Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(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
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
ACE2 plays a pivotal role in the central regulation of blood pressure and volume homeostasis
-
-
?
additional information
?
-
-
ACE2 plays a pivotal role in the central regulation of blood pressure and volume homeostasis
-
-
?
additional information
?
-
-
ACE2 activation promotes antithrombotic activity. ACE2 is an ACE, EC 3.4.15.1, homologue
-
-
?
additional information
?
-
-
a combination of ACE2 and ACE convert amyloid-beta protein 43 to amyloid-beta protein 40
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
ACE2 plays a crucial role in liver fibrogenesis
-
-
?
additional information
?
-
-
ACE2 activation promotes antithrombotic activity. ACE2 is an ACE, EC 3.4.15.1, homologue
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(2S)-3-(biphenyl-4-yl)-2-((3S)-2-mercapto-3-methylpentanamido)propanoic acid
-
(2S)-3-biphenyl-4-yl-2-[(2-methyl-2-sulfanylpropanoyl)amino]propanoic acid
-
(2S)-3-biphenyl-4-yl-2-[(2-sulfanylpropanoyl)amino]propanoic acid
-
(2S)-3-biphenyl-4-yl-2-[(sulfanylacetyl)amino]propanoic acid
-
(2S)-3-biphenyl-4-yl-2-[[(2R)-2-sulfanylbutanoyl]amino]propanoic acid
-
(2S)-3-biphenyl-4-yl-2-[[(2R)-3-methyl-2-sulfanylbutanoyl]amino]propanoic acid
-
(2S)-3-biphenyl-4-yl-2-[[(2R)-3-phenyl-2-sulfanylpropanoyl]amino]propanoic acid
-
(2S)-3-biphenyl-4-yl-2-[[(2S)-2-phenyl-2-sulfanylacetyl]amino]propanoic acid
-
(2S)-3-biphenyl-4-yl-2-[[(2S)-2-sulfanylhexanoyl]amino]propanoic acid
-
(2S)-3-biphenyl-4-yl-2-[[(2S)-3-phenyl-2-sulfanylpropanoyl]amino]propanoic acid
-
(2S)-3-biphenyl-4-yl-2-[[cyclobutyl(sulfanyl)acetyl]amino]propanoic acid
-
(S)-3-(biphenyl-4-yl)-2-((2R,3R)-2-mercapto-3-methylpentanamido)propanoic acid
-
(S)-3-(biphenyl-4-yl)-2-((R)-2-cyclohexyl-2-mercaptoacetamido)propanoic acid
-
(S)-3-(biphenyl-4-yl)-2-((R)-2-cyclopentyl-2-mercaptoacetamido)propanoic acid
-
(S)-3-(biphenyl-4-yl)-2-((R)-2-mercapto-3-(naphthalen-2-yl)propanamido)propanoic acid
-
(S)-3-(biphenyl-4-yl)-2-((R)-2-mercapto-4,4-dimethylpentanamido)propanoic acid
-
(S)-3-(biphenyl-4-yl)-2-((R)-2-mercapto-4-methylpentanamido)propanoic acid
-
(S)-3-(biphenyl-4-yl)-2-((R)-2-mercapto-4-phenylbutanamido)propanoic acid
-
(S)-3-(biphenyl-4-yl)-2-((R)-3-cyclohexyl-2-mercaptopropanamido)propanoic acid
-
(S,S)-2-[1-carboxy-2-[3-(3,5-dichlorobenzyl)-3H-inidazol-4-yl]-ethylamino]-4-methylpentanoic acid
-
MLN-4760
(S,S)-2-{1-carboxy-2-[3-(3,5-dichlorobenzyl)-3H-imidazol-4-yl]-ethylamino}-4-methylpentanoic acid
i.e MLN-4760
1,3,8-trihydroxy-6-methylanthraquinone
-
1,3,8-trihydroxy-6-methylanthraquinone (emodin) blocks interaction between the SARS corona virus spike protein and its receptor angiotensin-converting enzyme 2, 94.12% inhibition at 0.05 mM
1,4-bis-(1-anthraquinonylamino)-anthraquinone
-
slight inhibition
1,8,dihydroxy-3-carboxyl-9,10-anthraquinone
-
1,8,dihydroxy-3-carboxyl-9,10-anthraquinone (rhein) exhibits slight inhibition
10-hydroxyusambarensine
binding energy -10.4 kcal/mol, and binding energy to SARS-CoV-2 spike protein is -9.4 kcal/mol
-
1N-08795
-
90% inhibition at 0.2 mM
1N-26923
-
93% inhibition at 0.2 mM
1N-27714
-
89% inhibition at 0.2 mM
1N-28616
-
93% inhibition at 0.2 mM
1S-90995
-
11% inhibition at 0.2 mM
1S-91206
-
75% inhibition at 0.2 mM
2-benzyl-3-(hydroxy-pyrrolidin-2-yl-phosphinoyl)-propionic acid
-
2-benzyl-3-[(1-benzyloxycarbonylamino-2-phenyl-ethyl)-hydroxy-phosphinoyl]-propionic acid
-
2-benzyl-3-[(1-benzyloxycarbonylamino-3-methyl-butyl)-hydroxy-phosphinoyl]-propionic acid
-
2-benzyl-3-[(1-benzyloxycarbonylamino-ethyl)-hydroxy-phosphinoyl]-propionic acid
-
2-methylphenyl-benzylsuccinic acid
-
2-[(2-carboxy-3-phenyl-propyl)-hydroxy-phosphinoyl]-pyrrolidine-1-carboxylic acid benzyl ester
-
2-[(2-carboxy-4-methyl-pentyl)-hydroxy-phosphinoyl]-pyrrolidine-1-carboxylic acid benzyl ester
-
2-[(2-carboxy-propyl)-hydroxy-phosphinoyl]-pyrrolidine-1-carboxylic acid benzyl ester
-
3,4-dimethylphenyl-benzylsuccinic acid
-
3,5-dichloro-benzylsuccinate
-
3,5-dimethylphenyl-benzylsuccinic acid
-
3-([1-[2-acetylamino-3-(1H-imidazol-4-yl)-propionylamino]-3-methyl-butyl]-hydroxy-phosphinoyl)-2-(3-phenyl-isoxazol-5-ylmethyl)-propionic acid
-
3-([1-[2-acetylamino-3-(1H-imidazol-4-yl)-propionylamino]-3-methyl-butyl]-hydroxy-phosphinoyl)-2-benzyl-propionic acid
