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(7-methoxycoumarin-4-yl)-acetyl-Ala-Pro-Lys(2,4-dinitrophenyl) + H2O
(7-methoxycoumarin-4-yl)-acetyl-Ala-Pro + N6-(2,4-dinitrophenyl)-L-Lys
-
-
-
-
?
(7-methoxycoumarin-4-yl)-acetyl-APK(2,4-dinitrophenyl) + H2O
(7-methoxycoumarin-4-yl)-acetyl-AP + N6-(2,4-dinitrophenyl)-L-Lys
-
-
-
-
?
(7-methoxycoumarin-4-yl)-acetyl-APK(2,4-dinitrophenyl)-OH + H2O
(7-methoxycoumarin-4-yl)-acetyl-AP + N6-(2,4-dinitrophenyl)-L-Lys
-
-
-
-
?
(7-methoxycoumarin-4-yl)-acetyl-Tyr-Val-Ala-Asp-Ala-Pro-Lys(2,4-dinitrophenyl)-OH + H2O
(7-methoxycoumarin-4-yl)-acetyl-Tyr-Val-Ala-Asp-Ala-Pro + N6-(2,4-dinitrophenyl)-L-Lys
-
-
-
?
(7-methoxycoumarin-4-yl)-acetyl-YVADAPK-(2,4-dinitrophenyl)-OH + H2O
(7-methoxycoumarin-4-yl)-acetyl-YVADAP + N6-(2,4-dinitrophenyl)-L-Lys
(7-methoxycoumarin-4-yl)-YVADAPK-(2,4-dinitrophenyl)-OH + H2O
(7-methoxycoumarin-4-yl)-YVADAP + N6-(2,4-dinitrophenyl)-L-lysine
-
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Ala-Pro-Lys(2,4-dinitrophenyl) + H2O
(7-methoxycoumarin-4-yl)acetyl-Ala-Pro + Lys(2,4-dinitrophenyl)
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Ala-Pro-Lys(2,4-dinitrophenyl) + H2O
(7-methoxycoumarin-4-yl)acetyl-Ala-Pro + N6-(2,4-dinitrophenyl)-L-lysine
-
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-APK(2,4-dinitrophenyl) + H2O
(7-methoxycoumarin-4-yl)acetyl-AP + N6-(2,4-dinitrophenyl)-L-lysine
(7-methoxycoumarin-4-yl)acetyl-APK(2,4-dinitrophenyl)-OH + H2O
(7-methoxycoumarin-4-yl)acetyl-AP + N6-(2,4-dinitrophenyl)-L-lysine
(7-methoxycoumarin-4-yl)acetyl-APK-(2,4-dinitrophenyl)-OH + H2O
?
-
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-APK-2,4-dinitrophenyl + H2O
(7-methoxycoumarin-4-yl)acetyl-AP + N6-(2,4-dinitrophenyl)-L-lysine
-
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-YVADAPK(2,4-dinitrophenyl)-OH + H2O
(7-methoxycoumarin-4-yl)acetyl-YVADAP + N6-(2,4-dinitrophenyl)-L-lysine
(des-Arg9)-bradykinin + H2O
?
-
-
-
-
?
7-methoxycoumarin-4-acetyl-Ala-Pro-Lys-(2,4-dinitrophenyl)-OH + H2O
?
-
-
-
-
?
7-methoxycoumarin-4-acetyl-Arg-Pro-Pro-Gly-Phe-Ser-Ala-Phe-Lys-(2,4-dinitrophenyl)-OH + H2O
?
7-methoxycoumarin-4-acetyl-Tyr-Val-Ala-Asp-Ala-Pro-Lys-(2,4-dinitrophenyl)-OH + H2O
?
amyloid-beta protein 43 + H2O
amyloid-beta protein 42 + ?
-
ACE2 converts amyloid-beta protein 43 to amyloid-beta protein 42 in mouse brain lysates
-
-
?
angiotensin I + H2O
angiotensin-(1-9) + Leu
angiotensin I + H2O
DRVYIHPFH + L-Leu
-
-
-
?
angiotensin II + H2O
angiotensin(1-7) + L-Phe
angiotensin II + H2O
angiotensin-(1-7) + L-Phe
angiotensin II + H2O
angiotensin-(1-7) + L-phenylalanine
-
-
-
-
?
angiotensin II + H2O
angiotensin-(1-7) + Phe
angiotensin II + H2O
DRVYIHP + L-Phe
-
-
-
?
angiotensin IV + H2O
VYIHP + Phe
-
-
-
-
?
angiotensin-(3-8) + H2O
angiotensin-(3-7) + Phe
-
-
-
ir
angiotensin-(4-8) + H2O
angiotensin-(4-7) + Phe
-
-
-
ir
angiotensin-(5-8) + H2O
angiotensin-(5-7) + Phe
-
-
-
ir
apelin 17 + H2O
?
