
-
-
-
-
?
[Met5]enkephalin + H2O
?
show the reaction diagram
-
-
-
-
?
[Met5]enkephalinamide + H2O
?
show the reaction diagram
-
-
-
-
?
[Phe9,Arg10]angiotensin I + H2O
?
show the reaction diagram
-
-
-
-
?
[Phe9]angiotensin I + H2O
?
show the reaction diagram
-
-
-
-
?
MKRSRGPSPRR + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
-
-
-
-
additional information
?
-
-
no cleavage of imido-bonds. No hydrolysis of angiotensin II and angiotensin III
-
?
additional information
?
-
-
potential role of follicular enzyme in early stages of follicular maturation and atresia
-
-
-
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
?
-
-
may contribute to elevated blood pressure in hypertensive disease via conversion of angiotensin I to angiotensin II or inactivation of bradykinin
-
-
-
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
?
-
-
plays a role in blood pressure regulation
-
-
-
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
?
-
P12821
somatic angiotensin I-converting enzyme plays a central role in blood pressure regulation
-
-
-
additional information
?
-
P12820
ACE is a key regulator of blood pressure homeostasis
-
-
-
additional information
?
-
-
ACE may influence trypsin biosynthesis in the larval gut by interacting with a trypsin-modulating oostatic factor
-
-
-
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
?
-
-
ACE degrades bradykinin, other vasoactive peptides, and activates angiotensin
-
-
-
additional information
?
-
Q10714
AnCE is a single domain protein with ACE activity, an ACE homologue
-
-
-
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 is a dipeptidyl carboxypeptidase
-
-
-
additional information
?
-
-
ACE structure-activity relationship, overview
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
amyloid beta-peptide(1-40) + H2O
amyloid beta-peptide(1-7) + amyloid beta-peptide(8-40)
show the reaction diagram
-
cleavage at the Asp7-Ser9 bond. Compared with amyloid beta-peptide(1-40), aggregation and cytotoxic effects of the degradation products amyloid beta-peptide(1-7) and amyloid beta-peptide(8-40) are reduced ot virtually absent. The enzyme inhibits aggregation, deposition, and cytotoxicity of amyloid beta-peptide in vitro may affect susceptibility to Alzheimers disease
-
?
amyloid beta-protein 1-40 + H2O
amyloid beta-peptide(1-7) + amyloid beta-peptide(8-40)
show the reaction diagram
-
ACE cleaves amyloid beta-protein 1-40 between Asp7 and Ser8
-
-
?
amyloid beta-protein 1-42 + H2O
amyloid beta-protein 1-420 + ?
show the reaction diagram
-
angiotensin-converting enzyme converts amyloid beta-protein 1-42 to amyloid beta-protein1-40. ACE regulates Abeta1-42/Abeta1-40 ratio in vivo by converting secreted Abeta1-42 to Abeta1-40 and degrading Abetas.The upregulation of ACE activity can be a novel therapeutic strategy for Alzheimers disease
-
-
?
amyloid beta-protein 1-42 + H2O
amyloid beta-protein 1-420 + ?
show the reaction diagram
-
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 Alzheimers disease
-
-
?
amyloid beta-protein 1-42 + H2O
amyloid beta-peptide(1-40) + amyloid beta-peptide(41-42)
show the reaction diagram
-
ACE cleaves amyloid beta-protein 1-42 at multiple sites
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
show the reaction diagram
-
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
show the reaction diagram
-
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
show the reaction diagram
P47820
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
show the reaction diagram
-
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
show the reaction diagram
-
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
show the reaction diagram
-
enzyme plays a major role in blood pressure regulation
-
?
angiotensin I + H2O
angiotensin II + His-Leu
show the reaction diagram
-
the enzyme plays an important role in blood pressure homeostasis
-
?
angiotensin I + H2O
angiotensin II + His-Leu
show the reaction diagram
-
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
show the reaction diagram
-
i.e. DRVYIHPFHL
i.e. DRVYIHPF
-
?
angiotensin I + H2O
angiotensin II + His-Leu
show the reaction diagram
-
i.e. DRVYIHPFHL
i.e. DRVYIHPF
-
?
angiotensin I + H2O
angiotensin II + L-His-L-Leu
show the reaction diagram
-
-
-
-
?
angiotensin I + H2O
angiotensin II + L-His-L-Leu
show the reaction diagram
-
-
-
-
?
angiotensin I + H2O
angiotensin II + L-His-L-Leu
show the reaction diagram
P12820
-
-
-
?
angiotensin I + H2O
angiotensin II + L-His-L-Leu
show the reaction diagram
-
-
-
-
?
angiotensin I + H2O
angiotensin II + L-His-L-Leu
show the reaction diagram
-
-
-
-
?
angiotensin I + H2O
angiotensin II + L-His-L-Leu
show the reaction diagram
-
-
-
-
?
angiotensin I + H2O
angiotensin II + L-His-L-Leu
show the reaction diagram
-
-
-
-
?
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met-NH2 + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
-
-
-
?
Bradykinin + H2O
?
show the reaction diagram
-
-
-
-
?
Bradykinin + H2O
?
show the reaction diagram
P12820
-
-
-
?
Bradykinin + H2O
?
show the reaction diagram
-
degradation
-
-
?
Bradykinin + H2O
?
show the reaction diagram
-
inactivation
-
-
?
Bradykinin + H2O
?
show the reaction diagram
-
bradykinin is a nonapeptide released from high molecular weight kininogen, it exerts its vasodilatory effect mainly by stimulation of B2 receptors
-
-
?
bradykinin + H2O
L-Phe-L-Arg + L-Ser-L-Pro + L-Arg-L-Pro-L-Pro-Gly-L-Phe
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
-
-
-
-
additional information
?
-
-
potential role of follicular enzyme in early stages of follicular maturation and atresia
-
-
-
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
?
-
-
may contribute to elevated blood pressure in hypertensive disease via conversion of angiotensin I to angiotensin II or inactivation of bradykinin
-
-
-
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
?
-
-
plays a role in blood pressure regulation
-
-
-
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
?
-
P12821
somatic angiotensin I-converting enzyme plays a central role in blood pressure regulation
-
-
-
additional information
?
-
P12820
ACE is a key regulator of blood pressure homeostasis
-
-
-
additional information
?
-
-
ACE may influence trypsin biosynthesis in the larval gut by interacting with a trypsin-modulating oostatic factor
-
-
-
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
?
-
-
ACE degrades bradykinin, other vasoactive peptides, and activates angiotensin
-
-
-
additional information
?
-
Q10714
AnCE is a single domain protein with ACE activity, an ACE homologue
-
-
-
additional information
?
-
-
complex formation witht e bradykinin B2 receptor
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
CaCl2
-
activates in absence of Cl-, maximal activity at 0.3 mM
Cl-
-
the activity of the C-domain of sACE depends highly on chloride ion concentration and is inactive in its absence, whereas the N-domain can be completely activated at relatively low concentrations of this anion and is still active in the absence of chloride
Co2+
-
activation
Co2+
-
CoCl2 stimulates
Co2+
-
activation
CoCl2
-
0.1-1.0 mM, 2fold activation
KBr
-
activation is lower than with NaCl
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
Na2SO4
-
activates in absence of Cl-
NaCl
-
activates in absence of Cl-
NaCl
-
maximal activation at 20 mM NaCl, hydroysis of angiotensin I; maximal activation at 620 mM NaCl, hydrolysis of hippuryl-His-Leu
NaCl
-
stimulates hydrolysis of hippuryl-His-Leu in concentration-dependent manner between 0 and 300 mM
NaCl
-
activates
NaCl
-
activates
NaCl
-
required
NaCl
-
activates
NaCl
-
required
NaCl
-
500 mM, 50% inhibition
NaF
-
activation is lower than with NaCl
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
Zinc
-
contains approximately one molar equivalent of bound zinc
Zinc
-
contains 0.9 gatom of zinc per mol of enzyme
Zinc
-
contains 1.2 gatom of zinc per mol of enzyme
Zinc
-
contains 0.8 gatom of zinc per mol of enzyme
Zinc
-
required
Zinc
-
0.3 mM ZnCl2 completely reverses the inhibition caused by 0.1 mM EDTA
Zinc
-
contains approximately 1 gatom of zinc per mol of enzyme
Zinc
-
contains approximately 1 gatom of zinc per mol of enzyme
Zinc
-
contains approximately 1 gatom of zinc per mol of enzyme
Zinc
-
a single Zn atom is bound per molecule of enzyme
Zinc
-
contains zinc
Zinc
-
contains zinc
Zinc
-
contains zinc
Zn2+
-
a highly ordered Zn2+ is bound at the active site
Zn2+
-
contains zinc
Zn2+
-
zinc metallopeptidase
Zn2+
-
-
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
Zn2+
-
activates
Zn2+
-
catalytically important
Zn2+
-
ACE is a zinc-metalloprotease
KI
-
activation is lower than with NaCl
additional information
-
enzyme is not affected by addition of 0.1-1.0 mM CaCl2, Mn2Cl2, MgCl2 or 0.1 mM ZnCl2
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(+)-catechin
-
IC50: about 1.6 mM
(-)-epicatechin
-
IC50: about 1.7 mM
(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-(3-methoxyphenyl)-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
-
-
(2E)-3-(4-methoxyphenyl)-1-(3,4,5-trimethoxyphenyl)prop-2-en-1-one
-
-
(2E)-3-phenyl-1-(3,4,5-trimethoxyphenyl)prop-2-en-1-one
-
-
(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]-(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
Q9BYF1
;
(2S)-2-[[(2S)-2-mercapto-3-methylpentanoyl]amino]-3-(2-naphthyl)propanoic acid
-
;
(2S)-2-[[(2S)-2-mercapto-3-methylpentanoyl]amino]-3-phenylpropanoic acid
Q9BYF1
;
(2S)-2-[[(2S)-2-mercapto-3-methylpentanoyl]amino]propanoic acid
Q9BYF1
;
(2S)-3-(4-hydroxyphenyl)-2-[[(2S)-2-mercapto-3-methylpentanoyl]amino]propanoic acid
Q9BYF1
;
(2S)-3-biphenyl-2-yl-2-[[(2S)-3-methyl-2-sulfanylpentanoyl]amino]propanoic acid
-
;
(2S)-3-biphenyl-3-yl-2-[[(2S)-3-methyl-2-sulfanylpentanoyl]amino]propanoic acid
-
;
(2S)-3-biphenyl-4-yl-2-[(2-mercapto-2-methylpropanoyl)amino]propanoic acid
Q9BYF1
;
(2S)-3-biphenyl-4-yl-2-[(mercaptoacetyl)amino]propanoic acid
Q9BYF1
;
(2S)-3-biphenyl-4-yl-2-[[(2S)-2-mercaptobutanoyl]amino]propanoic acid
Q9BYF1
;
(2S)-3-biphenyl-4-yl-2-[[(2S)-2-mercaptopropanoyl]amino]propanoic acid
Q9BYF1
;
(2S)-3-biphenyl-4-yl-2-[[(2S)-3-methyl-2-sulfanylpentanoyl]amino]propanoic acid
-
;
(5S)-5-[(N-benzoyl)-amino]-4-oxo-6-phenyl-hexanoyl-L-phenylalanine
-
phosphinic peptide inhibitor kAF
(5S)-5-[(N-benzoyl)amino]-4-oxo-6-phenylhexanoyl-L-phenylalanine
-
the inhibitor has a 30fold higher affinity for the C domain than for the N domain of ACE
(5S)-5-[(N-benzoyl)amino]-4-oxo-6-phenylhexanoyl-L-tryptophan
-
the inhibitor shows strong C domain selectivity, having almost 1300-fold greater affinity for the C domain than for the N domain of ACE
(5S)-5-[(N-benzoyl)amino]-4-oxo-6-phenylhexanoyl-L-tryptophan
-
phosphinic peptide inhibitor kAW
(pE)WPRPQIPP
-
-
1,10-phenanthroline
-
5.0 mM, complete inhibition
1,10-phenanthroline
-
-
1,10-phenanthroline
-
-
1,10-phenanthroline
-
-
1,10-phenanthroline
-
-
1,10-phenanthroline
-
-
1-cyclohexyl-3-(2-morpholinoethyl)carbodiimide metho-p-toluene sulfonate
-
20 mM, 99.6% inhibition
1-Fluoro-2,4-dinitrobenzene
-
1 mM, 96% inhibition of N-domain ACE
1-Fluoro-2,4-dinitrobenzene
-
1 mM, 31% inhibition
1-methyl-5-phenyl-3-(3,4,5-trimethoxyphenyl)-4,5-dihydro-1H-pyrazole
-
-
1-[(5S)-4-oxo-6-phenyl-5-[(phenylcarbonyl)amino]hexanoyl]-L-proline
P12821
-
1-[(5S)-5-[(tert-butoxycarbonyl)amino]-4-oxo-6-phenylhexanoyl]-L-proline
P12821
-
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
2,3-butendione
-
10 mM, 97.4% inhibition
2,3-Dimercapto-1-propanol
-
-
2-(benzyloxy)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-phenylalanine
-
;
2-hydroxyemodin 1-methylether
-
47.52% inhibition at 1.63 ng/ml
2-mercaptoethanol
-
-
2-mercaptoethanol
-
-
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
3-(benzyloxy)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-phenylalanine
-
;
3-mercapto-2-D-methylpropanoyl-L-Pro
-
i.e. SQ-14,225
3-p-acetyl-aminophenylpropionate
-
-
3-p-aminophenylpropionate
-
-
3-Phenylpropionate
-
-
4-phenylbutyrate
-
-
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
-
-
8-hydroxyquinoline
-
-
9-[1-carboxy-3-(4-hydroxyphenyl)propylamino]octahydro-10-oxo-6H-pyridazo[1,2-a][1,2]diazepine-1-carboxylic acid
-
-
-
A 58365A
-
-
A 58365B
-
-
Ac-FKCRRWQWRMKKLGA-NH2
-
0.02 mM, 38% loss of activity with hippuryl-His-Leu, 41% loss of activity with angiotensin I
Ac-RKKPFW-NH2
-
0.02 mM, 24% loss of activity with hippuryl-His-Leu
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-RKWRFW-NH2
-
0.02 mM, 3% 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
acetate
-
-
Acetyl-Ala-Ala-Ala
-
hydrolysis of hippuryl-His-Leu
Acetyl-Ala-Ala-Ala-Ala
-
hydrolysis of hippuryl-His-Leu
acidic protease
-
about 80% ACE inhibitory
-
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-Ala
-
hydrolysis of hippuryl-His-Leu
Ala-Ala
-
-
Ala-Ala
-
inhibits hydrolysis of Gly-Ala-Ala
Ala-Ala-Ala
-
hydrolysis of hippuryl-His-Leu
Ala-Ala-Ala-Ala
-
hydrolysis of hippuryl-His-Leu
Ala-Gly-Ser
-
-
Ala-Gly-Ser-Pro
-
-
Ala-Gly-Ser-Ser
-
-
Ala-His-Ser-Tyr
-
a noncompetitive inhibitor, the peptide is resistant to further degenration by pepsin, trypsin, and chymotrypsin
Ala-Leu-Pro-His-Ala
-
-
Ala-Pro-Gly-Ala-Gly-Val-Tyr
-
-
Ala-Trp
-
IC50: 0.0064 mM, non-competitive
Ala-Trp-Pro-Phe
-
-
Ala-Val-Val
-
-
alaternin
-
24.26% inhibition at 1.63 ng/ml
alcacepril
-
synthetic ACE inhibitor and antihypertensive drug
alcalase
-
about 20% ACE inhibitory
-
aliphatic monocarboxylates
-
degree of inhibition increases in proportion to their chain length up to C14
-
aminoethyl-chitin
-
with 10%, 50%, and 90% deacetylation
ancovenin
-
-
angiotensin converting enzyme inhibitor
-
ACE-I, inhibition is impacting both the renin-angiotensin cascade and the degradation metabolism of bradykinin, inhibition mechanism, overview. ACE-I is used as therapeutic agent in congestive heart failure, diabetic nephropathy, hypertension, and coronary artery disease. ACE-I medications can induce chronic cough, hypotension, hyperkalemia, bone marrow depression, angioedema, and rarely, hepatic failure. Angioedema involves a subcutaneous swelling reaction that evolves over several hours and is not associated with itching or pain, pathomechanism, detailed overview
-
angiotensin I
-
-
angiotensin I
-
-
angiotensin I converting enzyme inhibitory peptides
-
from wheat milling byproducts by proteolysis through aspartic proteases, optimally produced at pH 3.2. Milled whole grain, bran, shorts, and red dog acquire ACE inhibitory activity though water soaking treatment, preparation of shorts exhibits the strongest inhibitory activity with an IC50 value of 0.08 mg/ml, overview
-
angiotensin I-converting enzyme inhibitory peptides
-
i.e. ACE-Is, from enzymatic hydrolysates of cuttlefish, Sepia officinalis, muscle proteins, generated by the crude enzyme from Bacillus mojavensis A21, show 87.11% inhibition at 2 mg/ml, mass spectrometric analysis, overview