-
3-([1-[2-acetylamino-3-(1H-imidazol-4-yl)-propionyl]-pyrrolidin-2-yl]-hydroxy-phosphinoyl)-2-(3-phenyl-isoxazol-5-ylmethyl)-propionic acid
-
3-([1-[2-acetylamino-3-(1H-imidazol-4-yl)-propionyl]-pyrrolidin-2-yl]-hydroxy-phosphinoyl)-2-benzyl-propionic acid
-
3-([1-[2-acetylamino-3-(4-hydroxy-phenyl)-propionyl]-pyrrolidin-2-yl]-hydroxy-phosphinoyl)-2-benzyl-propionic acid
-
3-methylphenyl-benzylsuccinic acid
-
3-[(1-amino-2-phenyl-ethyl)-hydroxy-phosphinoyl]-2-benzylpropionic acid
-
3-[(1-amino-3-methyl-butyl)-hydroxy-phosphinoyl]-2-benzylpropionic acid
-
3-[(1-amino-ethyl)-hydroxy-phosphinoyl]-2-benzyl-propionic acid
-
3-[[1-(2-acetylamino-3-methyl-butyryl)-pyrrolidin-2-yl]-hydroxy-phosphinoyl]-2-benzyl-propionic acid
-
3-[[1-(2-acetylamino-3-phenyl-propionyl)-pyrrolidin-2-yl]-hydroxy-phosphinoyl]-2-benzyl-propionic acid
-
3-[[1-(2-acetylamino-4-methyl-pentanoyl)-pyrrolidin-2-yl]-hydroxy-phosphinoyl]-2-(3-phenyl-isoxazol-5-ylmethyl)-propionic acid
-
3-[[1-(2-acetylamino-4-methyl-pentanoyl)-pyrrolidin-2-yl]-hydroxy-phosphinoyl]-2-benzyl-propionic acid
-
3-[[1-(2-acetylamino-4-methyl-pentanoylamino)-2-phenylethyl]-hydroxy-phosphinoyl]-2-benzyl-propionic acid
-
3-[[1-(2-acetylamino-6-amino-hexanoyl)-pyrrolidin-2-yl]-hydroxy-phosphinoyl]-2-benzyl-propionic acid
-
3-[[1-(2-acetylamino-propionyl)-pyrrolidin-2-yl]-hydroxyphosphinoyl]-2-benzyl-propionic acid
-
3S-95223
-
40% inhibition at 0.2 mM
4-acetylamino-5-[2-[(2-carboxy-3-phenyl-propyl)-hydroxyphosphinoyl]-pyrrolidin-1-yl]-5-oxo-pentanoic acid
-
4-methylphenyl-benzylsuccinic acid
-
4-nitrophenyl-benzylsuccinic acid
-
4S-14713
-
70% inhibition at 0.2 mM
4S-16659
-
76% inhibition at 0.2 mM
5,7-dihydroxyflavone
-
5,7-dihydroxyflavone (chrysin) is a weak inhibitor
5115980
-
1% inhibition at 0.2 mM
6-gingerol
inhibition of the ACE2 enzyme
7490938
-
20% inhibition at 0.2 mM
7850455
-
20% inhibition at 0.2 mM
7857351
-
27% inhibition at 0.2 mM
7870029
-
11% inhibition at 0.2 mM
Ac-GDYSHCSPLRYYPWWKCTYPDPEGGG-NH2
strong inhibition, most potent inhibitory peptide, i.e. DX600
Ac-GDYSHCSPLRYYPWWPDPEGGG-NH2
-
i.e. DX600
amentoflvaone
inhibitor of SARS-CoV-2-(receptor binding domain):ACE2 complex
-
Amphotericin B
binding affinity -10.50 kcal/mol, favorable binding modes, critical interactions, and pharmaceutical properties
andrographolide
inhibition of the ACE2 enzyme
angiotensin II C-terminal analogs
-
screening of a library of angiotensin II C-terminal analogs identifies a number of tetrapeptides with increased ACE2 inhibition, and identifies residues critical to the binding of angiotensin II to the active site of ACE2
-
anthraquinone
-
slight inhibition
apigenin
inhibition of the ACE2 enzyme
arbidol
inhibitor of SARS-CoV-2-(receptor binding domain):ACE2 complex
-
artemisnin
inhibition of the ACE2 enzyme
-
asparoside C
inhibitor of SARS-CoV-2-(receptor binding domain):ACE2 complex
-
AY-NH2
inhibitor of SARS-CoV-2-(receptor binding domain):ACE2 complex
-
benzyl (6aS,9aS)-10-benzyl-4-[benzyl(methyl)amino]-8-(cyclopropanecarbonyl)-6a,7,8,9,9a,10-hexahydrocyclopenta[b]pyrimido[4,5-e][1,4]diazepine-6(5H)-carboxylate
inhibits the protein-protein interaction between ACE2 and the receptor-binding domain of SARS-CoV-2 spike protein and suppresses SARS-CoV-2 infection in cultured cells by inhibiting viral entry via the modulation of ACE2. The compound does not have any adverse effect on ACE2 function
-
benzyl (6aS,9aS)-4-[benzyl(methyl)amino]-10-[(4-chlorophenyl)methyl]-8-(cyclopropanecarbonyl)-6a,7,8,9,9a,10-hexahydrocyclopenta[b]pyrimido[4,5-e][1,4]diazepine-6(5H)-carboxylate
inhibits the protein-protein interaction between ACE2 and the receptor-binding domain of SARS-CoV-2 spike protein and suppresses SARS-CoV-2 infection in cultured cells by inhibiting viral entry via the modulation of ACE2. The compound does not have any adverse effect on ACE2 function
-
benzyl (6aS,9aS)-4-[benzyl(methyl)amino]-8-(cyclopropanecarbonyl)-10-[(4-methylphenyl)methyl]-6a,7,8,9,9a,10-hexahydrocyclopenta[b]pyrimido[4,5-e][1,4]diazepine-6(5H)-carboxylate
inhibits the protein-protein interaction between ACE2 and the receptor-binding domain of SARS-CoV-2 spike protein and suppresses SARS-CoV-2 infection in cultured cells by inhibiting viral entry via the modulation of ACE2. The compound does not have any adverse effect on ACE2 function
-
benzylsuccinate
-