-
-
-
?
apelin-13 + H2O
apelin-12 + Phe
-
-
-
?
apelin-13 + H2O
QRPRLSHKGPMP + Phe
apelin-36 + H2O
apelin-35 + Phe
beta-casomorphin + H2O
YPFVEP + Ile
-
-
-
-
?
casomorphin + H2O
?
-
-
-
-
?
des-Arg10-Lys-bradykinin + H2O
KRPPGFSP + Phe
-
-
-
-
?
des-Arg9-bradykinin + H2O
?
des-Arg9-bradykinin + H2O
bradykinin (1-7) + Phe
-
-
-
-
?
des-Arg9-bradykinin + H2O
RPPGFSP + Phe
-
-
-
-
?
dynorphin A 1-13 + H2O
dynorphin A 1-12 + Lys
-
-
-
ir
dynorphin A(1-13) + H2O
YGGFLRRIRPKL + Lys
-
-
-
-
?
ghrelin + H2O
?
-
-
-
-
?
ghrelin + H2O
ghrelin minus C-terminal amino acid + arginine
-
-
-
ir
kinetensin + H2O
?
-
-
-
-
?
KRPPGSPF + H2O
KRPPGSP + Phe
i.e. Lys-des-Arg-bradykinin
-
-
ir
Lys-des-Arg9 bradykinin + H2O
KRPPGFSP + Phe
-
-
-
-
?
Lys-des-Arg9-bradykinin + H2O
?
neocasomorphin + H2O
neocasomorphin minus C-terminal amino acid + isoleucine
-
-
-
ir
neurotensin 1-13 + H2O
?
-
-
-
-
?
neurotensin(1-11) + H2O
pELYENKPRRP + Tyr
-
-
-
-
?
neurotensin(1-8) + H2O
pELYENKP + Arg
-
-
-
-
?
neurotensin-(1-8) + H2O
neurotensin-(1-7) + arginine
-
-
-
ir
pyr-apelin 13 + H2O
?
-
-
-
?
QRPRLSHKGPMPF + H2O
QRPRLSHKGPMP + L-Phe
i.e. apein(1-13)
-
-
?
RPPGSPF + H2O
RPPGSP + Phe
SARS-coronavirus S1 protein + H2O
?
TBC5046 + H2O
o-aminobenzoic acid-des-Arg-bradykinin-(1-7) + 3-nitrophenylalanine
synthetic fluorogenic peptide, i.e. des-Arg-bradykinin with N-terminal o-aminobenzoic acid and a 3-nitrophenylalanine instead of Phe at the C-terminus
-
-
ir
YGGFLRRIRPKLK + H2O
YGGFLRRIRPKL + L-Lys
i.e. dynorphin A 1-13
-
-
?
YPVEPFI + H2O
YPVEPF + Ile
i.e. beta-casomorphin
-
-
ir
additional information
?
-
(7-methoxycoumarin-4-yl)-acetyl-YVADAPK-(2,4-dinitrophenyl)-OH + H2O
(7-methoxycoumarin-4-yl)-acetyl-YVADAP + N6-(2,4-dinitrophenyl)-L-Lys
-
-
-
-
?
(7-methoxycoumarin-4-yl)-acetyl-YVADAPK-(2,4-dinitrophenyl)-OH + H2O
(7-methoxycoumarin-4-yl)-acetyl-YVADAP + N6-(2,4-dinitrophenyl)-L-Lys
-
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-APK(2,4-dinitrophenyl) + H2O
(7-methoxycoumarin-4-yl)acetyl-AP + N6-(2,4-dinitrophenyl)-L-lysine
-
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-APK(2,4-dinitrophenyl) + H2O
(7-methoxycoumarin-4-yl)acetyl-AP + N6-(2,4-dinitrophenyl)-L-lysine
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-APK(2,4-dinitrophenyl) + H2O
(7-methoxycoumarin-4-yl)acetyl-AP + N6-(2,4-dinitrophenyl)-L-lysine
-
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-APK(2,4-dinitrophenyl)-OH + H2O
(7-methoxycoumarin-4-yl)acetyl-AP + N6-(2,4-dinitrophenyl)-L-lysine
synthetic fluorogenic substrate
-
-
?