-
angiotensin II
-
hydrolysis of hippuryl-His-Leu
angiotensin II
-
-
angiotensin II
-
-
angiotensin II
-
inhibits hydrolysis of angiotensin I and Gly-Ala-Ala
angiotensin II
-
-
angiotensin II
-
-
Angiotensin III
-
-
angiotensin IV
-
IC50: 0.07 mM
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
-
angiotensin-I converting enzyme inhibitory peptides
-
activity of hydrolysates, using diverse proteases, from Avena sativa proteins by in silico and in vitro analyses, peptide sequencing, overview
-
antipain
-
0.1 mg/ml, 26% inhibition
Arg-Ala
-
hydrolysis of hippuryl-His-Leu
Arg-Met-Leu
-
IC50: 1.019 mM, competitive inhibition
Arg-Phe
-
IC50: 4.365 mM
Arg-Pro-Pro
-
hydrolysis of hippuryl-His-Leu
Arg-Pro-Pro
-
inhibition of enzyme form I and II, enzyme form III is not inhibited
Arg-Pro-Pro
-
more inhibitory at pH 8 than at pH 6
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
-
hydrolysis of hippuryl-His-Leu
Asn-Trp-Gly-Pro-Leu-Val
-
-
Asp-Ala
-
hydrolysis of hippuryl-His-Leu
Asp-Asp-Thr-Gly-His-Asp-Phe-Glu-Asp-Thr-Gly-Glu-Ala-Met
-
an inhibitory peptide from the marine rotifer, Brachionus rotundiformis
Asp-Ile-Gly-Tyr-Tyr
-
-
Asp-Leu-Pro
-
-
Asp-Phe-Gly
-
-
Asp-Tyr-Gly-Leu-Tyr-Pro
-
-
Asp-Tyr-Val-Gly-Asn
-
-
aspergillomarasmine A
-
-
aspergillomarasmine B
-
-
benazepril
-
induces isolated visceral angioedema: a rare and under diagnosed adverse effect of angiotensin converting enzyme inhibitors
benazepril
-
treatment with angiotensin-converting enzyme inhibitors is of benefit in reducing the progression of renal damage in young patients with moderately proteinuric IgA nephropathy
benazepril
-
-
benzapril
-
-
benzenesulfonate
-
-
Benzoate
-
-
benzoyl-NHCOCH2CH(COOH)-Ala-Pro-OH
-
-
benzoyl-NHCOCH2CH(COOH)-Trp-Pro-OH
-
-
benzyloxycarbonyl-PhePSI[PO2-CH]Ala-Ala
-
-
benzyloxycarbonyl-PhePSI[PO2-CH]Ala-Trp
-
-
Bothrops bradykinin potentiating peptides
-
-
-
bradykinin
-
-
bradykinin potentating factor nonapeptide
-
-
-
bradykinin potentiating peptide
-, Q4KXL2
i.e. BPP1 or pGlu-Trp-Pro-Arg-Pro-Gln-Ile-Pro-Pro
-
bradykinin potentiator B
-
-
bradykinin potentiator C
-
-
bradykinin potentiator C
-
inhibition of enzyme form I and II, enzyme form III is not inhibited
Bradykinin-potentiating factor SQ 20881
-
-
bradykinin-potentiating peptide 9a
-
-
bradykinin-potentiator B
-
-
bradykinin-potentiator C
-
-
caffeic acid
-
IC50: about 1.7 mM
caffeoyl acetate
-
-
Captopril
-
0.1 mM, complete inhibition
Captopril
-
inhibition study by capillary electrophoresis
Captopril
-
0.00002 mM
Captopril
-
lipophilic ACE inhibitors quinapril, enalapril, and captopril increase the survival and lifetime of rats with experimental chronic heart failure
Captopril
-
the angiotensin-converting enzyme inhibitor, promotes growth of immunogenic tumors in mice
Captopril
-
plasma angiotensin converting enzyme inhibitors
Captopril
-
the relative potency of the inhibitors in the order of decreasing efficieny is: enalaprilat, lisinopril, captopril. The thermodynamic behaviour of the binding process is analyzed
Captopril
-
hyperalgesic effect
Captopril
-
it is likely that prevention of angiotensin II receptor stimulation is a major mechanism underlying the inhibition of myosin-induced myocarditis by captopril
Captopril
-
angiotensin-converting enzyme inhibition confers renoprotection in adriamycin nephropathy by reducing intrarenal angiotensin II and augmenting expression of N-acetylseryl-aspartyl-lysyl-proline that together attenuate signaling of mitogen-activated protein kinase and its downstream proinflammatory and fibrinogenic properties
Captopril
-
the anngiotensin converting enzyme inhibitor captopril modifies conditioned place preference induced by morphine and morphine withdrawal signs in rats
Captopril
-
i.e. D-3-mercapto-2-methyl-propionyl-L-proline, 80.5% inhibition at 0.005 mg/mg in L6 larvae
Captopril
-
87.87% inhibition at 1.63 ng/ml
Captopril
-
-
Captopril
-
inhibits in vivo and reduces the blood glucose level, but not the plasma insulin level
Captopril
-
ACE inhibition during pregnancy and lactation in adult offspring rats induces behavioural changes, e.g. in the open field test, overview
Captopril
-
98.5% inhibition at 0.2 mM
Captopril
-
microarray gene expression profiling of the aorta during atherosclerosis prevention with the ACE inhibitor, overview. Captopril treatment for 7 months strongly decreases the recruitment of proatherogenic immune cells into the aorta. Captopril-mediated inhibition of plaque infiltrating immune cells involves downregulation of the C-C chemokine receptor 9, CCR9, phenotype and physiological mechanism, overview
Captopril
-, Q4KXL2
binding mode, molecular docking, detailed overview
Captopril
-
synthetic ACE inhibitor and antihypertensive drug
Captopril
-
the ACE inhibitor shows best renoprotective effect in patients with renal disease
Captopril
-
competitive, of great value for use in chronic therapy of human hypertensive disease
Captopril
-
i.e. D-(3-mercapto-2-methylpropanoyl)-L-Pro
Captopril
-
i.e. D-(3-mercapto-2-methylpropanoyl)-L-Pro
Captopril
-
i.e. SQ 14225
Captopril
-
i.e. SQ 14225
Captopril
-
-
catechin
-
IC50: 1.593 mM, competitive
CGS-35066
-
-
chitooligosaccharide derivatives
-
i.e. COS, chitosan derivatives, polycationic polymers comprised principally of glucosamine units, generated via either chemical or enzymatic hydrolysis of chitosan. ACE inhibitory activity of hetero-COS, derived from crab chitin, is dependent on the degree of deacetylation of chitosan
-
chitosan trimer
-
effective in lowering blood pressure
chloramine-T
-
50 mM, 97.1% inhibition
chlorogenic acid
-
IC50: about 1.8 mM
chlorogenic acid
-
-
cilazapril
-
-
citrate
-
-
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
Co2+
-
testicular enzyme is inhibited, lung enzyme not
concanavalin A
-
-
-
CuCl2
-
73% inhibition at 0.1 mM, 99% inhibition at 1.0 mM
cyanide
-
-
cyanidin-3-O-beta-D-glucoside
-
isolated from flower buds of Rosa damascena. Metal ions might be involved in the inhibition
cyanidin-3-O-sambubioside
-
an anthocyanin isolated from Hibiscus sabdariffa calyces, competitive ACE inhibition reducing blood pressure in humans, IC50 is 0.0684 mg/ml
D-3-thio-2-methylpropanoyl-Pro
-
-
D-Cys-L-Pro
-
competitive to hippuryl-His-Leu
D-Mannitol
-
IC50: 3 mg/ml
D-Mannitol
-
antihypertensive effect in spontaneously hypertensive rats by oral administration
delphinidin-3-O-sambubioside
-
an anthocyanin isolated from Hibiscus sabdariffa calyces, competitive ACE inhibition reducing blood pressure in humans, IC50 is 0.0845 mg/ml
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
dieckol
-
deribed from Ecklonia stolonifera
diethyl dicarbonate
-
10 mM, 92.8% inhibition
dimethyl phosphate
-
-
diphosphate
-
-
dithiothreitol
-
-
DQVFPMNPPK
-
-
eckol
-
derived from Ecklonia stolonifera
EDTA
-
10 mM, complete inhibition of hydrolysis of o-aminobenzoyl-SDK-(dinitrophenyl)-P-OH and o-aminobenzoyl-FRK-(dinitrophenyl)-P-OH of wild-type enzyme, N-domain and C-domain
EDTA
-
1.0 mM, complete inhibition
EDTA
-
recombinant enzyme, restored by ZnSO4
EDTA
-
somewhat more effective at pH 6 than at pH 8
Ellagic acid
-
IC50: 0.4 mM
emodin
-
45.79% inhibition at 1.63 ng/ml
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
-
angioedema is a rare but potentially life-threatening adverse effect of angiotensin-converting enzyme inhibitors. Angioedema due to angiotensin-converting enzyme inhibitors usually appears during the first weeks of treatment. Late-onset anioedema is often unrecognized
enalapril
-
the angiotensin-converting enzyme inhibitor has no effect on the rate of endothelial apoptosis in vitro in HUVEC cells
enalapril
-
the angiotensin-converting enzyme inhibitor has no significant effect on apoptosis induced via endotoxic shock with Escherichia coli lipopolysaccharides
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
-
plasma angiotensin converting enzyme inhibitors
enalapril
-
standing and supine blood pressure decreases significantly in both autosomal-dominant polycystic kidney disease patients and controls after the administration of enalapril on low and high-sodium intakes, with no differences between the two groups
enalapril
-
i.e. ((S)-1-ethoxycarbonyl-3-phenylpropyl)-L-alanyl-L-proline, 74.9% inhibition at 0.005 mg/mg in L6 larvae
enalapril
-
-
enalapril
-
-
enalapril
-
synthetic ACE inhibitor and antihypertensive drug
enalapril
-
inhibits corneal angiogenesis in vivo, enalapril treatment causes a notable decrease in corneal neovascularization, and enalapril-treated rabbit corneas showing a lesser degree of blood vessel staining for collagen type IV and lectin, overview
enalapril
-
i.e. (2S)-1-[(2S)-2-[(2S)-1-ethoxy-1-oxo-4-phenylbutan-2-yl]aminopropanoyl]pyrrolidine-2-carboxylic acid
enalaprilat
-
-
enalaprilat
-
the relative potency of the inhibitors in the order of decreasing efficieny is: enalaprilat, lisinopril, captopril. The thermodynamic behaviour of the binding process is analyzed
enalaprilat
Q10714
-
enalaprilat
-
inhibits ACE and the bradykinin degradation in vivo, which is reversed by insulin
enalaprilate
-
bradykinin receptor 2 (BDKRB2) BE1 polymorphism influences bradykinin type 2 receptor mediated vasodilation during angiotensin-converting enzyme inhibition
enalaprilate
-
-
enalaprilate
-
-
enalaprilate
-
-
enalaprilate
-
no inhibition
enaprilat
-
-
-
enaprilat
-
-
-
enaprilat
-
i.e. N-[(S)-1-carboxy-3-phenylpropyl]-Ala-Pro
-
enaprilat
-
-
-
epicatechin
-
IC50: 1.781 mM, competitive
epicatechin dimer
-
IC50: 0.267 mM, competitive
epicatechin hexamer
-
IC50: 0.01 mM, competitive
epicatechin pentamer
-
IC50: 0.025 mM, competitive
epicatechin tetramer
-
IC50: 0.012 mM, competitive
epicatechin trimer
-
IC50: 0.126 mM, competitive
epigallocatechin
-
IC50: about 0.3 mM
ESIINF
-
the inhibitor produces an acute blood-pressure-lowering effect in spontaneously hypertensive rats upon a single oral administration
ethyl caffeate
-
0.01 mg/ml, 32.4% inhibition
EtOAc extract of Rabdosia coetsa
-
angiotensin-converting enzyme inhibitory activity
-
flavanol
-
flavanols either isolated or present in foods can inhibit enzyme activity
flavourzyme
-
about 20% ACE inhibitory
-
foroxymithine
-
-
fosinopril
-
administered as a prodrug and then rapidly converted by the liver and the gastrointestinal mucosa to the active form fosinoprilat
fosinopril
-
causes a significant decrease in plasminogen activator inhibitor 1, PAI-1, levels, probably by aldosterone escape
Gallic acid
-
IC50 : about 1.7 mM
gastrin I
-
-
-
genistein
-
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
Glu-Trp-Pro-Arg-Pro-Gln-Ile-Pro-Pro
-
-
gluco-aurantioobtusin
-
competitive inhibitor, 137.62% inhibition at 1.63 ng/ml
Gly-Asp-Ala-Pro
-
-
Gly-Gln
-
IC50: 5.63 mM, competitive inhibition
Gly-Glu-Pro
-
-
Gly-Gly-Val-Ile-Pro-Asn
-
-
Gly-His-Gly
-
-
Gly-L-Ala-Hyp-Gly-L-Leu-Hyp-Gly-L-Pro
-
highest ACE-inhibitory activity
Gly-L-Ala-Hyp-Gly-L-Pro-L-Ala-Gly-L-Pro-Gly-Gly-L-Ile-Hyp-Gly-L-Glu-L-Arg-Gly
-
-
Gly-L-Ile-Hyp-Gly-L-Glu-L-Arg-Gly-L-Pro-L-Val-Gly-L-Pro-L-Ser-Gly
-
-
Gly-L-Leu-Hyp-Gly-L-Ser-L-Arg-Gly-L-Glu-L-Arg-Gly-L-Leu-Hyp-Gly
-
-
Gly-Leu-Pro
-
IC50: 1.62 mM
Gly-Phe
-
IC50: 10.471 mM
Gly-Phe-Hyp-Gly-Thr-Hyp-Gly-Leu-Hyp-Gly-Phe
-
IC50: 0.026 mM. Inhibitory peptide derived from chicken breast muscle
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
Gly-Pro
-
IC50: 252.63 mM
Gly-Pro-Ala
-
inhibits hydrolysis of Gly-Ala-Ala
Gly-Pro-Leu
-
IC50: 2.65 mM
Gly-Pro-Pro
-
-
Gly-Trp
-
IC50: 20.417 mM
Gly-Tyr
-
IC50: 5.495 mM
Gly-Val-His-His-Ala
-
-
glycinin hydrolysate
-
-
-
GQGGP
-
extraction and characterization of an ACE inhibitor from the fruiting body of Pholiota adiposa ASI 24012, which can be used as an antihypertensive drug
guanethidine
-
weak
H2S
-
Zn2+ but not Cd2+, Ca2+ or Mg2+ could counteract the inhibitory effect
HERDPTHIKWGD
-
IC50: about 0.008 mM. Production kinetics of angiotensin-I converting enzyme inhibitory peptides from bonito meat in artificial gastric juice
HERDPTHIKWGD
-
ACE inhibitor peptide B derived from water extracts of bonito protein, glyceraldehyde-3-phosphate dehydrogenase, hydrolysates, tandem multimer expression in and purification from Escherichia coli strain XL1-Blue and BL21(DE3), detailed overview
His-His-Leu
-
-
His-Leu
-
hydrolysis of hippuryl-His-Leu
His-Leu
-
-
His-Leu
-
inhibits hydrolysis of Gly-Ala-Ala
Hyp-Gly-Leu-Hyp-Gly-Phe
-
0.01 mM
Hyp-Gly-Phe
-
IC50: 0.433 mM
Hyp-Gly-Thr-Hyp-Gly-Leu-Hyp-Gly-Phe
-
0.019 mM
hyperosid
-
IC50: 0.2 mM
Ile-Ala-Tyr-Lys-Pro-Ala-Gly
-
-
Ile-Ala-Val
-
-
Ile-Asn-Ser-Gln
-
-
Ile-Gln-Pro
-
-
Ile-Glu-Pro
-
molecular docking analysis at the active site of testis ACE, overview
Ile-Glu-Pro
-
-
Ile-Glu-Tyr
-
molecular docking analysis at the active site of testis ACE, overview
Ile-Glu-Tyr
-
-
Ile-Lys-Pro
-
a potent competitive inhibitor, molecular docking analysis at the active site of testis ACE, overview
Ile-Lys-Pro
-
-
Ile-Lys-Pro-Leu-Asn-Tyr
-
-
Ile-Lys-Trp
-
molecular docking analysis at the active site of testis ACE, overview
Ile-Lys-Trp
-
-
Ile-Lys-Tyr
-
molecular docking analysis at the active site of testis ACE, overview
Ile-Lys-Tyr
-
-
Ile-Phe-Leu
-
-
Ile-Pro-Pro
-
casein hydrolysate containing VPP and IPP improves the vascular endothelial dysfunction in subjects with mild hypertension. The continuous intake of VPP and IPP could help to prevent cardiovascular diseases in hypertensive subjects
Ile-Pro-Pro-Gly-Val-Pro-Tyr
-
-
Ile-Pro-Pro-Gly-Val-Pro-Tyr-Trp-Thr
-
-
Ile-Thr-Phe
-
-
Ile-Trp
-
IC50: 0.0047 mM, non-competitive
-
Ile-Trp-His-His-Thr
-
-
Ile-Tyr-Leu-Leu
-
-
Ile-Val-Gly-Arg-Pro-Arg-His-Gln-Gly
-
-
Ile-Val-Tyr
-
-
imidapril
-
-
inhibitory peptides from rice dreg hydrolysate
-
significant antihypertensive action and no other side effects by oral administration in spontaneous hypertension rats
-
iodoMK-351A
-
-
-
isoacteoside
-
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
isoquercitrin
-
IC50: 0.3 mM
isorhamnetin-3-beta-glucopyranoside
-
IC50: 0.4089 mM
K-26
-
-
-
kaempferol
-
IC50: about 1.2 mM
kaempferol
-
dose-dependent inhibition, 46% inhibition at 0.1 mM
kaempferol-3-alpha-arabinopyranoside
-
IC50: 0.3928 mM
kaempferol-3-O-alpha-L-arabinopyranoside
-
-
kaempferol-3-O-beta-D-galactopyranoside
-
-
KAPVA
-
a peptide derived from muscle titin
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
L-681,176
-
-
L-Cys-L-Pro
-
-
L-Glu-L-Arg-L-Tyr-L-Pro-L-Ile
-
-
L-Ile-L-Pro-L-Phe
-
-
L-Leu-L-Pro-L-Phe
-
-
L-Met-L-Pro-L-Phe
-
-
L-Thr-L-Thr-L-Ile
-
-
L-Tyr-L-Thr-L-Ala-Gly-L-Val
-
-
L-Val-L-Asp-L-Phe
-
-
L-Val-L-Tyr
-
-
laurate
-
-
leptin
-
-
-
Leu-Ala
-
hydrolysis of hippuryl-His-Leu
Leu-Ala-Ile-pro-Val-Asn-Lys-Pro
-
-
Leu-Arg-Ile-Pro-Val-Ala
-
-
Leu-Arg-Pro
-
-
Leu-Gln-Pro
-
competitive
Leu-Gln-Pro
-
-
Leu-Gly-Ile
-
-
Leu-Gly-Pro
-
IC50: 0.72 mM
Leu-Ile-Tyr
-
i.e. acein-2, isolated from tryptic hydrolysate of human plasma, non-competitive inhibitor, IC50: 0.00082 mM.