essentially abolishes the formation of Ang(1-9) by ACE2
Berberine
inhibition of the ACE2 enzyme
beta-sitosterol
inhibition of the ACE2 enzyme
bis-demethoxy curcumin
inhibitor of SARS-CoV-2-(receptor binding domain):ACE2 complex
cepharanthine
potential inhibitor of the SARS-CoV-2-S protein:ACE2 complex
chebulagic acid
inhibitor of SARS-CoV-2-(receptor binding domain):ACE2 complex
-
chrysin
shows a strong affinity for the active site of ACE2, ACE2-inhibitor complexes display structural stability with suitable binding energies. The interaction of chrysin with Phe40, Asp350, and Gly352 on ACE2 can interfere with the binding of SARS-CoV-2
crisimaritin
inhibition of the ACE2 enzyme
-
cryptoquindoline
binding energy -9.9 kcal/mol, and binding energy to SARS-CoV-2 spike protein is -9.5 kcal/mol
-
cryptospirolepine
binding energy -10.7 kcal/mol, and binding energy to SARS-CoV-2 spike protein is -10.6 kcal/mol
-
Cu2+
-
69% inhibition at 0.01 mM
cucurbitacin B
inhibition of the ACE2 enzyme
curcumin
inhibition of the ACE2 enzyme
cyclohexyl-benzylsuccinic acid
-
cynaropicrin
inhibition of the ACE2 enzyme
darunavir
inhibitor of SARS-CoV-2-(receptor binding domain):ACE2 complex
denopamine
inhibitor of SARS-CoV-2-(receptor binding domain):ACE2 complex
dicyclohexyl-benzylsuccinic acid
-
digitoxin
binding affinity -11.25 kcal/mol, favorable binding modes, critical interactions, and pharmaceutical properties
dithymoquinone
inhibitor of SARS-CoV-2-(receptor binding domain):ACE2 complex
-
DRVYIYbetaPF
-
angiotensin II chimera prepared by combining key elements of ACE2 binding and proteolytic stability, 90% inhibition at 10 microM and complete resistance to cleavage over 5 h
DRVYIYPF
-
angiotensin II chimera prepared by combining key elements of ACE2 binding and proteolytic stability, 96% inhibition at 10 microM and 18% cleavage over 5h
ergoloid
potential inhibitor of the SARS-CoV-2-S protein:ACE2 complex
-
eriodictyol
potential inhibitor of the SARS-CoV-2-S protein:ACE2 complex
Evans blue
inhibits viral replication in a Vero-E6 cell-based SARS-CoV-2 infection assay
favipiravir
potential inhibitor of the SARS-CoV-2-S protein:ACE2 complex
glycyrrhizinate
binding affinity -11.75 kcal/mol, favorable binding modes, critical interactions, and pharmaceutical properties
hesperidin
inhibition of the ACE2 enzyme; inhibitor of SARS-CoV-2-(receptor binding domain):ACE2 complex
hispudulin
inhibition of the ACE2 enzyme
-
hypericin
potential inhibitor of the SARS-CoV-2-S protein:ACE2 complex
Ile-Pro-Pro
-
inhibits EC 3.4.15.1 at one-thousandth of the concentration needed to inhibit ACE2
isocryptolepine
binding energy to SARS-CoV-2 spike protein is -9.7 kcal/mol
-
isoniazid pyruvate
potential inhibitor of the SARS-CoV-2-S protein:ACE2 complex
-
isothymol
inhibition of the ACE2 enzyme
-
Leu-Pro-Pro
-
inhibits EC 3.4.15.1 at one-thousandth of the concentration needed to inhibit ACE2
lumacaftor
inhibits viral replication in a Vero-E6 cell-based SARS-CoV-2 infection assay
-
luteolin
shows a strong affinity for the active site of ACE2, ACE2-inhibitor complexes display structural stability with suitable binding energies
menthol
potential inhibitor of the SARS-CoV-2-S protein:ACE2 complex
methylene blue
binding energy -4.89 kcal/mol, KD value 0.621mM
N-acetyl-D-glucosamine
binding energy -5.6 kcal/mol
N-[(1S)-1-carboxy-3-methylbutyl]-3-(3,5-dichlorobenzyl)-L-histidine
enzyme-specific inhibitor
N-[(1S)-1-carboxy-3-methylbutyl]-3-(3,5-dichlorophenyl)-L-histidine
-
i.e. C16, a ACE2 specific inhibitor
naringin
inhibition of the ACE2 enzyme
neoandrographolide
inhibitor of SARS-CoV-2-(receptor binding domain):ACE2 complex
Nitrofurantoin
potential inhibitor of the SARS-CoV-2-S protein:ACE2 complex
orientin
inhibition of the ACE2 enzyme
paritaprevir
inhibition of the ACE2 enzyme
phenylbenzylsuccinic acid
-
PHVF
-
angiotensin II analog, shows almost saturating levels of inhibition at the screening concentration of 100 microm
piceatannol
inhibitor of SARS-CoV-2-(receptor binding domain):ACE2 complex
pimozide
effectively binds to the ACE2 binding site for SARS-CoV-2 spike protein, does not show stability during molecular dynamics simulation
pseudojervine
inhibitor of SARS-CoV-2-(receptor binding domain):ACE2 complex
-
PYPF
-
angiotensin II analog, shows almost saturating levels of inhibition at the screening concentration of 100 microm
PYVF
-