(7-methoxycoumarin-4-yl)acetyl-APK(2,4-dinitrophenyl)-OH + H2O
(7-methoxycoumarin-4-yl)acetyl-AP + N6-(2,4-dinitrophenyl)-L-lysine
-
synthetic fluorogenic substrate
-
-
?
(7-methoxycoumarin-4-yl)acetyl-YVADAPK(2,4-dinitrophenyl)-OH + H2O
(7-methoxycoumarin-4-yl)acetyl-YVADAP + N6-(2,4-dinitrophenyl)-L-lysine
synthetic fluorogenic caspase-1 substrate
-
-
?
(7-methoxycoumarin-4-yl)acetyl-YVADAPK(2,4-dinitrophenyl)-OH + H2O
(7-methoxycoumarin-4-yl)acetyl-YVADAP + N6-(2,4-dinitrophenyl)-L-lysine
-
synthetic fluorogenic caspase-1 substrate
-
-
?
7-methoxycoumarin-4-acetyl-Arg-Pro-Pro-Gly-Phe-Ser-Ala-Phe-Lys-(2,4-dinitrophenyl)-OH + H2O
?
-
-
-
-
?
7-methoxycoumarin-4-acetyl-Arg-Pro-Pro-Gly-Phe-Ser-Ala-Phe-Lys-(2,4-dinitrophenyl)-OH + H2O
?
-
-
-
-
?
7-methoxycoumarin-4-acetyl-Tyr-Val-Ala-Asp-Ala-Pro-Lys-(2,4-dinitrophenyl)-OH + H2O
?
-
-
-
-
?
7-methoxycoumarin-4-acetyl-Tyr-Val-Ala-Asp-Ala-Pro-Lys-(2,4-dinitrophenyl)-OH + H2O
?
-
-
-
-
?
angiotensin I + H2O
angiotensin-(1-9) + Leu
-
-
-
-
?
angiotensin I + H2O
angiotensin-(1-9) + Leu
-
-
-
?
angiotensin I + H2O
angiotensin-(1-9) + Leu
-
-
-
-
?
angiotensin I + H2O
angiotensin-(1-9) + Leu
-
-
-
?
angiotensin I + H2O
angiotensin-(1-9) + Leu
-
-
-
-
?
angiotensin I + H2O
angiotensin-(1-9) + Leu
-
-
-
?
angiotensin I + H2O
angiotensin-(1-9) + Leu
-
-
-
-
?
angiotensin I + H2O
angiotensin-(1-9) + Leu
-
-
-
?
angiotensin I + H2O
angiotensin-(1-9) + Leu
-
-
-
-
?
angiotensin I + H2O
angiotensin-(1-9) + Leu
C-terminal bond between His-Leu is cleaved
-
-
?
angiotensin I + H2O
angiotensin-(1-9) + Leu
no angiotensin-converting activity, i.e. no conversion of the decapeptide angiotensin I to the octapeptide angiotensin II
-
-
?
angiotensin I + H2O
angiotensin-(1-9) + Leu
wild-type and truncated mutant
-
-
?
angiotensin I + H2O
angiotensin-(1-9) + Leu
-
poor affinity
-
-
?
angiotensin I + H2O
angiotensin-(1-9) + Leu
the affinity for Ang-I is poor in comparison with ACE, therefore the conversion of Ang-I to Ang-(1-9) is not of physiological importance, except maybe under conditions in which ACE activity is inhibited
-
-
?
angiotensin I + H2O
angiotensin-(1-9) + Leu
-
-
-
-
?
angiotensin I + H2O
angiotensin-(1-9) + Leu
-
-
-
?
angiotensin I + H2O
angiotensin-(1-9) + Leu
-
-
-
-
?
angiotensin I + H2O
angiotensin-(1-9) + Leu
-
ACE2 contributes to the production of angiotensin(1-7) from angiotensin I in proximal straight tubule
-
-
?
angiotensin I + H2O
angiotensin-(1-9) + Leu
-
-
-
?
angiotensin II + H2O
angiotensin(1-7) + L-Phe
-
-
-
-
?