Leu-Lys-Pro-Asn-Met
-
-
Leu-Lys-Tyr
-
competitive
Leu-Phe
-
IC50: 0.3832 mM, competitive
Leu-Pro-Gly
-
IC50: 5.73 mM
Leu-Trp
-
IC50: 0.0174 mM, non-competitive
Leu-Val-Tyr
-
competitive
Leupeptin
-
0.1 mg/ml, 18% inhibition
LFDKPVSPL
-
-
Lisinopril
-
the inhibitor binds in a highly ordered, extended conformation, with the phenyl group extended in an N-terminal direction and a lysine side chain parallel to the alpha13 helix containing the HEXXH zinc binding motif
Lisinopril
-
IC50: 1 nM
Lisinopril
-
tumor growth is significantly inhibited as measured by tumor weight
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
-
the relative potency of the inhibitors in the order of decreasing efficieny is: enalaprilat, lisinopril, captopril. The thermodynamic behaviour of the binding process is analyzed
Lisinopril
-
i.e. [(S)-1-carboxy-3-phenylpropyl]-L-lysyl-L-proline
Lisinopril
-
treatment with 75 mg/l lisinopril significantly reduces renal ACE activity without affecting renal ACE2 activity
Lisinopril
-
the compound shows a 4fold domain-selectivity for the C-domain compared to the N-domain. Active site binding structure, overview
Lisinopril
-
synthetic ACE inhibitor and antihypertensive drug
Lisinopril
-
i.e. N2-[(1S)-1-carboxy-3-phenylpropyl]-L-lysyl-L-proline, molecular docking analysis at the active site of testis ACE, PDB ID 1086, overview
Lisinopril
-
i.e. N2-[(1S)-1-carboxy-3-phenylpropyl]-L-lysyl-L-proline
Lisinopril
-
i.e. N-[(S)-1-carboxy-3-phenylpropyl]-L-Lys-L-Pro
Lisinopril
-
-
Lisinopril
-
no inhibition
lisW-S
-
a C-domain-selective derivative of the drug lisinopril. The compound shows a 258fold domain-selectivity for the C-domain compared to the N-domain, that is largely due to the co-operative effect of C-domain-specific residues in the S2' subsite. Interactions in the active site: comparison between N- and C-domain residues, overview
lisW-S
Q10714
lisinopril-tryptophan S-enantiomer, a C-domain human sACE specific inhibitor and antihypertensive drug
LRPARPTSPP
-
-
LRPARPTSPPA
-
-
luteolin-7-O-beta-D-glucopyranoside
-
-
Lys-Ala
-
hydrolysis of hippuryl-His-Leu
Lys-Ala-Phe-Arg
-
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
Lys-Asp-Tyr-Arg-Leu
-
-
Lys-Leu-Pro-Arg-Gly-Thr-Leu-Phe
-
-
malonate
-
-
melanoidin
-
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
-
Met-Arg-Trp
-
-
Met-Arg-Trp-Arg-Asp
-
-
Met-Trp
-
IC50: 0.0098 mM, non-competitive
methyl rosmarinate
-
0.01 mg/ml, 39.5% inhibition
Monascus-fermented soybean extract
-
butanol, ethyl acetate, 50% ethanol-soluble extract and water-soluble extract
-
mugineic acid
-
IC50: 0.00028 mM
muracein A
-
and SQ 28,370, the reduction product of muracein A
muracein A
-
-
muracein B
-
less potent inhibitor
muracein B
-
-
muracein C
-
less potent inhibitor
muracein C
-
-
N-(3-{[(1R)-1-{[(benzyloxy)carbonyl]amino}-2-phenylethyl](hydroxy)phosphoryl}-2-{[3-(biphenyl-4-yl)-4,5-dihydro-1,2-oxazol-5-yl]methyl}propanoyl)-L-tryptophan
-
-
N-alpha-[1-(S)-carboxy-3-phenylpropyl]-L-Lys-L-Pro
-
-
N-bromosuccinimide
-
2 mM, 99.8% inhibition
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
N-[(2S)-3-methyl-2-sulfanylpentanoyl]-2-phenoxy-L-phenylalanine
-
;
N-[(2S)-3-methyl-2-sulfanylpentanoyl]-3-phenoxy-L-phenylalanine
-
;
N-[(2S)-3-methyl-2-sulfanylpentanoyl]-O-phenyl-L-tyrosine
-
;
N-[(2S)-3-methyl-2-sulfanylpentanoyl]-O-[4-(trifluoromethyl)benzyl]-L-tyrosine
-
;
N-[(5S)-4-oxo-6-phenyl-5-[(phenylcarbonyl)amino]hexanoyl]-L-phenylalanine
P12821
-
N-[(5S)-4-oxo-6-phenyl-5-[(phenylcarbonyl)amino]hexanoyl]-L-tryptophan
P12821
-
N-[(5S)-5-[(tert-butoxycarbonyl)amino]-4-oxo-6-phenylhexanoyl]-L-phenylalanine
P12821
-
N-[(5S)-5-[(tert-butoxycarbonyl)amino]-4-oxo-6-phenylhexanoyl]-L-tryptophan
P12821
-
N-[(S)-1-(ethoxycarbonyl)-3-phenylpropyl]-L-alanyl-L-proline
-
i.e. MK 421. Effect of the inhibitor on the components of the renin system in healthy subjects : the drug has a prolonged duration of action and effectively reduces plasma converting enzyme activity, angiotensin II and aldosterone levels and thereby increases sodium diuresis
N-[(S)-1-Carboxy-3-phenylpropyl]-L-Ala-L-Pro
-
-
N-[1(S)-carboxy-5-aminopentyl]glycylglycine
-
weak competitive
N-[3-{[(1R)-1-{[(benzyloxy)carbonyl]amino}-2-phenylethyl](hydroxy)phosphoryl}-2-(biphenyl-4-ylmethyl)propanoyl]-L-tryptophan
-
-
N-{(2R)-3-{[(1R)-1-{[(benzyloxy)carbonyl]amino}-2-phenylethyl](hydroxy)phosphoryl}-2-[(3-phenyl-1,2-oxazol-5-yl)methyl]propanoyl}-L-tyrosine
-
-
N-{(2S)-3-{[(1R)-1-{[(benzyloxy)carbonyl]amino}-2-phenylethyl](hydroxy)phosphoryl}-2-[(3-phenyl-1,2-oxazol-5-yl)methyl]propanoyl}-L-tryptophan
-
-
N2-[(S)-1-carboxy-3-phenylpropyl]-L-lysyl-L-proline
-
effect of the inhibitor on the components of the renin system in healthy subjects : the drug has a prolonged duration of action and effectively reduces plasma converting enzyme activity, angiotensin II and aldosterone levels and thereby increases sodium diuresis
NaCl
-
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
-
concentration dependent inhibition of hippuryl-His-Leu between 0 and 100 mM
NaCl
-
500 mM, 50% inhibition
neutrase
-
about 70% ACE inhibitory
-
nicotianamine
-
IC50: 0.000085 mM
nicotianamine
-
mixed inhibition. The preferential inhibition of circulating and tissue angiotensin I-converting enzyme by nicotianamine can contribute to the suppression of hypertension
nicotianamine
-
-
nitrate
-
-
-
O-(2,4-difluorobenzyl)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-tyrosine
-
;
O-(3,4-difluorobenzyl)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-tyrosine
-
;
O-(4-fluorobenzyl)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-tyrosine
-
;
O-benzyl-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-tyrosine
-
;
O-[3,5-bis(trifluoromethyl)benzyl]-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-tyrosine
Q9BYF1
;
oenothein B
-
IC50: 0.25 mM
omapatrilat
-
-
omega-phenylalkylcarboxylates
-
-
-
oxalate
-
-
p-aminocinnamate
-
-
PCMB
-
1.0 mM, 42% inhibition
peimisine
-
IC50: 0.5265 mM
peimisine
-
an ACE inhibitory steroidal alkaloid from Fritillaria puqiensis, 20.2% inhibition at 0.2 mM
Pepsin
-
about 60% ACE inhibitory
-
peptide
-
more angiotensin I converting enzyme-inhibitory peptides are present in hydrolyzed wet-milled corn germ compared to hydrolyzed dry-milled germ
Peptide inhibitors
-
-
-
Peptides
-
purified from sunflower hydrolysate
Peptides
-
purified from sunflower hydrolysate or rapeseed hydrolysate
perindopril
-
in a murine hepatocellular carcinoma xenograft model perindopril suppresses hepatocellular carcinoma development and inhibits neovascularization
perindopril
-
the angiotensin-converting enzyme inhibitor has no effect on the rate of endothelial apoptosis in vitro in HUVEC cells
perindopril
-
chronic in vivo administration of the angiotensin-converting enzyme inhibitor reduces apoptosis induced via endotoxic shock with Escherichia coli lipopolysaccharides
perindopril
-
itssue angiotensin converting enzyme inhibitors
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
-
chronic administration of perindopril results in a decrease in body adiposity
perindopril
-
shows beneficial effects, independent of the presence of cardiovascular risk factors at baseline in all study groups, in patients after myocardial infarction and revascularization, detailed overview
perindopril
-
-
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
perindoprilat
-
-
perindoprilat
-
weak
perindoprilat
-
strong inhibitor
perindoprilat
Q10714
-
pGlu-Asn-Trp-Pro-His-Pro-Gln-Ile-Pro-Pro
-
-
pGlu-Gly-Leu-Pro-Pro-Arg-Pro-Lys-Ile-Pro-Pro
-
-
pGlu-Gly-Leu-Pro-Pro-Gly-Pro-Pro-Ile-Pro-Pro
-
-
pGlu-Trp-Pro-Arg-Pro-Gln-Ile-Pro-Pro
-
-
Phe-Arg
-
hydrolysis of hippuryl-His-Leu
Phe-Gly
-
IC50: 134.9 mM
Phe-Gly-Ala-Ser-Thr-Arg-Gly-Ala
-
IC50: 0.0147 mM, noncompetitive
Phe-Gly-Gly
-
-
Phe-Gly-Gly-Phe
-
inhibits hydrolysis of Gly-Ala-Ala
Phe-His-Leu
-
inhibits hydrolysis of Gly-Ala-Ala
Phe-Hyp-Gly
-
IC50: 0.171 mM
Phe-Hyp-Gly-Thr-Hyp-Gly
-
0.406 mM
Phe-Hyp-Gly-Thr-Hyp-Gly-Leu-Hyp-Gly
-
25 mM
Phe-Leu
-
IC50: 0.0136 mM, non-competitive
Phe-Phe-Leu
-
-
Phe-Val-Asn-Pro-Gln-Ala-Gly-Ser
-
the peptide corresponds to a fragment of helianthinin, the 11S globulin from sunflower seeds, which is the main storage protein in sunflower. Sunflower seed proteins are a potential source of angiotensin-converting enzyme inhibitory peptides when hydrolyzed with pepsin and pancreatin
Phe-Val-Asn-Pro-Gln-Ala-Gly-Ser
-
-
phenacein
-
-
phlorofucofuroeckol A
-
derived from Ecklonia stolonifera
phlorotannins
-
e.g. from Ahnfeltiopsis flabelliformis, Ecklonia cava, Ecklonia stolonifera, Pelvetia siliqousa, and Undaria pinnatifida, phenolic compounds formed by the polymerization of phloroglucinol or defined as 1,3,5-trihydroxybenzene monomer units and biosynthesized through the acetate-malonate pathway. They are highly hydrophilic components with a wide range of molecular sizes ranging between 126-650 kDa. A closed ring dibenzo-1,4-dioxin moiety may be crucial for ACE inhibitory effects
-
PHO3(2-)
-
-
phosphoramidon
-
weak, IC50: 0.001 mM
phosphoramidon
-
-
phosphoramidon
-
-
Phthalate
-
-
plant extract
-
of Brazilian plants: Calophyllum brasiliense, Combretum fruticosum, Leea rubra, Phoenix roebelinii and Terminalia catappa
-
plantainoside D
-
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
plantamajoside
-
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
PO43-
-
100 mM, 50% inhibition
Pro-Asn-Asn-Lys-Pro-Phe-Gln
-
-
Pro-Gly-Leu
-
IC50: 13.93 mM
Pro-Leu
-
IC50: 337.32 mM
Pro-Leu-Gly
-
IC50: 4.74 mM
Pro-Ser-Tyr
-
-
Pro-Thr-His-Ile-Lys-Trp-Gly-Asp
-
inhibitor is isolated from tuna muscle
PTHIKWGD
-
IC50: about 0.008 mM. Production kinetics of angiotensin-I converting enzyme inhibitory peptides from bonito meat in artificial gastric juice
PTPVP
-
a peptide derived from muscle titin
puqiedine
-
an ACE inhibitory steroidal alkaloid from Fritillaria puqiensis, 6.1% inhibition at 0.2 mM
puqienine A
-
an ACE inhibitory steroidal alkaloid from Fritillaria puqiensis, 20.4% inhibition at 0.2 mM
puqienine B
-
an ACE inhibitory steroidal alkaloid from Fritillaria puqiensis, 24.7% inhibition at 0.2 mM
puqienine C
-
an ACE inhibitory steroidal alkaloid from Fritillaria puqiensis, 19.8% inhibition at 0.2 mM
puqienine D
-
an ACE inhibitory steroidal alkaloid from Fritillaria puqiensis, 16.5% inhibition at 0.2 mM
puqienine E
-
an ACE inhibitory steroidal alkaloid from Fritillaria puqiensis, 72% inhibition at 0.2 mM
puqietinone
-
an ACE inhibitory steroidal alkaloid from Fritillaria puqiensis, 9.3% inhibition at 0.2 mM
Pyr-Asn-Trp-Pro-Arg-Pro-Gln-Ile-Pro-Pro
-
hydrolysis of hippuryl-His-Leu
Pyr-Asn-Trp-Pro-His-Pro-Gln-Ile-Pro-Pro
-
hydrolysis of hippuryl-His-Leu
Pyr-Gly-Gly-Trp-Pro-Arg-Pro-Gly-Pro-Glu-Ile-Pro-Pro
-
hydrolysis of hippuryl-His-Leu
-
Pyr-Gly-Leu-Pro-Pro-Arg-Pro-Lys-Ile-Pro-Pro
-
hydrolysis of hippuryl-His-Leu
Pyr-Gly-Leu-Pro-Pro-Gly-Pro-Pro-Ile-Pro-Pro
-
hydrolysis of hippuryl-His-Leu
Pyr-Lys-Trp-Ala-Pro
-
i.e. venom bradykinin-potentiating peptide V-3A, hydrolysis of hippuryl-His-Leu
Pyr-Lys-Trp-Ala-Pro
-
mixed type inhibition
Pyr-Ser-Trp-Pro-Asn-Ile-Pro-Pro
-
hydrolysis of hippuryl-His-Leu
Pyr-Trp-Pro-Arg-Pro-Gln-Ile-Pro
-
i.e. SQ20881, competitive with angiotensin I and hippuryl-L-His-L-Leu
Pyr-Trp-Pro-Arg-Pro-Gln-Ile-Pro
-
therapeutical useful
Pyr-Trp-Pro-Arg-Pro-Gln-Ile-Pro-Pro
-
hydrolysis of hippuryl-His-Leu
Pyr-Trp-Pro-Arg-Pro-Gln-Ile-Pro-Pro
-
i.e. SQ20858, competitive with angiotensin I and hippuryl-L-His-L-Leu
Pyr-Trp-Pro-Arg-Pro-Thr-Pro-Gln-Ile-Pro-Pro
-
hydrolysis of hippuryl-His-Leu
pyrrolidone-Lys-Trp-Ala-Pro
-
-
-
quercetin
-
IC50: about 2.0 mM
quercetin 3-O-(6''-galloyl)-galactoside
-
IC50: 0.16 mM
quercetin 3-O-alpha-(6''-p-coumaroylglucosyl-beta -1,2-rhamnoside)
-
IC50: 0.351 mM
quercetin-3-beta-glucopyranoside
-
IC50: 0.7088 mM
quercetin-3-O-alpha-(6''-caffeoylglucosyl-beta-1,2-rhamnoside)
-
IC50: 0.1589 mM
quercetin-3-O-alpha-L-arabinopyranoside
-
-
quercitrin
-
IC50: 0.25 mM
quercitrin glucuronide
-
IC50: 0.2 mM
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 effect on the rate of endothelial apoptosis in vitro in HUVEC cells
quinapril
-
the angiotensin-converting enzyme inhibitor has no significant effect on apoptosis induced via endotoxic shock with Escherichia coli lipopolysaccharides