angiotensin II analog, shows almost saturating levels of inhibition at the screening concentration of 100 microm
quercetin-3-O-galatosyl-rhamnosyl-glucoside
inhibitor of SARS-CoV-2-(receptor binding domain):ACE2 complex
-
Quinacrine
KD value 0.102 mM
Rapamycin
binding affinity -10.57 kcal/mol, favorable binding modes, critical interactions, and pharmaceutical properties
raspberry ketone
potential inhibitor of the SARS-CoV-2-S protein:ACE2 complex
-
rifaximin
binding affinity -10.54 kcal/mol, favorable binding modes, critical interactions, and pharmaceutical properties
-
rutin
inhibition of the ACE2 enzyme
rutin DAB10
inhibitor of SARS-CoV-2-(receptor binding domain):ACE2 complex
-
saikosaponin A
inhibition of the ACE2 enzyme
sennoside A
binding energy -4.51 kcal/mol, KD value 0.041 mM
sodium lifitegrast
inhibits viral replication in a Vero-E6 cell-based SARS-CoV-2 infection assay
-
spinochrome A
inhibitor of SARS-CoV-2-(receptor binding domain):ACE2 complex
-
strychnopentamine
binding energy -9.9 kcal/mol
-
sunitinib
KD value 0.781 mM
T0507-4963
-
41% inhibition at 0.2 mM
T0513-5544
-
4% inhibition at 0.2 mM
T0515-3007
-
13% inhibition at 0.2 mM
telmisartan
-
specific angiotensin II type 1 receptor blocker
thymoquinone
potential inhibitor of the SARS-CoV-2-S protein:ACE2 complex
Ursodeoxycholic acid
effectively binds to the ACE2 binding site for SARS-CoV-2 spike protein, does not show stability during molecular dynamics simulation
Val-Pro-Pro
-
inhibits EC 3.4.15.1 at one-thousandth of the concentration needed to inhibit ACE2
varenicline
binding energy -4.42 kcal/mol, KD value 0.017 mM
-
vitexin
inhibition of the ACE2 enzyme
angiotensin I
-
Cl-
inhibition is substrate dependent, inhibitory with substrate angiotensin II
Cl-
ACE2 activity is regulated by chloride ions. The presence of chloride increases the hydrolysis of angiotensin I by ACE2, but inhibits cleavage of the vasoconstrictor angiotensin II
DX600
-
IC50: 10 nM
DX600
-
competitive inhibitor, 0.1 mM
DX600
-
competitive inhibitor, 0.1 mM
DX600
-
0.01 mM, 99% inhibition
DX600
-
a decrease in thrombus ACE2 activity is associated with increased thrombus formation in nude mice
DX600
-
competitive inhibitor, 0.1 mM
DX600
-
a decrease in thrombus ACE2 activity is associated with increased thrombus formation in spontaneously hypertensive rats
EDTA
no inhibition by benzylsuccinate, no inhibition by lisinopril, no inhibition by captopril, no inhibition by enalaprilat
EDTA
-
complete inhibition at 10 mM
hydroxychloroquine
docks at the active site of the Human ACE2 receptor as a possible way of inhibition; malaria drug hydroxychloroquine docks at the active site of the human ACE2 receptor as a possible way of inhibition, with a docking score and glide energy of -6.34 and -49.34 kcal/mol, respectively. Hydroxychloroquine forms two hydrogen bond interactions with active site amino acids of Asp367 and Asn277 at distances of 2.65 A and 2.85 A, respectively. In addition, pi-pi interactions are also observed from the active site of His345, and ionic interactions are found with Lys363
hydroxychloroquine
potential inhibitor of the SARS-CoV-2-S protein:ACE2 complex
ivermectin
inhibition of the ACE2 enzyme; potential inhibitor of the SARS-CoV-2-S protein:ACE2 complex
ivermectin
binding affinity -10.87 kcal/mol, favorable binding modes, critical interactions, and pharmaceutical properties
MLN 4760
-
IC50: 3 nM
MLN-4760
-
i.e. (SS) 2-[(1)-carboxy-2-[3-(3,5-dichlorobenzyl)-3H-imidazol-4-yl]ethylamino]-4-methyl-pentanoic acid, IC50: 0.44 nM
MLN-4760
ACE2-specific inhibitor. Inhibition of wild-type ACE2 was sensitive to chloride concentration
MLN-4760
i.e. ((S,S)-2-[1-carboxy-2-[3-(3,5-dichlorobenzyl)-3H-imidazol4-yl]-ethylamino]-4-methylpentanoic acid)
MLN-4760
inhibitor of SARS-CoV-2-(receptor binding domain):ACE2 complex
MLN-4760
binding energy -7.0 kcal/mol
MLN-4760
-
total inhibition at 0.01 mM
MLN-4760
-
specific inhibitor, 1 mM
Pro-Phe
-
IC50: 0.15 mM
quercetin
inhibition of the ACE2 enzyme
quercetin
KD value 0.130 mM
additional information
no inhibition by lisinopril
-
additional information
no inhibition by captopril
-
additional information
-
no inhibition by captopril
-
additional information
no inhibition by enalaprilat
-
additional information
-
no inhibition by enalaprilat
-
additional information
no inhibition by lisinopril, no inhibition by captopril, no inhibition by enalaprilat