angiotensin II + H2O
angiotensin(1-7) + L-Phe
-
-
-
?
angiotensin II + H2O
angiotensin(1-7) + L-Phe
-
-
-
-
?
angiotensin II + H2O
angiotensin(1-7) + L-Phe
-
Ang-(17) is a potential endogenous inhibitor of the classical renin-angiotensin system cascade
-
?
angiotensin II + H2O
angiotensin(1-7) + L-Phe
-
ACE2, a homologue of ACE, EC 3.4.15.1, converts angiotensin II into Ang(1-7). Ang(1-7) shows vasoprotective effects, serum autoantibodies to ACE2 predispose patients with connective tissue diseases to constrictive vasculopathy, pulmonary arterial hypertension, or persistent digital ischemia
-
-
?
angiotensin II + H2O
angiotensin(1-7) + L-Phe
cleavage of angiotensin II analogue is minimally affected by the binding of the SARS-CoV-2 spike protein
-
-
?
angiotensin II + H2O
angiotensin(1-7) + L-Phe
-
-
-
-
?
angiotensin II + H2O
angiotensin(1-7) + L-Phe
-
-
Ang(1-7) is a vasodilator peptide
-
?
angiotensin II + H2O
angiotensin(1-7) + L-Phe
-
i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe
i.e. Asp-Arg-Val-Tyr-Ile-His-Pro
-
?
angiotensin II + H2O
angiotensin(1-7) + L-Phe
-
angiotensin II has many adverse cardiovascular effects when acting through the AT1 receptor
-
-
?
angiotensin II + H2O
angiotensin(1-7) + L-Phe
-
-
-
-
?
angiotensin II + H2O
angiotensin(1-7) + L-Phe
-
-
-
-
?
angiotensin II + H2O
angiotensin(1-7) + L-Phe
-
i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe
i.e. Asp-Arg-Val-Tyr-Ile-His-Pro
-
?
angiotensin II + H2O
angiotensin(1-7) + L-Phe
-
angiotensin II has many adverse cardiovascular effects when acting through the AT1 receptor
-
-
?
angiotensin II + H2O
angiotensin(1-7) + L-Phe
-
high levels of angiotensin II induces pulmonary arterial hypertension
-
-
?
angiotensin II + H2O
angiotensin(1-7) + L-Phe
-
i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe, detection of myocardial ACE2 activity by surface enhanced laser desorption lionization time of flight mass spectroscopy, SELDI-TOF-MS
i.e. Asp-Arg-Val-Tyr-Ile-His-Pro
-
?
angiotensin II + H2O
angiotensin-(1-7) + L-Phe
-
-
-
-
?
angiotensin II + H2O
angiotensin-(1-7) + L-Phe
-
the enzyme is involved in the renin angiotensin system
-
-
?
angiotensin II + H2O
angiotensin-(1-7) + Phe
-
-
-
-
?
angiotensin II + H2O
angiotensin-(1-7) + Phe
-
-
-
?
angiotensin II + H2O
angiotensin-(1-7) + Phe
-
-
-
-
?
angiotensin II + H2O
angiotensin-(1-7) + Phe
-
-
-
?
angiotensin II + H2O
angiotensin-(1-7) + Phe
-
-
-
ir
angiotensin II + H2O
angiotensin-(1-7) + Phe
preferred substrate
-
-
?
angiotensin II + H2O
angiotensin-(1-7) + Phe
-
efficient cleavage
-
-
?
angiotensin II + H2O
angiotensin-(1-7) + Phe
400fold higher activity than with angiotensin I
-
-
?
angiotensin II + H2O
angiotensin-(1-7) + Phe
wild-type and truncated mutant
-
-
?
angiotensin II + H2O
angiotensin-(1-7) + Phe
-
the uteroplacental location of angiotensin (1-7) and ACE2 in pregnancy suggests an autocrine function of angiotensin(1-7) in the vasoactive regulation that characterizes placentation and establishes pregnancy
-
-
?
angiotensin II + H2O
angiotensin-(1-7) + Phe
the major role of ACE2 in Ang peptides metabolism is the production of Ang-(1-7). ACE2 also participates in the metabolism of other peptides non related to the renin-angiotensin system: apelin-13, neurotensin, kinetensin, dynorphin, [des-Arg9]-bradykinin, and [Lys-des-Arg9]-bradykinin
-
-
?