quinapril
-
tissue angiotensin converting enzyme inhibitors
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
quinapril
-
-
quinaprilat
-
-
ramipril
-
human physiologically based pharmacokinetic model for the inhibitor
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
-
diabetic nephropathy can be delayed by the use of angiotensin-converting enzyme inhibitors. Critical role of bradykinin B2 receptor activation in the mediation of angiotensin-converting enzyme inhibitors renal protection against diabetic nephropathy
ramipril
-
the angiotensin-converting enzyme inhibitor has no effect on the rate of endothelial apoptosis in vitro in HUVEC cells
ramipril
-
the angiotensin-converting enzyme inhibitor has no significant effect on apoptosis induced via endotoxic shock with Escherichia coli lipopolysaccharides
ramipril
-
short-term ramipril treatment adequately reduces angiotensin-converting enzyme activity and blood pressure, but has no significant effects on insulin sensitivity, forearm blood flow, substrate fluxes across the forearm, whole-body substrate oxidation and intramuscular triacylglycerol content in obese insulinresistant subjects
ramipril
-
ACE-specific inhibitor
ramipril
-
plasma-ACE activity is almost completely abolished 0.5-2.0 h after treatment with ramipril (0.125, 0.25, 0.5, and 1.0 mg/kg), irrespective of the dose rate, significant inhibition of ACE activity of 54.7 to 82.6% (depending on the dosage) is still present 24 h after treatment, ramipril at a dose rate of 0.125 mg/kg once daily produces significant and long-lasting inhibition of ACE activity in healthy cats
ramipril
-
-
ramipril
-
the ACE inhibitor is associated with a major reduction of proteinuria, slower GFR decline and risk of doubling serum creatinine or progression to end-stage renal disease in patients with nondiabetic kidney disease
ramiprilat
-
human physiologically based pharmacokinetic model for the inhibitor
ramiprilat
-
the ACE inhibitor-induced dimerization of angiotensin-converting enzyme, via the C domain of the enzyme, represents the initial step in the angiotensin-converting enzyme signaling pathway that involves the activation of the JNK/c-Jun pathway and leads to changes in endothelial cell gene expression
ramiprilat
-
-
resveratrol
-
IC50: about 1.6 mM
RMLGQ
-
IC50: 0.358 mM, competitive inhibition
RMLGQTP
-
IC50: 0.503 mM, mixed-type inhibition
RMLGQTPTK
-
IC50: 0.034 mM, noncompetitive inhibition
rosmarinic acid
-
0.01 mg/ml, 55.2% inhibition
RPARPTSPP
-
-
RVAPEEHPT
-
-
RXP407
Q10714
i.e. Ac-Asp-L-Phe(PO2CH2)-L-Ala-Ala-NH2, a human sACE domain-specific phosphinic peptidyl inhibitor and antihypertensive drug
RXPA380
-
C domain-specific inhibitor
RXPA380
Q10714
i.e. (2S)-2-[([2-[(1R)-1-[((benzyloxy)carbonyl)amino]-2-(phenylethyl)(hydroxyl)-phosphinyl]cyclopentyl]carbonyl)amino]-3-(1H-indo-3-yl)-propionic acid (Cbz-PhePSI[P(O)(OH)CH]Pro-Trp-OH), a human sACE domain-specific phosphinic peptidyl inhibitor and antihypertensive drug
S-acetylcaptopril
-
-
-
salicylate
-
-
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
-
SCH 54470
-
-
Ser-Pro
-
hydrolysis of hippuryl-His-Leu
-
Ser-Pro-Pro
-
-
Ser-Trp-Ser-Phe
-
-
SFTAGARTFNFDENPCDYFQGGKIKAT
-
-
snake venom peptide
-
-
-
snake venom peptide
-
of Bothrops jararaca
-
soymilk protein proteolytic peptides
-
generated by proteolytic action of Lactobacilli and Bifidobacterium, which is increased in presence of fructooligosaccharides. The peptides show inhibitory activity to ACE, with IC50 values of 0.02 to 0.17 mg/ml, and antihypertensive effect in vivo, overview
-
spirapril
-
-
SSYVHLRPARPTSPP
-
-
Substance P
-
-
succinate
-
-
talopeptin
-
-
tannin
-
-
-
temocapril
-
chronic treatment with temocapril improves the carotid arterial stiffness in healthy, normotensive elderly, and hence may reduce their risk for cardiovascular disease
Teprotide
-
from snake venom peptides
Teprotide
-
-
Teprotide
-
i.e. SQ 20881
Tetranitromethane
-
5 mM, 99.1% inhibition
Thermolysin
-
extract of dried bonito
-
thiorphan
-
weak, IC50: 0.0001 mM
Thr-Ala-Pro-Tyr
-
-
Thr-Gln-Val-Tyr
-
-
Thr-Lys
-
IC50: 1.634 mM, mixed-type inhibition
Thr-Pro
-
IC50: 2.071 mM, competitive inhibition
Thr-Tyr-Leu-Gly-Ser
-
-
Thr-Val-Pro-Tyr
-
-
Thr-Val-Val-Pro-Gly
-
-
Tokuho A
-
-
-
trandolapril
-
the angiotensin-converting enzyme inhibitor has no effect on the rate of endothelial apoptosis in vitro in HUVEC cells
trandolapril
-
the angiotensin-converting enzyme inhibitor has no significant effect on apoptosis induced via endotoxic shock with Escherichia coli lipopolysaccharides
trandolaprilat
Q10714
-
trandolaprilat
-
-
Trp-Ala
-
IC50: 0.2773 mM, competitive
Trp-Leu
-
IC50: 0.0341 mM, non-competitive
Trp-Met
-
IC50: 0.0986 mM, competitive
Trp-Pro-Glu-Ala-Ala-Glu-Leu-Met-Met-Glu-Val-Asp-Pro
-
noncompetitive inhibitor
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
Trp-Val
-
IC50: 0.5005 mM, competitive
Trp-Val-Pro-Ser-Val-Tyr
-
-
Trypsin
-
about 10% ACE inhibitory
-
Tyr-Ala
-
hydrolysis of hippuryl-His-Leu
Tyr-Gln-Tyr
-
-
Tyr-Leu-Ala-Gly-Asn-Gln
-
-
Tyr-Pro-Lys
-
-
Tyr-Tyr-Ala-Pro-Phe
-
-
Tyr-Tyr-Ala-Pro-Phe-Asp-Gly-Ile-Leu
-
-
Tyr-Val-Val-Phe-Lys
-
-
Val-Ile-Glu-Lys-Tyr-Pro
-
-
Val-Leu-Ile-Val-Pro
-
IC50: 0.00169 mM. The peptide is resistant to digestion by proteases of the gastrointestinal tract. The antihypertensive property of this peptide derived from glycinin might find importance in the development of therapeutic functional foods
Val-Leu-Ile-Val-Pro
-
-
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
Val-Met-Asp-Lys-Pro-Gln-Gly
-
-
Val-Phe-Pro-Tyr
-
-
Val-Pro-Pro
-
-
Val-Pro-Pro
-
casein hydrolysate containing VPP and IPP improves the vascular endothelial dysfunction in subjects with mild hypertension. The continuous intake of VPP and IPP could help to prevent cardiovascular diseases in hypertensive subjects
Val-Thr-Pro-Ala-Leu-Arg
-
-
Val-Trp
-
IC50: 3.311 mM
Val-Trp
-
IC50: 0.0025 mM, uncompetitive
Val-Tyr
-
IC50: 0.263 mM
verticine
-
IC50: 0.3128 mM
verticinone
-
IC50: 0.165 mM
WF-10,129
-
-
YRGGLEPINF
-
the inhibitor produces an acute blood-pressure-lowering effect in spontaneously hypertensive rats upon a single oral administration
YVHLRPARPTSPP
-
-
ZnCl2
-
1.0 mM, 98% inhibition
zofenpril
-
-
[[(2S)-2-mercapto-3-methylpentanoyl]amino]acetic acid
-
;
monomethyl phosphate
-
-
additional information
-
enzyme is not affected by addition of 0.1-1.0 mM CaCl2, Mn2Cl2, MgCl2 or 0.1 mM ZnCl2
-
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
-
synthetic peptides derived from human collagen XVIII hinge domain with sequences similar to bradykinin potentiating peptides from snake venom
-
additional information
-
isolation of angiotensin converting enzyme (ACE) inhibitory flavonoids from Sedum sarmentosum
-
additional information
-
hot water extract of Tamogi-take mushroom, IC50: 6 mg/ml
-
additional information
-
hot water extract of Tamogi-take mushroom, antihypertensive effect in spontaneously hypertensive rats by oral administration
-
additional information
-
inhibitory peptide from Alaska pollack (Theragra chalcogramma) frame protein hydrolysate
-
additional information
-
inhibitory peptides from in vitro pepsin-pancreatin digestion of soy protein
-
additional information
-
compounds from Epilobium angustifolium inhibit. Taking into account the role of these peptidase in prostate diseases, the results may partly support and explain the use of Epilobium extracts in folk medicine
-
additional information
-
inhibition by food extract solution from garlic, buckwheat, mushroom, soy sauce, Tokuho A, Tokuho B
-
additional information
-
the purified mucilage of storage roots (Ipomoea batatas (L.) Lam. Tainong 57) exhibits dose-dependent ACE inhibitory activity in vitro. The mucilage acted as a mixed type inhibitor toward ACE with an IC50 of 0.3645 mg/ml
-
additional information
-
angiotensin-converting enzyme inhibitors are recommended in dogs and cats with chronic renal failure. They decrease the glomerular capillary pressure, have antiproteinuric effects, tend to delay the progression of chronic renal failure and to limit the extent of renal lesions
-
additional information
-
tissue angiotensin converting enzyme inhibitors exert more pronounced antithrombotic effect than plasma ACE-Is in experimental thrombosis
-
additional information
-
the immobilized enzyme is used to purify inhibitory peptides from sunflower
-
additional information
-
the immobilized lung extract is used to purify inhibitory peptides from sunflower and rapeseed protein hydrolysates that has been obtained by treatment of protein isolates with alcalase
-
additional information
-
simultaneous determination of angiotensin I-converting enzyme inhibitory peptides in tryptic casein hydrolysate by high-performance liquid chromatography combined with a replicate heart-cut column-switching technique
-
additional information
-
inhibitory peptide is isolated from tuna dark muscle hydrolysate prepared by alcalase, neutrase, pepsin, papain, alpha-chymotrypsin, and trypsin, respectively. Among hydrolysates, the pepsin-derived hydrolysate exhibited the highest ACE I inhibitory activity versus those of other enzyme hydrolysates. The structure of the peptide is identified to be Trp-Pro-Glu-Ala-Ala-Glu-Leu-Met-Met-Glu-Val-Asp-Pro
-
additional information
-
yak milk casein could be a resource to generate antihypertensive peptides
-
additional information
-
angiotensin I-converting enzyme inhibitory peptides from protein hydrolysates by a soybean protease D3
-
additional information
-
trichloroacetic acid filtrates of lactic acid bacteria (Lactobacillus casei 2607, Lactobacillus casei 15286, Lactobacillus acidophilus 4461, Lactobacillus acidophilus 33200, Streptococcus thermophilus 1275, Streptococcus thermophilus 285, Lactobacillus delbrueckii ssp. bulgaricus 1092, Lactobacillus delbrueckii ssp. bulgaricus 1368, Bifidobacterium longum 5022) show inhibitory activity
-
additional information
-
isolation and characterization of angiotensin I-converting enzyme inhibitory peptides derived from porcine hemoglobin. IC50-vlue for pepsin is 1.19 mg/ml, IC50-value for trypsin is 8.79 mg/ml, IC50-value for papain is 2.21 mg/ml
-
additional information
-
inhibition of angiotensin converting enzyme seems to augment catabolism of calcitonin gene related peptide
-
additional information
-
not inhibited by MLN4760, SCH39370, amastatin bestatin, chymostatin, and p-chloromercuribenzoate
-
additional information
-
pacific hake (Merluccius productus) fillet hydrolysate demonstrates in vitro ACE-inhibitory activity (IC50 0.165 mg/ml), which is enhanced by ultrafiltration through a 10 kDa molecular weight cutoff membrane (IC50 0.044 mg/ml), PeptACE peptides and the unfractionated pacific hake (Merluccius productus) fillet hydrolysate show significantly greater ACE inhibitory activity (i.e., significantly lower IC50 values) after simulated gastrointestinal digestion and may therefore be considered as prodrug type inhibitors
-
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
-
autolysis of protein isolates from vascular bundle and inner tuber tissues of potato (Solanum tuberosum) enhances the inhibition of the angiotensin converting enzyme I, the highest inhibitory activities (50% reduction in ACE activity achieved following autolysis at a protein concentration of 0.36 mg/ml) are measured in tubers after 5-6 months of storage prior to sprouting, the rate of ACE inhibition is positively correlated with protease activity in tuber tissues
-
additional information
-
soybean flour hydrolysate and soybean ACE inhibitory peptides have an inhibitory effect towards ACE, adding isoflavones into both soybean flour hydrolysate and soybean ACE inhibitory peptide samples to a concentration of as high as 31.5% (w/w) does not affect ACE inhibitory activity
-
additional information
-
plant methanol extracts from Amaranthus dubius, Amaranthus hybridus, Asystasia gangetica, Galinsoga parviflora, Justicia flava, Oxygonum sinuatum, Physalis viscosa, and Tulbaghia violacea show ACE inhibitory activities
-
additional information
-
not inhibited by resveratrol
-
additional information
-