-
additional information
construction of 6 constrained peptide libraries, selected from peptide libraries displayed on phage, peptides, 21-27 amino acids, with inhibitory effects on the enzyme, specificity and stability, selection of inhibitory sequence motifs, best CXPXRXXPWXXC, overview
-
additional information
-
construction of 6 constrained peptide libraries, selected from peptide libraries displayed on phage, peptides, 21-27 amino acids, with inhibitory effects on the enzyme, specificity and stability, selection of inhibitory sequence motifs, best CXPXRXXPWXXC, overview
-
additional information
-
carboxylalkyl compounds cilazaprilat, indolaprilat, perindoprilat, quinaprilat and spiraprilat, the thiol compounds rentiapril and zofenapril, and the phosphoryl compounds ceranopril and fosinoprilat fail to inhibit the hydrolysis of either angiotensin I or angiotensin II by ACE2 at concentrations that abolished activity of EC 3.4.15.1
-
additional information
-
ACE-2 mRNA and activity are severely downregulated in lung fibrosis
-
additional information
-
not inhibited by captopri and lisinopril
-
additional information
-
not inhibited by Ca2+, Cd2+, Co2+, Mg2+, Mn2+, and Zn2+
-
additional information
-
GM6001 does not have any effect on the activity of ACE2 and little effect on basal shedding of ACE2
-
additional information
-
not inhibited by rentiapril, ceranopril, indolaprilat, zofenoprilat, spiraprilat, quinaprilat, perindoprilat, fosinoprilat, cilazaprilat, captopril, lisinopril, and enalaprilat
-
additional information
identification of compounds that bind to either the angiotensin converting enzyme 2 (ACE2) and/or the SARS-CoV-2 spike protein receptor binding domain (SARS-CoV-2 spike protein RBD). All 22 identified compounds provide scaffolds for the development of new chemical entities for the treatment of COVID-19
-
additional information
-
identification of compounds that bind to either the angiotensin converting enzyme 2 (ACE2) and/or the SARS-CoV-2 spike protein receptor binding domain (SARS-CoV-2 spike protein RBD). All 22 identified compounds provide scaffolds for the development of new chemical entities for the treatment of COVID-19
-
additional information
inhibitors of SARS-CoV-2:ACE2 binding
-
additional information
ACE2 activity is not regulated by ibuprofen, flurbiprofen, etoricoxib or paracetamol
-
additional information
-
ACE-2 mRNA and activity are severely downregulated in lung fibrosis
-
additional information
-
the Spike protein of the SARS-coronavirus reduces ACE2 expression
-
additional information
-
not inhibited by captopril and benzyloxycarbonyl-Pro-Pro
-
additional information
-
central angiotensin II type 1 receptors reduce ACE2 expression/activity in hypertensive mice
-
additional information
ACE2 activity in plasma is not altered by ibuprofen treatment
-
additional information
-
rampiril does not influence the mRNA content in renal tubules
-
additional information
-
ACE-2 mRNA and activity are severely downregulated in lung fibrosis
-
additional information
-
ACE2 is insensitive to ACE inhibitors
-
additional information
-
chronic cigarette smoke administration causes an reduction in ACE2 activity and increases angiotensin II levels in the lung
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0000015
(2S)-3-(biphenyl-4-yl)-2-((3S)-2-mercapto-3-methylpentanamido)propanoic acid
apparent value, in (7-methoxycoumarin-4-yl)-acetyl-Tyr-Val-Ala-Asp-Ala-Pro-Lys(2,4-dinitrophenyl)-OH as substrate in 0.001 mM Zn(OAc)2, 0.1 mM TCEP, 50 mM HEPES, 0.3 mM CHAPS, and 300 mM NaCl, at pH 7.5
0.0023
(2S)-3-biphenyl-4-yl-2-[(2-methyl-2-sulfanylpropanoyl)amino]propanoic acid
apparent value, in (7-methoxycoumarin-4-yl)-acetyl-Tyr-Val-Ala-Asp-Ala-Pro-Lys(2,4-dinitrophenyl)-OH as substrate in 0.001 mM Zn(OAc)2, 0.1 mM TCEP, 50 mM HEPES, 0.3 mM CHAPS, and 300 mM NaCl, at pH 7.5
0.0000069
(2S)-3-biphenyl-4-yl-2-[(2-sulfanylpropanoyl)amino]propanoic acid
apparent value, in (7-methoxycoumarin-4-yl)-acetyl-Tyr-Val-Ala-Asp-Ala-Pro-Lys(2,4-dinitrophenyl)-OH as substrate in 0.001 mM Zn(OAc)2, 0.1 mM TCEP, 50 mM HEPES, 0.3 mM CHAPS, and 300 mM NaCl, at pH 7.5
0.00032
(2S)-3-biphenyl-4-yl-2-[(sulfanylacetyl)amino]propanoic acid
apparent value, in (7-methoxycoumarin-4-yl)-acetyl-Tyr-Val-Ala-Asp-Ala-Pro-Lys(2,4-dinitrophenyl)-OH as substrate in 0.001 mM Zn(OAc)2, 0.1 mM TCEP, 50 mM HEPES, 0.3 mM CHAPS, and 300 mM NaCl, at pH 7.5