angiotensin II + H2O
angiotensin-(1-7) + Phe
ACE2 has approximately a 400fold greater affinity for Ang-II than Ang-I
-
-
?
angiotensin II + H2O
angiotensin-(1-7) + Phe
-
-
-
-
?
angiotensin II + H2O
angiotensin-(1-7) + Phe
-
-
-
?
angiotensin II + H2O
angiotensin-(1-7) + Phe
primary substrate
-
-
?
angiotensin II + H2O
angiotensin-(1-7) + Phe
-
-
-
-
?
angiotensin II + H2O
angiotensin-(1-7) + Phe
-
-
-
?
angiotensin II + H2O
angiotensin-(1-7) + Phe
-
ACE2 is highly regulated at transcription. ACE2 plays a critical role in regulating the balance between vasoconstrictor and vasodilator effects within the RAS cascade. Angiotensin II may be a stimulus determining cardiac ACE2 gene expression, because either reduction in its levels or prevention of angiotensin II binding to the AT1 receptor increases ACE2 mRNA. ACE2 serves as the cellular entry point for severe acute respiratory syndrome (SARS) virus
-
-
?
angiotensin II + H2O
angiotensin-(1-7) + Phe
hepatic production of Ang-(1-7) is catalysed by ACE2
-
-
?
apelin-13 + H2O
?
-
-
-
-
?
apelin-13 + H2O
?
-
high catalytic efficiency
-
-
?
apelin-13 + H2O
?
-
high catalytic efficiency
-
-
?
apelin-13 + H2O
QRPRLSHKGPMP + Phe
-
-
-
-
?
apelin-13 + H2O
QRPRLSHKGPMP + Phe
-
-
-
-
?
apelin-36 + H2O
?
-
-
-
-
?
apelin-36 + H2O
?
-
high catalytic efficiency
-
-
?
apelin-36 + H2O
?
-
high catalytic efficiency
-
-
?
apelin-36 + H2O
apelin-35 + Phe
-
-
-
?
apelin-36 + H2O
apelin-35 + Phe
-
-
-
-
?
beta-casomorphin + H2O
?
-
-
-
-
?
beta-casomorphin + H2O
?
-
-
-
-
?
des-Arg9-bradykinin + H2O
?
ACE2 cleavage of des-Arg9-bradykinin substrate analogue is markedly accelerated by SARS-CoV-2 infection
-
-
?
des-Arg9-bradykinin + H2O
?
-
-
-
-
?
des-Arg9-bradykinin + H2O
?
-
-
-
-
?
dynorphin A + H2O
?
-
-
-
-
?
dynorphin A + H2O
?
-
-
-
-
?
Lys-des-Arg9-bradykinin + H2O
?
-
-
-
-
?
Lys-des-Arg9-bradykinin + H2O
?
-
-
-
-
?
neurotensin + H2O
?
-
-
-
-
?
neurotensin + H2O
?
-
-
-
-
?
RPPGSPF + H2O
RPPGSP + Phe
i.e. des-Arg-bradykinin
i.e. des-Arg-bradykinin-(1-7)
-
ir
RPPGSPF + H2O
RPPGSP + Phe
-
i.e. des-Arg-bradykinin
i.e. des-Arg-bradykinin-(1-7)
-
ir
SARS-coronavirus S1 protein + H2O
?
-
-
-
?
SARS-coronavirus S1 protein + H2O
?
-
-
-
?
SARS-coronavirus S1 protein + H2O
?
-
-
-
?
SARS-coronavirus S1 protein + H2O
?
-
-
-
?
additional information
?
-
-
angiotensin-converting enzyme 2: a functional receptor for SARS coronavirus
-
-
?
additional information
?
-
-
presence of ACE2 alone is not sufficient for maintaining viral infection. Other virus receptors or coreceptors may be required in different tissues
-
-
?
additional information
?
-
-
the enzyme has a function in blood pressure regulation, blood flow and fluid regulation. Loss of ACE2 impairs heart function
-
-
?
additional information
?
-
-
the enzyme is involved in diesease condition including hypertension, diabetes and cardiac function. ACE2 is the SARS virus receptor
-
-
?
additional information
?
-
-
angiotensin I is not a good substrate for recombinant human ACE2
-
-
?
additional information
?
-
-
no activity with angiotensin (1-9) and angiotensin(1-7)
-
-
?
additional information
?