ACE is not inibited by gluco-obtusifolin, obtusifolin, aurantioobtusin, cassitoroside, toralactone gentiobioside, chrysophanol triglucoside, questin, and cassiaside; both of the methanol extracts from the raw and roasted Cassia tora seeds exhibit significant inhibitory properties against ACE, demonstrating more than 50% inhibition at a concentration of 0.16393 mg/ml
-
additional information
-
angiotensin-converting enzyme inhibition does not significantly modify major biomarkers of inflammation, hemostasis, and endothelial function, e.g. C-reactive protein, interleukin 6, plasminogen activator inhibitor 1, vascular cell adhesion molecule 1, and endothelin 1, while angiotensin II levels are reduced, overview
-
additional information
-
the enzyme inhibition by angiotensin-converting enzyme inhibitors is inhibited by aspirin, which can cause therapeutic problems during application of both in treatment of heart failure patients. Angiotensin receptor blockers do not interfere with the bradykinin pathway, detailed overview
-
additional information
-
angiotensin-converting enzyme inhibitors, ACEIs, treatment of myocardial infarction patients bears is asscoiated with increased mortality, the risk is also existent for renal failure patients, effects of ACEIs on heart failure patients with other diseases or risk factors, overview
-
additional information
-
preparation ACE inhibitor peptides from the enzymatic hydrolysis of arachin, the major storage protein of Arachis hypogaea, overview
-
additional information
-
inhibitor structure-activity relationship, overview
-
additional information
-
ACE inhibitory peptides from the marine rotifer, Brachionus rotundiformis, overview. The hydrolysate is prepared by Alcalase, a-chymotrypsin, Neutrase, papain, and trypsin, inhibitory activities of the different preparateions, overview. Glutamic acid, aspartic acid, proline, glycine and alanine from ACE inhibitory activity peptide are all observed in many other ACE inhibitory peptides. Peptides derived from rotifers may be beneficial as anti-hypertension compounds in functional foods resource
-
additional information
-
ACE-inhibitory protein hydrolysates produced from canola meals, after hydrolysis by different enzymes, IC50 of molecular weight fractions, overview
-
additional information
-
ACE inhibitors can induce angioedema, overview; ACE-inhibitors in vivo act in a competitive manner and their activity is dependent on their plasma concentration
-
additional information
-
angiotensin-converting enzyme inhibitors, ACE-I, protect against cardiac toxicity in patients receiving doxorubicin chemotherapy, overview
-
additional information
-
both angiotensin-converting enzyme inhibitors and angiotensin receptor blockers, e.g. losartan, can slow the progression of diabetic nephropathy, overview
-
additional information
-
angiotensin converting enzyme inhibitors inhibit angiotensin II formation and affect the bradykinin B1 and B2 receptor, B2R and B2R, signaling, overview. They indirectly potentiate the actions of bradykinin and enzyme-resistant analogues of bradykinin on receptor BR2R, leading to increased release of arachidonic acid and NO, and they increase B2R action as allosteric enhancers, via their C-domain, inducing a conformational change in the enzyme. The inhibitors are useful in therapy of cardiovascular diseases, overview. The bradykinin B1 receptor is directly activated by ACE inhibitors, even in absence of ACE
-
additional information
-
isoflavones from soymilk may have inhibitory potency to affect ACE
-
additional information
-
inhibition of angiotensin-converting enzyme, or angiotensin II receptor blockage, slows down the progression of renal disease and provide a renal-protective effect. Therefore, they are used in therapy of type 2 diabetes, the main cause of end-stage renal disease in Europe and the United States, antagonizing the diabetic nephropathy progresses, overview
-
additional information
-
mass spectrometric and structural analysis, and production and purification of plant food-derived ACE inhibitory peptides, bioactivities, overview
-
additional information
-
generation of angiotensin I-converting enzyme inhibitory, ACEI, peptides after gastrointestinal digestion of pork meat by the action of pepsin and pancreatin at simulated gut conditions, analysis by nanoLC-ESI-MS/MS and MALDI-TOF/TOF mass spectrometry, and peptide sequencing, overview
-
additional information
-
generation of ACE inhibitory peptides from flaxseed protein, molecular weights and inhibitory potencies of fractions, overview
-
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
-
no inhibition by flavonoid glycosides, isolated from flower buds of Rosa damascena, kaempferol-3-O-beta-D-glucopyranosyl-(1,4)-beta-D-xylopyranoside, i.e. roxyloside A, isoquercitrin, quercetin gentiobioside, and afzelin
-
additional information
-
quantitative retention-activity relationship models of ACE inhibitors using biopartitioning micellar chromatography, method evaluation, overview
-
additional information
-
treatment with ACE inhibitors can induce chronic cough in many patients
-
additional information
-
nutrient sources of ACE inhibitory peptides derived from marine organisms, enzymes used for hydrolysis, and IC50 values, overview. Tryptophan, tyrosine, proline or phenylalanine at the C-terminal and branched-chain aliphatic amino acids at the N-terminal is suitable for peptides to act as competitive inhibitors by binding with ACE, some peptides also show a non-competitive mechanism. Hydrophobicity of the N-terminus, which is one of the common features of ACE inhibitory peptides, may contribute to the inhibitory activity. The peptides exhibit antihypertensive activity in vivo rather than in vitro. Polyphenolic compounds inhibit ACE activity through sequestration of the enzyme metal factor, Zn2+ ion
-
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
-
antiproteinuric and renoprotective effects of ACE inhibitors, ACEi, overview
-
additional information
-
metabolic effects of low dose angiotensin converting enzyme inhibitor in dietary obesity in the rat
-
additional information
-
inhibitory potencies of tripeptides derived from arachin, the major storage globulin of peanut, Arachis hypogaea variety TMV-2, sequence analysis, overview. Active site biniding and the degree of inhibition by the peptides correlates with the coordination distance between the catalytic Zn2+ and the carbonyl oxygen of the peptide bond between the amino-terminal and middle residue
-
additional information
-
inhibitory potencies of tripeptides derived from arachin, the major storage globulin of peanut, Arachis hypogaea variety TMV-2, sequence analysis, overview. Active site biniding and the degree of inhibition by the peptides correlates with the coordination distance between the catalytic Zn2+ and the carbonyl oxygen of the peptide bond between the amino-terminal and middle residue. In vitro stability of the peptides to gastrointestinal proteases, overview
-
additional information
-
use of ACE inhibitor is associated with a significant decrease in long-term mortality and cardiovascular events in the patients with diastolic heart failure
-
additional information
-
screening of ACE inhibitors using the spectrocolorimetric assay method with synthetic substrate 3-hydroxybutyrylglycyl-glycyl-glycine, assay method development and optimization, detailed overview
-
additional information
-
monoclonal antibosies mAbs 9B9 and 3G8 prevent ACE dimerization in vitro in reverse micelles, and only mAb 3G8 inhibits ACE shedding from the cell surface
-
additional information
-
design and properties of N-carboxyalkyldipeptide inhibitors
-
additional information
-
-
-
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
-
inhibitors that occur naturally in body fluids
-
additional information
-
the two homologous domains of human angiotensin I-converting enzyme interact differently with competitive inhibitors
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Cl-
-
activates
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
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
Cl-
-
nonessential activator over the pH range 5.0-10.0
Cl-
-
required for hydrolysis of angiotensin I, not required for hydrolysis of bradykinin
Cl-
-
activates
Cl-
-
activates
Diazoacetylnorleucine methyl ester
-
1.0 mM, activation to 115% of control
diisopropylphosphoryl fluoride
-
1.0 mM, activation to 116.3% of control
PCMB
-
slight stimulation
Soybean trypsin inhibitor
-
0.5 mM, activation to 115% of control
-
tosylphenylalanine chloromethyl ketone
-
1.0 mM, activation to 113% of control
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.136
-
2-furanacryloyl-Phe-Gly-Gly
-
wild-type enzyme
0.174
-
2-furanacryloyl-Phe-Gly-Gly
-
recombinant enzyme
0.23
-
2-furylacryloyl-Phe-Gly-Gly
-
pH 7.5, 25C
0.25
-
2-furylacryloyl-Phe-Gly-Gly
-
pH 7.5, 25C, cobalt-ACE
28.54
-
3-hydroxybutyryl-Gly-Gly-Gly
-
37C
0.069
-
acetyl-His-Pro-(NO2)Phe-His-Leu
-
-
0.007
-
amyloid beta-protein 1-42
-
-
-
0.028
-
angiotensin
-
37C
0.009
-
angiotensin I
-
enzyme from lung and testis
0.01
-
angiotensin I
-
-
0.016
-
angiotensin I
-
recombinant enzyme
0.0308
-
angiotensin I
-
-
0.04
-
angiotensin I
-
pH 7.5, 37C, enzyme from brain, 200 mM NaCl
0.052
-
angiotensin I
-
37C, pH 7.5, wild-type enzyme
0.062
-
angiotensin I
-
lung enzyme
0.065
-
angiotensin I
-
detergent-solubilized enzyme
0.067
-
angiotensin I
-
37C
0.07
-
angiotensin I
-
-
0.071
-
angiotensin I
-
-
0.076
-
angiotensin I
-
kidney enzyme
0.076
-
angiotensin I
-
serum enzyme
0.078
-
angiotensin I
-
trypsin-extracted enzyme
0.078
-
angiotensin I
-
lung enzyme
0.09
-
angiotensin I
-
enzyme from testis and lung
0.1
-
angiotensin I
-
37C, pH 7.5, mutant enzyme R1098Q
0.119
-
angiotensin I
-
-
0.21
-
angiotensin I
-
pH 7.5, 0.2 mM NaCl
0.42
-
angiotensin I
-
pH 9.0, 0.5 mM NaCl
0.54
-
angiotensin I
-
pH 6.0, without NaCl
0.82
-
angiotensin I
-
35C, pH 7.0, 100 mM NaCl
1.04
-
angiotensin I
-
35C, pH 8.0, 100 mM NaCl
1.23
-
angiotensin I
-
35C, pH 8.0, 0 mM NaCl
2.7
-
angiotensin I
-
35C, pH 7.0, 0 mM NaCl
0.002
-
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met
-
-
0.58
-
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Tyr-Arg
-
35C, PH 8.0
0.073
-
Arg-Pro-Pro-Gly-Phe-Thr-Pro-Phe-Arg
-
35C, PH 8.0
0.0097
-
Asn-Arg-Val-Tyr-Ile-His-Pro-(NO2)Phe-His-Leu
-
-
3.4
-
benzoyl-Gly-Ala-His-Leu
-
-
2.1
-
benzoyl-Gly-Ala-Leu
-
-
7.19
-
benzoyl-Gly-Ala-Pro
-
-
2.7
-
benzoyl-Gly-Arg-His-Leu
-
-
1.3
-
benzoyl-Gly-Arg-Leu
-
-
4.9
-
benzoyl-Gly-Glu-Leu
-
-
6.2
-
benzoyl-Gly-Gly-Gly
-
-
4.9
-
benzoyl-Gly-His-Ala
-
-
0.12
-
benzoyl-Gly-His-Arg
-
-
0.56
-
benzoyl-Gly-His-Leu
-
-
1.2
-
benzoyl-Gly-His-Leu
-
-
1.2
-
benzoyl-Gly-His-Leu
-
-
1.3
-
benzoyl-Gly-His-Leu
-
-
18.2
-
benzoyl-Gly-His-Leu
-
-
5.2
-
benzoyl-Gly-His-Phe
-
-
4.4
-
benzoyl-Gly-Ile-His-Leu
-
-
0.6
-
benzoyl-Gly-Phe-Arg
-
-
0.89
-
benzoyl-Gly-Phe-His-Leu
-
-
2.1
-
benzoyl-Gly-Phe-Leu
-
-
4.6
-
benzoyl-Gly-Pro-His-Leu
-
-
2.3
-
benzoyl-Gly-Ser-His-Leu
-
-
0.067
-
benzyloxycarbonyl-(NO2)Phe-His-Leu
-
-
0.13
-
benzyloxycarbonyl-Phe-His-Leu
-
pH 7.5, 25C, enzyme from testis
0.14
-
benzyloxycarbonyl-Phe-His-Leu
-
pH 7.5, 25C
0.3
-
benzyloxycarbonyl-Phe-His-Leu
P12821
37C, pH 8.3, chimeric enzyme C583-623Ndom-ACE; 37C, pH 8.3, N-domain of tACE
0.4
-
benzyloxycarbonyl-Phe-His-Leu
-
pH 7.5
0.4
-
benzyloxycarbonyl-Phe-His-Leu
P12821
37C, pH 8.3, chimeric enzyme C1-163Ndom-ACE
1.2
-
benzyloxycarbonyl-Phe-His-Leu
P12821
37C, pH 8.3, ACE
2.8
-
benzyloxycarbonyl-Phe-His-Leu
P12821
37C, pH 8.3, chimeric enzyme C417579Ndom-ACE
0.6
-
benzyloxycarbonyl-Phe-His-Leu + H2O
-
pH 7.5, 25C, enzyme from testis
0.0004
-
bradykinin
-
-
0.27
-
bradykinin
-
35C, PH 8.0
0.047
-
Gly-Ile-His-Pro-(NO2)Phe-His-Leu
-
-
0.057
-
Gly-Pro-(NO2)Phe-His-Leu
-
-
0.9
-
hippuryl-Gly-Gly
-
pH 6, 0.1 M NaCl
0.0308
-
hippuryl-His-Leu
-
-
0.32
-
hippuryl-His-Leu
-
detergent-solubilized enzyme
0.5
-
hippuryl-His-Leu
P12821
37C, pH 8.3, N-domain of tACE
0.52
-
hippuryl-His-Leu
-
trypsin-extracted enzyme
0.6
-
hippuryl-His-Leu
-
100 mM borate/sodium carbonate buffer, pH 7.8
1
-
hippuryl-His-Leu
-
Tris-NaCl buffer
1.1
-
hippuryl-His-Leu
P12821
37C, pH 8.3, chimeric enzyme C1-163Ndom-ACE; 37C, pH 8.3, chimeric enzyme C583623Ndom-ACE; 37C, pH 8.3, tACE
1.1
-
hippuryl-His-Leu
-
10 mM potassium phosphate buffer, pH 8.3, enzyme form I, II, and III
1.2
-
hippuryl-His-Leu
-
lung enzyme