0.0000014
(2S)-3-biphenyl-4-yl-2-[[(2R)-2-sulfanylbutanoyl]amino]propanoic acid
apparent value, in (7-methoxycoumarin-4-yl)-acetyl-Tyr-Val-Ala-Asp-Ala-Pro-Lys(2,4-dinitrophenyl)-OH as substrate in 0.001 mM Zn(OAc)2, 0.1 mM TCEP, 50 mM HEPES, 0.3 mM CHAPS, and 300 mM NaCl, at pH 7.5
0.0000015
(2S)-3-biphenyl-4-yl-2-[[(2R)-3-methyl-2-sulfanylbutanoyl]amino]propanoic acid
apparent value, in (7-methoxycoumarin-4-yl)-acetyl-Tyr-Val-Ala-Asp-Ala-Pro-Lys(2,4-dinitrophenyl)-OH as substrate in 0.001 mM Zn(OAc)2, 0.1 mM TCEP, 50 mM HEPES, 0.3 mM CHAPS, and 300 mM NaCl, at pH 7.5
0.000086
(2S)-3-biphenyl-4-yl-2-[[(2R)-3-phenyl-2-sulfanylpropanoyl]amino]propanoic acid
apparent value, in (7-methoxycoumarin-4-yl)-acetyl-Tyr-Val-Ala-Asp-Ala-Pro-Lys(2,4-dinitrophenyl)-OH as substrate in 0.001 mM Zn(OAc)2, 0.1 mM TCEP, 50 mM HEPES, 0.3 mM CHAPS, and 300 mM NaCl, at pH 7.5
0.000084
(2S)-3-biphenyl-4-yl-2-[[(2S)-2-phenyl-2-sulfanylacetyl]amino]propanoic acid
apparent value, in (7-methoxycoumarin-4-yl)-acetyl-Tyr-Val-Ala-Asp-Ala-Pro-Lys(2,4-dinitrophenyl)-OH as substrate in 0.001 mM Zn(OAc)2, 0.1 mM TCEP, 50 mM HEPES, 0.3 mM CHAPS, and 300 mM NaCl, at pH 7.5
0.0000018
(2S)-3-biphenyl-4-yl-2-[[(2S)-2-sulfanylhexanoyl]amino]propanoic acid
apparent value, in (7-methoxycoumarin-4-yl)-acetyl-Tyr-Val-Ala-Asp-Ala-Pro-Lys(2,4-dinitrophenyl)-OH as substrate in 0.001 mM Zn(OAc)2, 0.1 mM TCEP, 50 mM HEPES, 0.3 mM CHAPS, and 300 mM NaCl, at pH 7.5
0.0014
(2S)-3-biphenyl-4-yl-2-[[(2S)-3-phenyl-2-sulfanylpropanoyl]amino]propanoic acid
apparent value, in (7-methoxycoumarin-4-yl)-acetyl-Tyr-Val-Ala-Asp-Ala-Pro-Lys(2,4-dinitrophenyl)-OH as substrate in 0.001 mM Zn(OAc)2, 0.1 mM TCEP, 50 mM HEPES, 0.3 mM CHAPS, and 300 mM NaCl, at pH 7.5
0.0000024
(2S)-3-biphenyl-4-yl-2-[[cyclobutyl(sulfanyl)acetyl]amino]propanoic acid
apparent value, in (7-methoxycoumarin-4-yl)-acetyl-Tyr-Val-Ala-Asp-Ala-Pro-Lys(2,4-dinitrophenyl)-OH as substrate in 0.001 mM Zn(OAc)2, 0.1 mM TCEP, 50 mM HEPES, 0.3 mM CHAPS, and 300 mM NaCl, at pH 7.5
0.0000016
(S)-3-(biphenyl-4-yl)-2-((2R,3R)-2-mercapto-3-methylpentanamido)propanoic acid
apparent value, in (7-methoxycoumarin-4-yl)-acetyl-Tyr-Val-Ala-Asp-Ala-Pro-Lys(2,4-dinitrophenyl)-OH as substrate in 0.001 mM Zn(OAc)2, 0.1 mM TCEP, 50 mM HEPES, 0.3 mM CHAPS, and 300 mM NaCl, at pH 7.5
0.000065
(S)-3-(biphenyl-4-yl)-2-((R)-2-cyclohexyl-2-mercaptoacetamido)propanoic acid
apparent value, in (7-methoxycoumarin-4-yl)-acetyl-Tyr-Val-Ala-Asp-Ala-Pro-Lys(2,4-dinitrophenyl)-OH as substrate in 0.001 mM Zn(OAc)2, 0.1 mM TCEP, 50 mM HEPES, 0.3 mM CHAPS, and 300 mM NaCl, at pH 7.5
0.0000018
(S)-3-(biphenyl-4-yl)-2-((R)-2-cyclopentyl-2-mercaptoacetamido)propanoic acid
apparent value, in (7-methoxycoumarin-4-yl)-acetyl-Tyr-Val-Ala-Asp-Ala-Pro-Lys(2,4-dinitrophenyl)-OH as substrate in 0.001 mM Zn(OAc)2, 0.1 mM TCEP, 50 mM HEPES, 0.3 mM CHAPS, and 300 mM NaCl, at pH 7.5
0.00055
(S)-3-(biphenyl-4-yl)-2-((R)-2-mercapto-3-(naphthalen-2-yl)propanamido)propanoic acid
apparent value, in (7-methoxycoumarin-4-yl)-acetyl-Tyr-Val-Ala-Asp-Ala-Pro-Lys(2,4-dinitrophenyl)-OH as substrate in 0.001 mM Zn(OAc)2, 0.1 mM TCEP, 50 mM HEPES, 0.3 mM CHAPS, and 300 mM NaCl, at pH 7.5
0.0000071
(S)-3-(biphenyl-4-yl)-2-((R)-2-mercapto-4,4-dimethylpentanamido)propanoic acid
apparent value, in (7-methoxycoumarin-4-yl)-acetyl-Tyr-Val-Ala-Asp-Ala-Pro-Lys(2,4-dinitrophenyl)-OH as substrate in 0.001 mM Zn(OAc)2, 0.1 mM TCEP, 50 mM HEPES, 0.3 mM CHAPS, and 300 mM NaCl, at pH 7.5
0.0000014
(S)-3-(biphenyl-4-yl)-2-((R)-2-mercapto-4-methylpentanamido)propanoic acid
apparent value, in (7-methoxycoumarin-4-yl)-acetyl-Tyr-Val-Ala-Asp-Ala-Pro-Lys(2,4-dinitrophenyl)-OH as substrate in 0.001 mM Zn(OAc)2, 0.1 mM TCEP, 50 mM HEPES, 0.3 mM CHAPS, and 300 mM NaCl, at pH 7.5
0.00086
(S)-3-(biphenyl-4-yl)-2-((R)-2-mercapto-4-phenylbutanamido)propanoic acid
apparent value, in (7-methoxycoumarin-4-yl)-acetyl-Tyr-Val-Ala-Asp-Ala-Pro-Lys(2,4-dinitrophenyl)-OH as substrate in 0.001 mM Zn(OAc)2, 0.1 mM TCEP, 50 mM HEPES, 0.3 mM CHAPS, and 300 mM NaCl, at pH 7.5
0.00042
(S)-3-(biphenyl-4-yl)-2-((R)-3-cyclohexyl-2-mercaptopropanamido)propanoic acid
apparent value, in (7-methoxycoumarin-4-yl)-acetyl-Tyr-Val-Ala-Asp-Ala-Pro-Lys(2,4-dinitrophenyl)-OH as substrate in 0.001 mM Zn(OAc)2, 0.1 mM TCEP, 50 mM HEPES, 0.3 mM CHAPS, and 300 mM NaCl, at pH 7.5