-
-
no hydrolysis of angiotensin (1-9), angiotensin (1-7), bradikinin, bradykinin(1-7), neurotensin(1-13)
-
-
?
additional information
?
-
-
the ACE2 ectodomain can be cleaved from the cell membrane and released into the extracellular milieu by stimulation of phorbol esters and ADAM17, calmodulin inhibits shedding of the ACE2 ectodomain from the membrane
-
-
?
additional information
?
-
ACE2 ectodomain shedding and/or sheddase(s) activation regulated by calmodulin is independent from the phorbol ester-induced shedding
-
-
?
additional information
?
-
ACE2 is down-regulated and ACE is up-regulated in hypertensive nephropathy. Ang II, once released, can act to up-regulate ACE but down-regulate ACE2 via the AT1 receptor-mediated mechanism. Activation of the ERK1/2 and p38 MAP kinase pathway may represent a key mechanism by which Ang II down-regulates ACE2
-
-
?
additional information
?
-
ACE2 is involved in the regulation of heart function, ACE 2 is a functional receptor for the coronavirus that causes the severe acute respiratory syndrome
-
-
?
additional information
?
-
ACE2 plays a key role in pulmonary, cardiovascular and hypertensive and diabetic kidney diseases. ACE2 plays a pivotal role in maintaining a balanced status of the RAS synergistically with ACE by exerting counter-regulatory effects
-
-
?
additional information
?
-
ACE2 plays a protective role in organs directly related to hypertension and associated diseases
-
-
?
additional information
?
-
the affinity for Ang-I is poor in comparison with ACE, therefore the conversion of Ang-I to Ang-(1-9) is not of physiological importance, except maybe under conditions in which ACE activity is inhibited
-
-
?
additional information
?
-
ACE2 functions predominantly as a carboxymonopeptidase with a substrate preference for hydrolysis between proline and a hydrophobic or basic C-terminal residue
-
-
?
additional information
?
-
hydrolyses its substrates by removing a single amino acid from their respective C-terminal
-
-
?
additional information
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ACE2 is a terminal carboxypeptidase and the receptor for the SARS and NL63 coronaviruses. Soluble sACE2 acts as receptor binding SARS-CoV glycoprotein S pseudotyped FIV virus and blocks virus infection of target cells
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ACE2 is a terminal carboxypeptidase and the receptor for the SARS and NL63 coronaviruses. Soluble sACE2 acts as receptor binding SARS-CoV glycoprotein S pseudotyped FIV virus and blocks virus infection of target cells
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the requirements for ACE2 binding at the first position of a tetrapeptide substrate, i.e. fourth position from the Ang II C-terminus XHPF, are a preference for non-polar, hydrophobic or cyclic residues, with Val and Pro substitutions showing enhanced binding. No strict preference is observed at position two of the tetrapeptide IXPF. Apolar cyclic residues Phe and Pro are not tolerated at the position. Substitution of position three results in moderate increases in binding for Val, 77% and decreases for Ile. The only other functional group tolerated at this position is naphthalene. Peptides PYPF/PHVF/PYVF show almost equivalent ACE2 binding compared to full-length angiotensin II
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ACE2 is a crucial SARS-CoV receptor. SARS-CoV infections and the Spike protein of the SARS-CoV reduce ACE2 expression. Injection of SARS-CoV Spike into mice worsens acute lung failure in vivo that can be attenuated by blocking the renin-angiotensin pathway
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ACE2 functions as a carboxymonopeptidase with a preference for C-terminal Leu or Phe, ACE2 counterbalances the enzymatic actions of ACE, ACE2 does not metabolize bradykinin
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ACE2 plays a pivotal role in the central regulation of blood pressure and volume homeostasis
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ACE2 plays a pivotal role in the central regulation of blood pressure and volume homeostasis
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ACE2 activation promotes antithrombotic activity. ACE2 is an ACE, EC 3.4.15.1, homologue
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a combination of ACE2 and ACE convert amyloid-beta protein 43 to amyloid-beta protein 40
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ACE2 functions as a carboxymonopeptidase with a preference for C-terminal Leu or Phe, ACE2 counterbalances the enzymatic actions of ACE, ACE2 does not metabolize bradykinin
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ACE2 plays a crucial role in liver fibrogenesis
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ACE2 activation promotes antithrombotic activity. ACE2 is an ACE, EC 3.4.15.1, homologue
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