1.54
-
hippuryl-His-Leu
-
recombinant enzyme
1.61
-
hippuryl-His-Leu
-
wild-type enzyme
1.7
-
hippuryl-His-Leu
-
enzyme from kidney
1.8
-
hippuryl-His-Leu
-
kidney enzyme
1.9
-
hippuryl-His-Leu
-
-
1.9
-
hippuryl-His-Leu
-
enzyme from lung
2
-
hippuryl-His-Leu
-
-
2.6
-
hippuryl-His-Leu
-
enzyme from lung and testis
2.7
-
hippuryl-His-Leu
-
-
2.7
-
hippuryl-His-Leu
P12821
37C, pH 8.3, chimeric enzyme C417-579Ndom-ACE
2.9
-
hippuryl-His-Leu
-
serum enzyme
3
-
hippuryl-His-Leu
-
phosphosaline buffer
3.1
-
hippuryl-His-Leu
-
lung enzyme
4
-
hippuryl-His-Leu
-, Q4KXL2
-
4
-
hippuryl-His-Leu
-
heart enzyme
20
-
hippuryl-His-Leu
-
-
5
-
hippuryl-L-His-L-Leu
-
-
2.3
-
hippuryl-Lys-Leu
-
-
0.5
-
hippuryl-Phe-Arg
-
heart enzyme
0.7
-
hippuryl-Phe-Arg
-
lung enzyme
1.8
-
hippuryl-Phe-Arg
-
kidney enzyme
0.067
-
His-Pro-(NO2)Phe-His-Leu
-
-
0.3
-
Ile-Ser-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
-
35C, PH 8.0
0.0157
-
LEQIYHL
-
pH 7.0, N-domain
0.0347
-
LEQIYHL
-
pH 7.0, somatic enzyme
0.1592
-
LEQIYHL
-
pH 7.0, C-domain
0.4125
-
LEQIYHL
-
pH 7.0
0.5
-
Leu-enkephalin
-
-
1
-
Leu5-enkephalin
-
-
0.014
-
LVVYPWTQRY
-
pH 7.5, 37C, enzyme from testis, 200 mM NaCl
0.015
-
LVVYPWTQRY
-
pH 7.5, 37C, enzyme from brain, 200 mM NaCl
0.019
-
LVVYPWTQRY
-
pH 7.5, 37C, enzyme from brain, 10 mM NaCl
0.033
-
LVVYPWTQRY
-
pH 7.5, 37C, enzyme from testis, 10 mM NaCl
0.3
-
Met-enkephalin
-
-
1
-
Met5-enkephalin
-
-
0.05
-
N-(3-(2-furyl)acryloyl)-Phe-Ala-Ala
-
pH 7.5, 25C, enzyme from testis
0.14
-
N-(3-(2-furyl)acryloyl)-Phe-Ala-Lys
-
pH 7.5, 25C, N-domain from lung enzyme
0.15
-
N-(3-(2-furyl)acryloyl)-Phe-Ala-Lys
-
pH 7.5, 25C, enzyme from lung
0.17
-
N-(3-(2-furyl)acryloyl)-Phe-Ala-Lys
-
pH 7.5, 25C, enzyme from testis
0.005
-
N-(3-(2-furyl)acryloyl)-Phe-Ala-Pro
-
pH 7.5, 25C, enzyme from testis
0.008
-
N-(3-(2-furyl)acryloyl)-Phe-Ala-Pro
-
pH 7.5, 25C, enzyme from lung; pH 7.5, 25C, N-domain from lung enzyme
0.5
-
N-(3-(2-furyl)acryloyl)-Phe-Gly-Gly
-
pH 7.5, 25C, enzyme from testis
0.98
-
N-(3-(2-furyl)acryloyl)-Phe-Gly-Gly
-
pH 7.5, 25C
0.05
-
N-(3-(2-furyl)acryloyl)-Phe-Phe-Arg
-
pH 7.5, 25C, enzyme from lung; pH 7.5, 25C, N-domain from lung enzyme
0.1
-
N-(3-(2-furyl)acryloyl)-Phe-Phe-Arg
-
pH 7.5, 25C
0.12
-
N-(3-(2-furyl)acryloyl)-Phe-Phe-Arg
-
pH 7.5, 25C, enzyme from testis
0.125
-
N-benzyloxycarbonyl-L-Phe-L-His-L-Leu
-
-
1.16
-
N-hippuryl-His-Leu
-
kinetic study by capillary electrophoresis
1.8
-
N-hippuryl-His-Leu
-
pH 7.5, 25C
0.014
-
neurotensin
-
-
0.0753
-
NKLKPSQ
-
pH 7.0, N-domain
0.0905
-
NKLKPSQ
-
pH 7.0, somatic enzyme
0.1126
-
NKLKPSQ
-
pH 7.0
0.01472
-
NKLKPSQWI
-
pH 7.0
0.0622
-
NKLKPSQWI
-
pH 7.0, N-domain
0.0815
-
NKLKPSQWI
-
pH 7.0, somatic enzyme
0.5237
-
NKLKPSQWI
-
pH 7.0, C-domain
0.0027
-
NKLKPSQWISL
-
pH 7.0
0.0069
-
NKLKPSQWISL
-
pH 7.0, N-domain
0.017
-
NKLKPSQWISL
-
pH 7.0, somatic enzyme
0.1505
-
NKLKPSQWISL
-
pH 7.0, C-domain
0.1367
-
NKLKPSQWISLSD
-
pH 7.0, somatic enzyme
0.2314
-
NKLKPSQWISLSD
-
pH 7.0, N-domain
0.459
-
NKLKPSQWISLSD
-
pH 7.0
0.6738
-
NKLKPSQWISLSD
-
pH 7.0, C-domain
0.011
-
o-aminobenzoyl-FDK-(dinitrophenyl)-P-OH
-
pH 8.0, 37C, wild-type enzyme
0.0187
-
o-aminobenzoyl-FDK-(dinitrophenyl)-P-OH
-
pH 8.0, 37C, N-domain
0.0248
-
o-aminobenzoyl-FDK-(dinitrophenyl)-P-OH
-
pH 8.0, 37C, C-domain
0.0027
-
o-aminobenzoyl-FRK-(dinitrophenyl)-P-OH
-
pH 8.0, 37C, C-domain
0.0034
-
o-aminobenzoyl-FRK-(dinitrophenyl)-P-OH
-
pH 8.0, 37C, N-domain
0.004
-
o-aminobenzoyl-FRK-(dinitrophenyl)-P-OH
-
pH 8.0, 37C, wild-type enzyme
0.001
-
o-aminobenzoyl-GFSPFAQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, N-domain
0.0013
-
o-aminobenzoyl-GFSPFAQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, wild-type enzyme
0.002
-
o-aminobenzoyl-GFSPFAQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, C-domain
0.0016
-
o-aminobenzoyl-GFSPFEQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, wild-type enzyme
0.0024
-
o-aminobenzoyl-GFSPFFQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, N-domain
0.0026
-
o-aminobenzoyl-GFSPFFQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, wild-type enzyme
0.0037
-
o-aminobenzoyl-GFSPFFQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, C-domain
0.0021
-
o-aminobenzoyl-GFSPFLQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, wild-type enzyme
0.003
-
o-aminobenzoyl-GFSPFLQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, N-domain
0.0034
-
o-aminobenzoyl-GFSPFLQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, C-domain
6e-05
-
o-aminobenzoyl-GFSPFQQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, N-domain
0.0009
-
o-aminobenzoyl-GFSPFQQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, C-domain
0.0011
-
o-aminobenzoyl-GFSPFQQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, wild-type enzyme
0.0013
-
o-aminobenzoyl-GFSPFRA-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, wild-type enzyme
0.0014
-
o-aminobenzoyl-GFSPFRA-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, C-domain
0.0018
-
o-aminobenzoyl-GFSPFRA-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, N-domain
0.0007
-
o-aminobenzoyl-GFSPFRF-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, N-domain
0.0011
-
o-aminobenzoyl-GFSPFRF-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, C-domain
0.0014
-
o-aminobenzoyl-GFSPFRF-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, wild-type enzyme
0.0014
-
o-aminobenzoyl-GFSPFRI-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, N-domain
0.0015
-
o-aminobenzoyl-GFSPFRI-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, wild-type enzyme
0.0024
-
o-aminobenzoyl-GFSPFRI-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, C-domain
0.0009
-
o-aminobenzoyl-GFSPFRN-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, wild-type enzyme
0.0033
-
o-aminobenzoyl-GFSPFRN-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, C-domain
0.005
-
o-aminobenzoyl-GFSPFRN-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, N-domain
0.0016
-
o-aminobenzoyl-GFSPFRQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, wild-type enzyme
0.003
-
o-aminobenzoyl-GFSPFRQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, N-domain
0.006
-
o-aminobenzoyl-GFSPFRQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, C-domain
0.0009
-
o-aminobenzoyl-GFSPFRR-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, wild-type enzyme
0.0014
-
o-aminobenzoyl-GFSPFRR-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, C-domain; pH 8.0, 37C, N-domain
0.0007
-
o-aminobenzoyl-GFSPFRS-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, wild-type enzyme
0.003
-
o-aminobenzoyl-GFSPFRS-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, C-domain; pH 8.0, 37C, N-domain
0.0021
-
o-aminobenzoyl-GFSPFSQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, C-domain
0.0023
-
o-aminobenzoyl-GFSPFSQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, N-domain
0.0025
-
o-aminobenzoyl-GFSPFSQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, wild-type enzyme
0.017
-
o-aminobenzoyl-SDK-(dinitrophenyl)-P-OH
-
pH 8.0, 37C, wild-type enzyme
0.022
-
o-aminobenzoyl-SDK-(dinitrophenyl)-P-OH
-
pH 8.0, 37C, N-domain
0.032
-
o-aminobenzoyl-SDK-(dinitrophenyl)-P-OH
-
pH 8.0, 37C, C-domain
0.0144
-
o-aminobenzoyl-SRK-(dinitrophenyl)-P-OH
-
pH 8.0, 37C, N-domain
0.0148
-
o-aminobenzoyl-SRK-(dinitrophenyl)-P-OH
-
pH 8.0, 37C, wild-type enzyme
0.0229
-
o-aminobenzoyl-SRK-(dinitrophenyl)-P-OH
-
pH 8.0, 37C, C-domain
0.0154
-
o-aminobenzoyl-TDK-(dinitrophenyl)-P-OH
-
pH 8.0, 37C, wild-type enzyme
0.0157
-
o-aminobenzoyl-TDK-(dinitrophenyl)-P-OH
-
pH 8.0, 37C, N-domain
0.0609
-
o-aminobenzoyl-TDK-(dinitrophenyl)-P-OH
-
pH 8.0, 37C, C-domain
0.0031
-
o-aminobenzoyl-TRK-(dinitrophenyl)-P-OH
-
pH 8.0, 37C, N-domain
0.0074
-
o-aminobenzoyl-TRK-(dinitrophenyl)-P-OH
-
pH 8.0, 37C, C-domain
0.0102
-
o-aminobenzoyl-TRK-(dinitrophenyl)-P-OH
-
pH 8.0, 37C, wild-type enzyme
0.0051
-
o-aminobenzoyl-YDK-(dinitrophenyl)-P-OH
-
pH 8.0, 37C, N-domain
0.0111
-
o-aminobenzoyl-YDK-(dinitrophenyl)-P-OH
-
pH 8.0, 37C, wild-type enzyme
0.015
-
o-aminobenzoyl-YDK-(dinitrophenyl)-P-OH
-
pH 8.0, 37C, C-domain
0.0047
-
o-aminobenzoyl-YRK-(dinitrophenyl)-P-OH
-
pH 8.0, 37C, C-domain
0.005
-
o-aminobenzoyl-YRK-(dinitrophenyl)-P-OH
-
pH 8.0, 37C, N-domain
0.0051
-
o-aminobenzoyl-YRK-(dinitrophenyl)-P-OH
-
pH 8.0, 37C, wild-type enzyme
0.146
-
Pro-(NO2)Phe-His-Leu
-
-
0.108
-
SLKPSNWLTPSE
-
pH 7.0, N-domain
0.2338
-
SLKPSNWLTPSE
-
pH 7.0
0.3117
-
SLKPSNWLTPSE
-
pH 7.0, somatic enzyme
0.025
-
Substance P
-
-
0.0381
-
TOAC1-angiotensin I
-
-
0.0472
-
TOAC3-angiotensin I
-
-
0.023
-
Tyr-Ile-His-Pro-(NO2)Phe-His-Leu
-
-
0.044
-
[Arg10]angiotensin I
-
37C, pH 7.5, wild-type enzyme
0.046
-
[Arg10]angiotensin I
-
37C, pH 7.5, mutant enzyme Y1096F
0.22
-
[Arg10]angiotensin I
-
37C, pH 7.5, mutant enzyme R1098Q
0.011
-
[Phe9,Arg10]angiotensin I
-
37C, pH 7.5, wild-type enzyme
0.014
-
[Phe9,Arg10]angiotensin I
-
37C, pH 7.5, mutant enzyme Y1096F
0.02
-
[Phe9,Arg10]angiotensin I
-
37C, pH 7.5, mutant enzyme R1098Q
0.025
-
[Phe9,Arg10]angiotensin I
-
37C, pH 7.5, mutant enzyme K1087A
0.032
-
[Phe9]angiotensin I
-
37C, pH 7.5, wild-type enzyme
0.042
-
[Phe9]angiotensin I
-
37C, pH 7.5, mutant enzyme R1098Q
0.056
-
[Phe9]angiotensin I
-
37C, pH 7.5, mutant enzyme Y1096F
0.37
-
MKRSRGPSPRR
-
35C, PH 8.0
additional information
-
additional information
-
Km-values of underglycosylated mutant enzymes
-
additional information
-
additional information
-
the two active sites within bovine lung enzyme exhibits strong negative cooperativity
-
additional information
-
additional information
-
kinetics
-
additional information
-
additional information
-
Km for angiotensin I as a function of pH
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
Km values for wild-type and mutant enzymes
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
320
-
2-furanacryloyl-Phe-Gly-Gly
-
recombinant enzyme
368
-
2-furanacryloyl-Phe-Gly-Gly
-
wild-type enzyme
5520
-
2-furylacryloyl-Phe-Gly-Gly
-
pH 7.5, 25C, cobalt-ACE
7590
-
2-furylacryloyl-Phe-Gly-Gly
-
pH 7.5, 25C
4.2
-
amyloid beta-protein 1-42
-
-
-
0.58
-
angiotensin
-
37C
8.33
-
angiotensin
-
-
0.03
0.55
angiotensin I
-
35C, pH 7.0, 0 mM NaCl
0.057
0.65
angiotensin I
-
35C, pH 8.0, 0 mM NaCl; 35C, pH 8.0, 100 mM NaCl
1.4
-
angiotensin I
-
pH 7.5, 37C, enzyme from brain, 200 mM NaCl
2.95
-
angiotensin I
-
detergent-solubilized enzyme
6.58
-
angiotensin I
-
trypsin-extracted enzyme
6.83
-
angiotensin I
-
35C, pH 7.0, 100 mM NaCl
6.84
-
angiotensin I
-
35C, pH 7.0, 0 mM NaCl
7.88
-
angiotensin I
-
-
8.7
-
angiotensin I
-
37C
10.78
-
angiotensin I
-
35C, pH 8.0, 100 mM NaCl
11.06
-
angiotensin I
-
35C, pH 8.0, 0 mM NaCl
12
-
angiotensin I
-
enzyme from testis
13.2
-
angiotensin I
-
-
13.2
-
angiotensin I
-
enzyme from testis
13.5
-
angiotensin I
-
enzyme from lung
52
-
angiotensin I
-
37C, pH 7.5, wild-type enzyme
60
-
angiotensin I
-
37C, pH 7.5, mutant enzyme R1098Q
2.41
-
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Tyr-Arg
-
35C, pH 8.0
0.24
-
Arg-Pro-Pro-Gly-Phe-Thr-Pro-Phe-Arg
-
35C, pH 8.0
283
-
benzoyl-Gly-Gly-Gly
-
-
76.7
-
benzoyl-Gly-His-Leu
-
-
345
-
benzoyl-Gly-His-Leu
-
-
383
-
benzoyl-Gly-Phe-Arg
-
-
2.1
-
benzyloxycarbonyl-Phe-His-Leu
P12821
37C, pH 8.3, ACE
19
-
benzyloxycarbonyl-Phe-His-Leu
-
pH 7.5, 25C, enzyme from testis
21.5
-
benzyloxycarbonyl-Phe-His-Leu
-
pH 7.5
34.4
-
benzyloxycarbonyl-Phe-His-Leu
P12821
37C, pH 8.3, chimeric enzyme C417-579Ndom-ACE
36.8
-
benzyloxycarbonyl-Phe-His-Leu
P12821
37C, pH 8.3, chimeric enzyme C583-623Ndom-ACE
73.2
-
benzyloxycarbonyl-Phe-His-Leu
P12821
37C, pH 8.3, ACE
97.5
-
benzyloxycarbonyl-Phe-His-Leu
P12821
37C, pH 8.3, chimeric enzyme C1-163Ndom-ACE
100
-
benzyloxycarbonyl-Phe-His-Leu
-
pH 7.5, 25C
128
-
benzyloxycarbonyl-Phe-His-Leu
P12821
37C, pH 8.3, N-domain of tACE
12
-
benzyloxycarbonyl-Phe-His-Leu + H2O
-
pH 7.5, 25C, enzyme from testis
1.09
-
bradykinin
-
35C, pH 8.0
8.33
-
bradykinin
-
-
9.1
-
bradykinin
-
-
179
-
furanacryloyl-L-Phe-Gly-Gly
-
-
210
-
furanacryloyl-L-Phe-Gly-Gly
-
-
5.4
-
hippuryl-His-Leu
-
detergent-solubilized enzyme
8.58
-
hippuryl-His-Leu
-
trypsin-extracted enzyme
11.8
-
hippuryl-His-Leu
P12821
37C, pH 8.3, chimeric enzyme C417-579Ndom-ACE
12.9
-
hippuryl-His-Leu
P12821