0.000044
(S,S)-2-[1-carboxy-2-[3-(3,5-dichlorobenzyl)-3H-inidazol-4-yl]-ethylamino]-4-methylpentanoic acid
-
-
0.00581
10-hydroxyusambarensine
pH not specified in the publication, temperature not specified in the publication
-
0.01
2-benzyl-3-(hydroxy-pyrrolidin-2-yl-phosphinoyl)-propionic acid
Ki above 0.01 mM
0.01
2-benzyl-3-[(1-benzyloxycarbonylamino-2-phenyl-ethyl)-hydroxy-phosphinoyl]-propionic acid
Ki above 0.01 mM
0.008
2-benzyl-3-[(1-benzyloxycarbonylamino-3-methyl-butyl)-hydroxy-phosphinoyl]-propionic acid
-
0.01
2-benzyl-3-[(1-benzyloxycarbonylamino-ethyl)-hydroxy-phosphinoyl]-propionic acid
Ki above 0.01 mM
0.0003
2-[(2-carboxy-3-phenyl-propyl)-hydroxy-phosphinoyl]-pyrrolidine-1-carboxylic acid benzyl ester
-
0.003
2-[(2-carboxy-4-methyl-pentyl)-hydroxy-phosphinoyl]-pyrrolidine-1-carboxylic acid benzyl ester
-
0.003
2-[(2-carboxy-propyl)-hydroxy-phosphinoyl]-pyrrolidine-1-carboxylic acid benzyl ester
-
0.00022
3-([1-[2-acetylamino-3-(1H-imidazol-4-yl)-propionylamino]-3-methyl-butyl]-hydroxy-phosphinoyl)-2-(3-phenyl-isoxazol-5-ylmethyl)-propionic acid
-
0.0008
3-([1-[2-acetylamino-3-(1H-imidazol-4-yl)-propionylamino]-3-methyl-butyl]-hydroxy-phosphinoyl)-2-benzyl-propionic acid
-
0.0000004
3-([1-[2-acetylamino-3-(1H-imidazol-4-yl)-propionyl]-pyrrolidin-2-yl]-hydroxy-phosphinoyl)-2-(3-phenyl-isoxazol-5-ylmethyl)-propionic acid
-
0.0000021
3-([1-[2-acetylamino-3-(1H-imidazol-4-yl)-propionyl]-pyrrolidin-2-yl]-hydroxy-phosphinoyl)-2-benzyl-propionic acid
-
0.0000052
3-([1-[2-acetylamino-3-(4-hydroxy-phenyl)-propionyl]-pyrrolidin-2-yl]-hydroxy-phosphinoyl)-2-benzyl-propionic acid
-
0.01
3-[(1-amino-2-phenyl-ethyl)-hydroxy-phosphinoyl]-2-benzylpropionic acid
Ki above 0.01 mM
0.01
3-[(1-amino-3-methyl-butyl)-hydroxy-phosphinoyl]-2-benzylpropionic acid
Ki above 0.01 mM
0.01
3-[(1-amino-ethyl)-hydroxy-phosphinoyl]-2-benzyl-propionic acid
Ki above 0.01 mM
0.00000035
3-[[1-(2-acetylamino-3-methyl-butyryl)-pyrrolidin-2-yl]-hydroxy-phosphinoyl]-2-benzyl-propionic acid
-
0.0000052
3-[[1-(2-acetylamino-3-phenyl-propionyl)-pyrrolidin-2-yl]-hydroxy-phosphinoyl]-2-benzyl-propionic acid
-
0.00000125
3-[[1-(2-acetylamino-4-methyl-pentanoyl)-pyrrolidin-2-yl]-hydroxy-phosphinoyl]-2-(3-phenyl-isoxazol-5-ylmethyl)-propionic acid
-
0.0000066
3-[[1-(2-acetylamino-4-methyl-pentanoyl)-pyrrolidin-2-yl]-hydroxy-phosphinoyl]-2-benzyl-propionic acid
-
0.00092
3-[[1-(2-acetylamino-4-methyl-pentanoylamino)-2-phenylethyl]-hydroxy-phosphinoyl]-2-benzyl-propionic acid
-
0.0000065
3-[[1-(2-acetylamino-6-amino-hexanoyl)-pyrrolidin-2-yl]-hydroxy-phosphinoyl]-2-benzyl-propionic acid
-
0.0000075
3-[[1-(2-acetylamino-propionyl)-pyrrolidin-2-yl]-hydroxyphosphinoyl]-2-benzyl-propionic acid
-
0.000007
4-acetylamino-5-[2-[(2-carboxy-3-phenyl-propyl)-hydroxyphosphinoyl]-pyrrolidin-1-yl]-5-oxo-pentanoic acid
-
0.0028
Ac-GDYSHCSPLRYYPWWKCTYPDPEGGG-NH2
pH 8.0, room temperature with substrate angiotensin I, pH 7.4, room temperature with substrate (7-methoxycoumarin-4-yl)acetyl-YVADAPK(2,4-dinitrophenyl)-OH
0.00267
cryptospirolepine
pH not specified in the publication, temperature not specified in the publication
-
0.0256
MLN-4760
pH not specified in the publication, temperature not specified in the publication
0.0657
N-acetyl-D-glucosamine
pH not specified in the publication, temperature not specified in the publication
0.00445
strychnopentamine
pH not specified in the publication, temperature not specified in the publication
-
additional information
additional information
-
0.0022
angiotensin I
-
-
additional information
additional information
Ki values of peptides from constrained peptide libraries
-
additional information
additional information
-
Ki values of peptides from constrained peptide libraries
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
drug target