37C, pH 8.3, chimeric enzyme C583-623Ndom-ACE
15.1
-
hippuryl-His-Leu
P12821
37C, pH 8.3, chimeric enzyme C1163Ndom-ACE
24.5
-
hippuryl-His-Leu
P12821
37C, pH 8.3, tACE
196
-
hippuryl-His-Leu
-
-
257
-
hippuryl-His-Leu
-
-
262.5
-
hippuryl-His-Leu
P12821
37C, pH 8.3, N-domain of tACE
302
-
hippuryl-His-Leu
-
enzyme from lung
308
-
hippuryl-His-Leu
-
enzyme from testis
408
-
hippuryl-His-Leu
-
recombinant enzyme
414
-
hippuryl-His-Leu
-
wild-type enzyme
545
-
hippuryl-His-Leu
-
-
1.1
-
Ile-Ser-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
-
35C, pH 8.0
11.7
-
Leu5-enkephalin
-
-
51
-
LVVYPWTQRY
-
pH 7.5, 37C, enzyme from testis, 10 mM NaCl
77
-
LVVYPWTQRY
-
pH 7.5, 37C, enzyme from testis, 200 mM NaCl
89
-
LVVYPWTQRY
-
pH 7.5, 37C, enzyme from brain, 200 mM NaCl
230
-
LVVYPWTQRY
-
pH 7.5, 37C, enzyme from brain, 10 mM NaCl
58.3
-
Met5-enkephalin
-
-
178
-
N-(3-(2-furyl)acryloyl)-Phe-Ala-Ala
-
pH 7.5, 25C, enzyme from testis
35
-
N-(3-(2-furyl)acryloyl)-Phe-Ala-Lys
-
pH 7.5, 25C, N-domain from lung enzyme
54
-
N-(3-(2-furyl)acryloyl)-Phe-Ala-Lys
-
pH 7.5, 25C, enzyme from lung
85
-
N-(3-(2-furyl)acryloyl)-Phe-Ala-Lys
-
pH 7.5, 25C, enzyme from testis
8
-
N-(3-(2-furyl)acryloyl)-Phe-Ala-Pro
-
pH 7.5, 25C, N-domain from lung enzyme
30
-
N-(3-(2-furyl)acryloyl)-Phe-Ala-Pro
-
pH 7.5, 25C, enzyme from lung
45
-
N-(3-(2-furyl)acryloyl)-Phe-Ala-Pro
-
pH 7.5, 25C, enzyme from testis
260
-
N-(3-(2-furyl)acryloyl)-Phe-Gly-Gly
-
pH 7.5, 25C, enzyme from testis
315
-
N-(3-(2-furyl)acryloyl)-Phe-Gly-Gly
-
pH 7.5, 25C
30
-
N-(3-(2-furyl)acryloyl)-Phe-Phe-Arg
-
pH 7.5, 25C
45
-
N-(3-(2-furyl)acryloyl)-Phe-Phe-Arg
-
pH 7.5, 25C, N-domain from lung enzyme
76
-
N-(3-(2-furyl)acryloyl)-Phe-Phe-Arg
-
pH 7.5, 25C, enzyme from testis
6.5
-
N-hippuryl-His-Leu
-
pH 7.5, 25C
0.567
-
neurotensin
-
-
31
-
o-aminobenzoyl-FDK-(dinitrophenyl)-P-OH
-
pH 8.0, 37C, C-domain
79
-
o-aminobenzoyl-FDK-(dinitrophenyl)-P-OH
-
pH 8.0, 37C, N-domain
79.9
-
o-aminobenzoyl-FDK-(dinitrophenyl)-P-OH
-
pH 8.0, 37C, wild-type enzyme
101.7
-
o-aminobenzoyl-FDK-(dinitrophenyl)-P-OH
-
pH 8.0, 37C, N-domain
26.7
-
o-aminobenzoyl-FRK-(dinitrophenyl)-P-OH
-
pH 8.0, 37C, wild-type enzyme
54.9
-
o-aminobenzoyl-FRK-(dinitrophenyl)-P-OH
-
pH 8.0, 37C, N-domain
69.2
-
o-aminobenzoyl-FRK-(dinitrophenyl)-P-OH
-
pH 8.0, 37C, C-domain
1
-
o-aminobenzoyl-GFSPFAQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, N-domain
2
-
o-aminobenzoyl-GFSPFAQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, C-domain
3.3
-
o-aminobenzoyl-GFSPFAQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, wild-type enzyme
2.2
-
o-aminobenzoyl-GFSPFEQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, wild-type enzyme
2.4
-
o-aminobenzoyl-GFSPFFQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, N-domain
10.1
-
o-aminobenzoyl-GFSPFFQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, wild-type enzyme
12.6
-
o-aminobenzoyl-GFSPFFQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, C-domain
3
-
o-aminobenzoyl-GFSPFLQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, N-domain
3.7
-
o-aminobenzoyl-GFSPFLQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, wild-type enzyme
4.8
-
o-aminobenzoyl-GFSPFLQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, C-domain
0.3
-
o-aminobenzoyl-GFSPFQQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, C-domain
0.6
-
o-aminobenzoyl-GFSPFQQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, N-domain
2
-
o-aminobenzoyl-GFSPFQQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, wild-type enzyme
3.4
-
o-aminobenzoyl-GFSPFRA-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, N-domain
5
-
o-aminobenzoyl-GFSPFRA-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, C-domain
10.4
-
o-aminobenzoyl-GFSPFRA-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, wild-type enzyme
1
-
o-aminobenzoyl-GFSPFRF-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, N-domain
1.4
-
o-aminobenzoyl-GFSPFRF-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, C-domain
4.2
-
o-aminobenzoyl-GFSPFRF-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, wild-type enzyme
2.6
-
o-aminobenzoyl-GFSPFRI-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, N-domain
2.9
-
o-aminobenzoyl-GFSPFRI-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, C-domain
8.7
-
o-aminobenzoyl-GFSPFRI-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, wild-type enzyme
1.8
-
o-aminobenzoyl-GFSPFRN-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, wild-type enzyme
3.3
-
o-aminobenzoyl-GFSPFRN-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, C-domain
3.8
-
o-aminobenzoyl-GFSPFRN-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, N-domain
2.2
-
o-aminobenzoyl-GFSPFRQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, wild-type enzyme
2.7
-
o-aminobenzoyl-GFSPFRQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, N-domain
4.2
-
o-aminobenzoyl-GFSPFRQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, C-domain
0.9
-
o-aminobenzoyl-GFSPFRR-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, N-domain
1
-
o-aminobenzoyl-GFSPFRR-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, wild-type enzyme
1.4
-
o-aminobenzoyl-GFSPFRR-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, C-domain
0.9
-
o-aminobenzoyl-GFSPFRS-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, wild-type enzyme
1.3
-
o-aminobenzoyl-GFSPFRS-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, N-domain
2.4
-
o-aminobenzoyl-GFSPFRS-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, C-domain
0.8
-
o-aminobenzoyl-GFSPFSQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, C-domain
2
-
o-aminobenzoyl-GFSPFSQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, wild-type enzyme
2.3
-
o-aminobenzoyl-GFSPFSQ-(N-2,4-dinitrophenyl)ethylenediamine
-
pH 8.0, 37C, N-domain
0.1
-
o-aminobenzoyl-SDK-(dinitrophenyl)-P-OH
-
pH 8.0, 37C, C-domain
24.6
-
o-aminobenzoyl-SDK-(dinitrophenyl)-P-OH
-
pH 8.0, 37C, N-domain
44.2
-
o-aminobenzoyl-SDK-(dinitrophenyl)-P-OH
-
pH 8.0, 37C, wild-type enzyme
13.7
-
o-aminobenzoyl-SRK-(dinitrophenyl)-P-OH
-
pH 8.0, 37C, C-domain
28.6
-
o-aminobenzoyl-SRK-(dinitrophenyl)-P-OH
-
pH 8.0, 37C, N-domain
0.06
-
o-aminobenzoyl-TDK-(dinitrophenyl)-P-OH
-
pH 8.0, 37C, C-domain
1.1
-
o-aminobenzoyl-TDK-(dinitrophenyl)-P-OH
-
pH 8.0, 37C, N-domain
18.7
-
o-aminobenzoyl-TDK-(dinitrophenyl)-P-OH
-
pH 8.0, 37C, N-domain
36.3
-
o-aminobenzoyl-TDK-(dinitrophenyl)-P-OH
-
pH 8.0, 37C, wild-type enzyme
0.2
-
o-aminobenzoyl-TRK-(dinitrophenyl)-P-OH
-
pH 8.0, 37C, C-domain
13.9
-
o-aminobenzoyl-TRK-(dinitrophenyl)-P-OH
-
pH 8.0, 37C, N-domain
82
-
o-aminobenzoyl-TRK-(dinitrophenyl)-P-OH
-
pH 8.0, 37C, wild-type enzyme
7
-
o-aminobenzoyl-YDK-(dinitrophenyl)-P-OH
-
pH 8.0, 37C, C-domain
28.9
-
o-aminobenzoyl-YDK-(dinitrophenyl)-P-OH
-
pH 8.0, 37C, N-domain
62.5
-
o-aminobenzoyl-YDK-(dinitrophenyl)-P-OH
-
pH 8.0, 37C, wild-type enzyme
1.01
-
o-aminobenzoyl-YRK-(dinitrophenyl)-P-OH
-
pH 8.0, 37C, wild-type enzyme
58.8
-
o-aminobenzoyl-YRK-(dinitrophenyl)-P-OH
-
pH 8.0, 37C, C-domain
85.6
-
o-aminobenzoyl-YRK-(dinitrophenyl)-P-OH
-
pH 8.0, 37C, N-domain
3.75
-
Substance P
-
-
21.3
-
Substance P
-
free acid, recombinant enzyme, and wild-type enzyme
5.83
-
TOAC1-angiotensin I
-
-
2.56
-
TOAC3-angiotensin I
-
-
57
-
[Arg10]angiotensin I
-
37C, pH 7.5, mutant enzyme Y1096F
100
-
[Arg10]angiotensin I
-
37C, pH 7.5, mutant enzyme R1098Q
460
-
[Arg10]angiotensin I
-
37C, pH 7.5, wild-type enzyme
6.5
-
[Phe9,Arg10]angiotensin I
-
37C, pH 7.5, mutant enzyme K1087A
220
-
[Phe9,Arg10]angiotensin I
-
37C, pH 7.5, mutant enzyme Y1096F
1400
-
[Phe9,Arg10]angiotensin I
-
37C, pH 7.5, wild-type enzyme
1700
-
[Phe9,Arg10]angiotensin I
-
37C, pH 7.5, mutant enzyme R1098Q
110
-
[Phe9]angiotensin I
-
37C, pH 7.5, mutant enzyme Y1096F
550
-
[Phe9]angiotensin I
-
37C, pH 7.5, wild-type enzyme
1500
-
[Phe9]angiotensin I
-
37C, pH 7.5, mutant enzyme R1098Q
18.8
-
MKRSRGPSPRR
-
35C, pH 8.0
additional information
-
additional information
-
turnover numbers of underglycosylated mutant enzymes
-
additional information
-
additional information
-
the two active sites within bovine lung enzyme exhibitsstrong negative cooperativity
-
additional information
-
additional information
-
Km-values for angiotensin I as a function of pH
-
additional information
-
additional information
-
Km values for wild-type and mutant enzymes
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
4e-07
-
(2S)-2-((3-[hydroxyl(2-phenyl-(1R)-1([(benzyloxy)carbonyl]amino)ethyl)phosphinyl]-(2R)-2-[(3-phenylisoxazol-5-yl)methyl]-1-oxopropyl)amino)-3-phenyl propanoic acid
-
pH and temperature not specified in the publication
1.4e-06
-
(2S)-2-((3-[hydroxyl(2-phenyl-(1R)-1-([(benzyloxy)carbonyl]-amino)ethyl)phosphinyl]-(2R)-2-[(3-phenylisoxazol-5-yl)methyl]-1-oxopropyl)amino) 1H-Indole-3-propanoic acid
-
pH and temperature not specified in the publication
6.5e-07
-
(2S)-2-((3-[hydroxyl(2-phenyl-(1R)-1-([(benzyloxy)carbonyl]-amino)ethyl)phosphinyl]-(2R)-2-[(3-phenylisoxazol-5-yl)methyl]-1-oxopropyl)amino)-3-(4-hydroxy-phenyl) propanoic acid
-
pH and temperature not specified in the publication
1.2e-05
-
(2S)-2-((3-[hydroxyl(2-phenyl-(1R)-1-([(benzyloxy)carbonyl]-amino)ethyl)phosphinyl]-(2S)-2-[(3-phenylisoxazol-5-yl)methyl]-1-oxopropyl)amino) 1H-indole-3-propanoic acid
-
pH and temperature not specified in the publication
-
3.8e-06
-
(2S)-2-((3-[hydroxyl(2-phenyl-(1R)-1-([(benzyloxy)carbonyl]-amino)ethyl)phosphinyl]-(2S)-2-[(3-phenylisoxazol-5-yl)methyl]-1-oxopropyl)amino)-3-(4-hydroxy-phenyl) propanoic acid
-
pH and temperature not specified in the publication
1.6e-05
-
(2S)-2-([3-(1,1'-biphenyl)-2-([hydroxyl(2-phenyl-(1R)-1-([(benzyloxy)carbonyl]amino)ethyl)phosphinyl]methyl)-1-oxopropyl]-amino) 1H-indole-3-propanoic acid
-
pH and temperature not specified in the publication
2.5e-05
-
(2S)-2-([3-(3'-[1,1'-biphenyl]-4''-yl-4',5'-dihydro-5'-isoxazolyl)-2-([hydroxyl(2-phenyl-(1R)-1-([(benzyloxy)carbonyl]amino)ethyl)-phosphinyl]methyl)-1-oxopropyl]amino) 1H-indole-3-propanoic acid
-
pH and temperature not specified in the publication
-
2.2e-06
-
(2S)-2-[[(2S)-2-mercapto-3-methylpentanoyl]amino]-3-(1-naphthyl)propanoic acid
Q9BYF1
pH 7.5, angiotensin-converting enzyme 2
0.0018
-
(2S)-2-[[(2S)-2-mercapto-3-methylpentanoyl]amino]-3-(1-naphthyl)propanoic acid
Q9BYF1
pH 7.5, angiotensin-converting enzyme
1.8e-06
-
(2S)-2-[[(2S)-2-mercapto-3-methylpentanoyl]amino]-3-(2-naphthyl)propanoic acid
Q9BYF1
pH 7.5, angiotensin-converting enzyme 2
2.4e-06
-
(2S)-2-[[(2S)-2-mercapto-3-methylpentanoyl]amino]-3-(2-naphthyl)propanoic acid
Q9BYF1
pH 7.5, angiotensin-converting enzyme 2
9.3e-06
-
(2S)-2-[[(2S)-2-mercapto-3-methylpentanoyl]amino]-3-(2-naphthyl)propanoic acid
Q9BYF1
pH 7.5, angiotensin-converting enzyme
0.00031
-
(2S)-2-[[(2S)-2-mercapto-3-methylpentanoyl]amino]-3-(2-naphthyl)propanoic acid
Q9BYF1
pH 7.5, angiotensin-converting enzyme
1.5e-06
-
(2S)-2-[[(2S)-2-mercapto-3-methylpentanoyl]amino]-3-phenylpropanoic acid
Q9BYF1
pH 7.5, angiotensin-converting enzyme 2
0.00057
-
(2S)-2-[[(2S)-2-mercapto-3-methylpentanoyl]amino]-3-phenylpropanoic acid
Q9BYF1
pH 7.5, angiotensin-converting enzyme
1.4e-05
-
(2S)-2-[[(2S)-2-mercapto-3-methylpentanoyl]amino]propanoic acid
Q9BYF1
pH 7.5, angiotensin-converting enzyme 2
0.00018
-
(2S)-2-[[(2S)-2-mercapto-3-methylpentanoyl]amino]propanoic acid
Q9BYF1
pH 7.5, angiotensin-converting enzyme
1.3e-06
-
(2S)-3-(4-hydroxyphenyl)-2-[[(2S)-2-mercapto-3-methylpentanoyl]amino]propanoic acid
Q9BYF1
pH 7.5, angiotensin-converting enzyme 2
0.00041
-
(2S)-3-(4-hydroxyphenyl)-2-[[(2S)-2-mercapto-3-methylpentanoyl]amino]propanoic acid
Q9BYF1
pH 7.5, angiotensin-converting enzyme
1.5e-06
-
(2S)-3-biphenyl-2-yl-2-[[(2S)-3-methyl-2-sulfanylpentanoyl]amino]propanoic acid
Q9BYF1
pH 7.5, angiotensin-converting enzyme 2
3.7e-05
-
(2S)-3-biphenyl-2-yl-2-[[(2S)-3-methyl-2-sulfanylpentanoyl]amino]propanoic acid
Q9BYF1
pH 7.5, angiotensin-converting enzyme 2
0.0002
-
(2S)-3-biphenyl-2-yl-2-[[(2S)-3-methyl-2-sulfanylpentanoyl]amino]propanoic acid
Q9BYF1
pH 7.5, angiotensin-converting enzyme
0.02
-
(2S)-3-biphenyl-2-yl-2-[[(2S)-3-methyl-2-sulfanylpentanoyl]amino]propanoic acid
Q9BYF1
pH 7.5, angiotensin-converting enzyme
1.5e-06
-
(2S)-3-biphenyl-3-yl-2-[[(2S)-3-methyl-2-sulfanylpentanoyl]amino]propanoic acid
Q9BYF1
pH 7.5, angiotensin-converting enzyme 2
2.2e-06
-
(2S)-3-biphenyl-3-yl-2-[[(2S)-3-methyl-2-sulfanylpentanoyl]amino]propanoic acid
Q9BYF1
pH 7.5, angiotensin-converting enzyme 2
0.00049
-
(2S)-3-biphenyl-3-yl-2-[[(2S)-3-methyl-2-sulfanylpentanoyl]amino]propanoic acid
Q9BYF1
pH 7.5, angiotensin-converting enzyme
0.001
-
(2S)-3-biphenyl-3-yl-2-[[(2S)-3-methyl-2-sulfanylpentanoyl]amino]propanoic acid
Q9BYF1
pH 7.5, angiotensin-converting enzyme
0.0023
-
(2S)-3-biphenyl-4-yl-2-[(2-mercapto-2-methylpropanoyl)amino]propanoic acid
Q9BYF1
pH 7.5, angiotensin-converting enzyme 2
0.0034
-
(2S)-3-biphenyl-4-yl-2-[(2-mercapto-2-methylpropanoyl)amino]propanoic acid
Q9BYF1
pH 7.5, angiotensin-converting enzyme
1.6e-05
-
(2S)-3-biphenyl-4-yl-2-[(mercaptoacetyl)amino]propanoic acid
Q9BYF1
pH 7.5, angiotensin-converting enzyme
0.00032
-
(2S)-3-biphenyl-4-yl-2-[(mercaptoacetyl)amino]propanoic acid
Q9BYF1
pH 7.5, angiotensin-converting enzyme 2
1.4e-06
-
(2S)-3-biphenyl-4-yl-2-[[(2S)-2-mercaptobutanoyl]amino]propanoic acid
Q9BYF1
pH 7.5, angiotensin-converting enzyme 2
8.6e-06
-
(2S)-3-biphenyl-4-yl-2-[[(2S)-2-mercaptobutanoyl]amino]propanoic acid
Q9BYF1
pH 7.5, angiotensin-converting enzyme
6.9e-06
-
(2S)-3-biphenyl-4-yl-2-[[(2S)-2-mercaptopropanoyl]amino]propanoic acid
Q9BYF1
pH 7.5, angiotensin-converting enzyme 2
2.1e-05
-
(2S)-3-biphenyl-4-yl-2-[[(2S)-2-mercaptopropanoyl]amino]propanoic acid
Q9BYF1
pH 7.5, angiotensin-converting enzyme
1.5e-06
-
(2S)-3-biphenyl-4-yl-2-[[(2S)-3-methyl-2-sulfanylpentanoyl]amino]propanoic acid
Q9BYF1
pH 7.5, angiotensin-converting enzyme 2
3e-05
-
(2S)-3-biphenyl-4-yl-2-[[(2S)-3-methyl-2-sulfanylpentanoyl]amino]propanoic acid
Q9BYF1
pH 7.5, angiotensin-converting enzyme
8.6e-05
-
(2S)-3-biphenyl-4-yl-2-[[(2S)-3-methyl-2-sulfanylpentanoyl]amino]propanoic acid
Q9BYF1
pH 7.5, angiotensin-converting enzyme 2
0.00049
-
(2S)-3-biphenyl-4-yl-2-[[(2S)-3-methyl-2-sulfanylpentanoyl]amino]propanoic acid
Q9BYF1
pH 7.5, angiotensin-converting enzyme
0.00081
-
(5S)-5-[(N-benzoyl)amino]-4-oxo-6-phenylhexanoyl-L-phenylalanine
-
mutant enzyme V379S, in 50 mM HEPES buffer (pH 6.8) containing 200 mM NaCl, and 0.01 mM ZnCl2, at 25C
0.00083
-
(5S)-5-[(N-benzoyl)amino]-4-oxo-6-phenylhexanoyl-L-phenylalanine
-
wild type enzyme, in 50 mM HEPES buffer (pH 6.8) containing 200 mM NaCl, and 0.01 mM ZnCl2, at 25C
0.0019
-
(5S)-5-[(N-benzoyl)amino]-4-oxo-6-phenylhexanoyl-L-phenylalanine
-
mutant enzyme V380T, in 50 mM HEPES buffer (pH 6.8) containing 200 mM NaCl, and 0.01 mM ZnCl2, at 25C
0.0024
-
(5S)-5-[(N-benzoyl)amino]-4-oxo-6-phenylhexanoyl-L-phenylalanine
-
mutant enzyme E376D, in 50 mM HEPES buffer (pH 6.8) containing 200 mM NaCl, and 0.01 mM ZnCl2, at 25C
0.0039
-
(5S)-5-[(N-benzoyl)amino]-4-oxo-6-phenylhexanoyl-L-phenylalanine
-
mutant enzyme F391Y, in 50 mM HEPES buffer (pH 6.8) containing 200 mM NaCl, and 0.01 mM ZnCl2, at 25C
0.0181
-
(5S)-5-[(N-benzoyl)amino]-4-oxo-6-phenylhexanoyl-L-phenylalanine
-
mutant enzyme V518T, in 50 mM HEPES buffer (pH 6.8) containing 200 mM NaCl, and 0.01 mM ZnCl2, at 25C
6.4e-05
-
(5S)-5-[(N-benzoyl)amino]-4-oxo-6-phenylhexanoyl-L-tryptophan
-
mutant enzyme V379S, in 50 mM HEPES buffer (pH 6.8) containing 200 mM NaCl, and 0.01 mM ZnCl2, at 25C
0.00024
-
(5S)-5-[(N-benzoyl)amino]-4-oxo-6-phenylhexanoyl-L-tryptophan
-
mutant enzyme E304R, in 50 mM HEPES buffer (pH 6.8) containing 200 mM NaCl, and 0.01 mM ZnCl2, at 25C
0.000497
-
(5S)-5-[(N-benzoyl)amino]-4-oxo-6-phenylhexanoyl-L-tryptophan
-
mutant enzyme S516N, in 50 mM HEPES buffer (pH 6.8) containing 200 mM NaCl, and 0.01 mM ZnCl2, at 25C
0.000618
-
(5S)-5-[(N-benzoyl)amino]-4-oxo-6-phenylhexanoyl-L-tryptophan
-
mutant enzyme D543E, in 50 mM HEPES buffer (pH 6.8) containing 200 mM NaCl, and 0.01 mM ZnCl2, at 25C
0.000679
-
(5S)-5-[(N-benzoyl)amino]-4-oxo-6-phenylhexanoyl-L-tryptophan
-
wild type enzyme, in 50 mM HEPES buffer (pH 6.8) containing 200 mM NaCl, and 0.01 mM ZnCl2, at 25C
0.00087
-
(5S)-5-[(N-benzoyl)amino]-4-oxo-6-phenylhexanoyl-L-tryptophan
-
mutant enzyme V379S/V380T, in 50 mM HEPES buffer (pH 6.8) containing 200 mM NaCl, and 0.01 mM ZnCl2, at 25C; mutant enzyme V380T, in 50 mM HEPES buffer (pH 6.8) containing 200 mM NaCl, and 0.01 mM ZnCl2, at 25C
0.00092
-
(5S)-5-[(N-benzoyl)amino]-4-oxo-6-phenylhexanoyl-L-tryptophan
-
mutant enzyme T282S, in 50 mM HEPES buffer (pH 6.8) containing 200 mM NaCl, and 0.01 mM ZnCl2, at 25C
0.00233
-
(5S)-5-[(N-benzoyl)amino]-4-oxo-6-phenylhexanoyl-L-tryptophan
-
mutant enzyme E376D, in 50 mM HEPES buffer (pH 6.8) containing 200 mM NaCl, and 0.01 mM ZnCl2, at 25C
0.00475
-
(5S)-5-[(N-benzoyl)amino]-4-oxo-6-phenylhexanoyl-L-tryptophan
-
mutant enzyme F391Y, in 50 mM HEPES buffer (pH 6.8) containing 200 mM NaCl, and 0.01 mM ZnCl2, at 25C
0.00974
-
(5S)-5-[(N-benzoyl)amino]-4-oxo-6-phenylhexanoyl-L-tryptophan
-
mutant enzyme V518T, in 50 mM HEPES buffer (pH 6.8) containing 200 mM NaCl, and 0.01 mM ZnCl2, at 25C
0.0004
-
(pE)KWAP
-
37C, pH 7.0, recombinant wild-type enzyme
0.0006
-
(pE)KWAP
-
37C, pH 7.0, full-length mutant containing only a functional N-domain catalytic site
0.0007
-
(pE)KWAP
-
37C, pH 7.0, full-length mutant containing only a functional C-domain catalytic site
0.0008
-
(pE)KWAP
-
37C, pH 7.0, enzyme from testis
3e-06
-
(pE)WPRPQIPP
-
37C, pH 7.0, full-length mutant containing only a functional C-domain catalytic site
1e-05
-
(pE)WPRPQIPP
-
37C, pH 7.0, enzyme from testis
3e-05
-
(pE)WPRPQIPP
-
37C, pH 7.0, recombinant wild-type enzyme
0.0001
-
(pE)WPRPQIPP
-
37C, pH 7.0, full-length mutant containing only a functional N-domain catalytic site
0.0018
-
1-[(5S)-4-oxo-6-phenyl-5-[(phenylcarbonyl)amino]hexanoyl]-L-proline
P12821
inhibition of C-domain
0.0452
-
1-[(5S)-4-oxo-6-phenyl-5-[(phenylcarbonyl)amino]hexanoyl]-L-proline
P12821
inhibition of N-domain
0.0336
-
1-[(5S)-5-[(tert-butoxycarbonyl)amino]-4-oxo-6-phenylhexanoyl]-L-proline
P12821
inhibition of N-domain
0.1435
-
1-[(5S)-5-[(tert-butoxycarbonyl)amino]-4-oxo-6-phenylhexanoyl]-L-proline
P12821
inhibition of C-domain
6e-06
-
2-(benzyloxy)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-phenylalanine
Q9BYF1
pH 7.5, angiotensin-converting enzyme 2
6.5e-05
-
2-(benzyloxy)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-phenylalanine
Q9BYF1
pH, angiotensin-converting enzyme 2
0.00077
-
2-(benzyloxy)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-phenylalanine
Q9BYF1
pH, angiotensin-converting enzyme
0.013
-
2-(benzyloxy)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-phenylalanine
Q9BYF1
pH, angiotensin-converting enzyme
2.4e-06
-
3-(benzyloxy)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-phenylalanine
Q9BYF1
pH 7.5, angiotensin-converting enzyme 2
8.4e-05
-
3-(benzyloxy)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-phenylalanine
Q9BYF1
pH 7.5, angiotensin-converting enzyme 2
0.00075
-
3-(benzyloxy)-N-[(2S)-3-methyl-2-sulfanylpentanoyl]-L-phenylalanine
Q9BYF1
pH 7.5, angiotensin-converting enzyme
2.747e-06
-
angiotensin I
-
-
0.035
-
angiotensin IV
-
pH 7.5
0.3176
-
Arg-Met-Leu
-
pH 8.5
0.365
-
benzyloxycarbonyl-PhePSI[PO2-CH]Ala-Ala
-
35C, pH 8.0
0.152
-
benzyloxycarbonyl-PhePSI[PO2-CH]Ala-Trp
-
35C, pH 8.0
1.278e-06
-
bradykinin
-
-
3e-07
-
Captopril
-
pH 7.5, 25C
5e-07
-
Captopril
-
pH 7.5, 37C, N-domain from lung enzyme
6e-07
-
Captopril
-
pH 7.5, 37C, enzyme from lung
1.38e-06
-
Captopril
-
-
9e-06
-
Captopril
-
pH 8.0, 37C, N-domain, hydrolysis of o-aminobenzoyl-SDK-(dinitrophenyl)-P-OH
9e-06
-
Captopril
-
pH 7.5, 37C, enzyme from testis
1e-05
-
Captopril
-
pH 8.0, 37C, wild-type enzyme, hydrolysis of o-aminobenzoyl-SDK-(dinitrophenyl)-P-OH
1.6e-05
-
Captopril
-
pH 8.0, 37C, C-domain, hydrolysis of o-aminobenzoyl-FRK-(dinitrophenyl)-P-OH
2.5e-05
-
Captopril
-
pH 8.0, 37C, N-domain, hydrolysis of o-aminobenzoyl-FRK-(dinitrophenyl)-P-OH
4.6e-05
-
Captopril
-
pH 8.0, 37C, wild-type enzyme, hydrolysis of o-aminobenzoyl-FRK-(dinitrophenyl)-P-OH
5.54e-05
-
Captopril
-
-
8.6e-05
-
Captopril
-
-
0.000191
-
Captopril
-
pH 8.0, 37C, C-domain, hydrolysis of o-aminobenzoyl-SDK-(dinitrophenyl)-P-OH
0.0569
-
cyanidin-3-O-sambubioside
-
pH 8.3, 37C
0.0319
-
delphinidin-3-O-sambubioside
-
pH 8.3, 37C
1.94e-06
-
enalaprilat
-
-
0.828
-
epicatechin
-
pH 8.3, 37C
0.124
-
epicatechin dimer
-
pH 8.3, 37C
0.0047
-
epicatechin hexamer
-
pH 8.3, 37C
0.0116
-
epicatechin pentamer
-
pH 8.3, 37C
0.0056
-
epicatechin tetramer
-
pH 8.3, 37C
0.059
-
epicatechin trimer
-
pH 8.3, 37C
8.3e-05
-
gluco-aurantioobtusin
-
in 50 mM Tris-HCl buffer (pH 7.5)
0.5547
-
Gly-Gln
-
pH 8.5
0.01148
-
Gly-Phe-Hyp-Gly-Thr-Hyp-Gly-Leu-Hyp-Gly-Phe
-
37C, pH 8.3
0.0072
-
Ile-Glu-Pro
-
-
0.055
-
Ile-Glu-Trp
-
-
0.0835
-
Ile-Glu-Tyr
-
-
0.0027
-
Ile-Lys-Pro
-
-
0.0085
-
Ile-Lys-Trp
-
-
0.013
-
Ile-Lys-Tyr
-
-
0.0005
-
Leu-Gln-Pro
-
-
0.00048
-
Leu-Lys-Tyr
-
-
0.00092
-
Leu-Val-Tyr
-
-
0.0028
-
LGFPTTKTYFPHF
-
-
1e-07
-
Lisinopril
-
-
1.2e-07
-
Lisinopril
-
pH 7.5, 37C, enzyme from testis
1.8e-07
-
Lisinopril
-
pH 7.5, 37C, enzyme from lung
2e-07
-
Lisinopril
-
pH 7.5, 37C, N-domain from lung enzyme
2.7e-07
-
Lisinopril
-
-
6e-07
-
Lisinopril
-
pH 7.5, 25C
1.2e-06
-
Lisinopril
-
pH 6.8, 25C, recombinant testis ACE C-domain
2.07e-06
-
Lisinopril
-
-
4.8e-06
-
Lisinopril
-
pH 6.8, 25C, recombinant testis ACE N-domain
9.96e-06
-
Lisinopril
-
-
5.1e-05
-
Lisinopril
P12821
inhibition of C-domain
0.0001315
-
Lisinopril
P12821
inhibition of N-domain
0.00028
-
Lisinopril
-
pH 8.3, 37C
6.6e-06
-
lisW-S
-
pH 6.8, 25C, recombinant testis ACE C-domain
0.0017
-
lisW-S
-
pH 6.8, 25C, recombinant testis ACE N-domain
0.0008
-
LRPARPTSPP
-
37C, pH 7.0, enzyme from testis
0.0026
-
LRPARPTSPP
-
37C, pH 7.0, recombinant wild-type enzyme
0.0032
-
LRPARPTSPP
-
37C, pH 7.0, full-length mutant containing only a functional C-domain catalytic site
0.017
-
LRPARPTSPP
-
37C, pH 7.0, full-length mutant containing only a functional N-domain catalytic site
0.0003
-
LRPARPTSPPA
-
37C, pH 7.0, enzyme from testis
0.0046
-
LRPARPTSPPA
-
37C, pH 7.0, full-length mutant containing only a functional C-domain catalytic site
0.012
-
LRPARPTSPPA
-
37C, pH 7.0, full-length mutant containing only a functional N-domain catalytic site
1.3e-05
-
N-(3-{[(1R)-1-{[(benzyloxy)carbonyl]amino}-2-phenylethyl](hydroxy)phosphoryl}-2-{[3-(biphenyl-4-yl)-4,5-dihydro-1,2-oxazol-5-yl]methyl}propanoyl)-L-tryptophan
-
pH and temperature not specified in the publication
9e-07
-
N-[(2S)-3-methyl-2-sulfanylpentanoyl]-2-phenoxy-L-phenylalanine
Q9BYF1
pH 7.5, angiotensin-converting enzyme 2
1.6e-06
-
N-[(2S)-3-methyl-2-sulfanylpentanoyl]-2-phenoxy-L-phenylalanine
Q9BYF1
pH 7.5, angiotensin-converting enzyme 2
0.0002
-
N-[(2S)-3-methyl-2-sulfanylpentanoyl]-2-phenoxy-L-phenylalanine
Q9BYF1
pH 7.5, angiotensin-converting enzyme
0.005
-
N-[(2S)-3-methyl-2-sulfanylpentanoyl]-2-phenoxy-L-phenylalanine
Q9BYF1
pH 7.5, angiotensin-converting enzyme
2.4e-06
-
N-[(2S)-3-methyl-2-sulfanylpentanoyl]-3-phenoxy-L-phenylalanine
Q9BYF1
pH 7.5, angiotensin-converting enzyme 2
5.8e-06
-
N-[(2S)-3-methyl-2-sulfanylpentanoyl]-3-phenoxy-L-phenylalanine
Q9BYF1
pH 7.5, angiotensin-converting enzyme 2
0.00062
-
N-[(2S)-3-methyl-2-sulfanylpentanoyl]-3-phenoxy-L-phenylalanine
Q9BYF1
pH 7.5, angiotensin-converting enzyme
0.0011
-
N-[(2S)-3-methyl-2-sulfanylpentanoyl]-3-phenoxy-L-phenylalanine
Q9BYF1
pH 7.5, angiotensin-converting enzyme
1.8e-06
-
N-[(2S)-3-methyl-2-sulfanylpentanoyl]-O-phenyl-L-tyrosine
Q9BYF1
pH 7.5, angiotensin-converting enzyme 2
2.2e-06
-
N-[(2S)-3-methyl-2-sulfanylpentanoyl]-O-phenyl-L-tyrosine
Q9BYF1
pH 7.5, angiotensin-converting enzyme 2
0.00025
-
N-[(2S)-3-methyl-2-sulfanylpentanoyl]-O-phenyl-L-tyrosine
Q9BYF1
pH 7.5, angiotensin-converting enzyme
0.0007
-
N-[(2S)-3-methyl-2-sulfanylpentanoyl]-O-phenyl-L-tyrosine
Q9BYF1
pH 7.5, angiotensin-converting enzyme
3.5e-05
-
N-[(2S)-3-methyl-2-sulfanylpentanoyl]-O-[4-(trifluoromethyl)benzyl]-L-tyrosine
Q9BYF1
pH 7.5, angiotensin-converting enzyme 2
9.3e-05
-
N-[(2S)-3-methyl-2-sulfanylpentanoyl]-O-[4-(trifluoromethyl)benzyl]-L-tyrosine
Q9BYF1
pH 7.5, angiotensin-converting enzyme
0.00086
-
N-[(2S)-3-methyl-2-sulfanylpentanoyl]-O-[4-(trifluoromethyl)benzyl]-L-tyrosine
Q9BYF1
pH 7.5, angiotensin-converting enzyme 2
0.0026
-
N-[(2S)-3-methyl-2-sulfanylpentanoyl]-