angiotensin converting enzyme 2 (ACE2) is the receptor of SARS-CoV-2, but only ACE2 of certain species can be utilized by SARS-CoV-2. SARS-CoV-2 tends to utilize ACE2 of various mammals, except murines, and some birds, such as pigeon. This prediction may help to screen the intermediate hosts of SARS-CoV-2. SARS-CoV-2 has a high genetic relationship with a bat coronavirus (BatCoV RaTG13) with a 96% genomic nucleotide sequence identity. The close phylogenetic relationship to Bat RaTG13 provides evidence for a bat origin of SARS-CoV-2. Direct transmission of the virus from bats to humans is unlikely due to the lack of direct contact between bats and humans (in Wuhan, China). There are probably intermediate hosts transmitting SARS-CoV-2 to humans. Combined phylogenetic analysis and critical site marking is used to predict the utilizing capability of ACE2 from different animal species by SARS-CoV-2. It is confirmed that pangolin (Manis javanica), cat (Felis catus), cow (Bos taurus), buffalo (Bubalus bubalis), goat (Capra hircus), sheep (Ovis aries) and pigeon (Columba livia) ACE2 might be utilized by SARS-CoV-2, indicating potential interspecies transmission of the virus from bats to these animals and among these animals
drug target
angiotensin-converting enzyme 2 (ACE2) fused to the Fc portion of immunoglobulin neutralizes SARS-CoV-2 in vitro. Provision of soluble recombinant human ACE2 protein can be beneficial as a novel biologic therapeutic to combat or limit infection progression caused by coronaviruses that utilize ACE2 as a receptor. If given in its soluble form as an appropriate recombinant ACE2 protein, a new tool may be at hand to combat the spread of coronavirus in susceptible individuals by limiting coronavirus attachment to the cell membranes, cell entry, and replication
drug target
antibodies and small molecular inhibitors that can block the interaction of the enzyme (ACE2) with the receptor binding domain can to combat the virus SARS-CoV-2
drug target
potential therapeutic approach to ACE2-mediated COVID-19. Treatment with a soluble form of ACE2 may exert dual functions, slow viral entry into cells and hence viral spread and protect the lung from injury
drug target
ACE2-based therapeutics confer a broad-spectrum neutralization potency for ACE2-tropic viruses, including SARS-CoV-2 variants
drug target
coronaviruses use the receptor-binding domain (RBD) of their glycosylated S protein to bind to cell specific surface receptors and initiate membrane fusion and virus entry. For both SARS-CoV and SARS-CoV-2, this involves binding to human angiotensin converting enzyme 2 (hACE2) followed by proteolytic activation by human proteases. Blockade of the receptor-binding domain-hACE2 protein-protein interaction (PPI) can disrupt infection efficiency. Screening of organic dyes and related novel druglike compounds leads to the identification of several small-molecule compounds showing promising broad-spectrum inhibition of the protein-protein interaction between coronavirus spike proteins and their cognate ACE2 receptor. Several of them, including dyes, such as Congo red and direct violet 1, but especially novel nondye compounds, such as DRI-23041 are able to inhibit the entry of SARSCoV-2-S expressing pseudoviruses into ACE2-expressing cells in a concentration-dependent manner
drug target
Food and Drug administration(FDA) approved drugs are examined for inhibiting serine protease TMPRSS2 and human ACE. Valrubicin and lopinavir have the least degree of toxicity
drug target
polyunsaturated fatty acids most effectively interfere with binding to hACE2, the receptor for SARSCoV-2. Using a spike protein pseudo-virus, linolenic acid and eicosapentaenoic acid significantly block the entry of SARS-CoV-2. In addition, eicosapentaenoic acid shows higher efficacy than linolenic acid in reducing activity of TMPRSS2 and cathepsin L proteases, but neither of the fatty acids affected their expression at the protein level. Also, neither reduction of hACE2 activity nor binding to the hACE2 receptor upon treatment with these two fatty acids is observed
drug target
SARS-CoV-2 spike protein uses the angiotensin converting enzyme 2 (ACE2) as a cellular receptor to initiate infection. Compounds that interfere with the SARS-CoV-2 spike protein receptor binding domain protein (RBD)-ACE2 receptor interaction may function as entry inhibitors
drug target
the enzyme (ACE2) plays an important role, facilitating the movement of SARSCoV-2 through the cell membrane. ED compound (Chembridge ID 7781334) will provide the basis for developing a drug that interacts with the angiotensin-converting enzyme 2 (ACE2). Drugs based on ED could hinder or prevent the interaction of ACE2 with SARS-CoV-2
evolution
ACE2 is widely expressed in the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Remarkably, its structure is highly conserved. Comparison of human ACE2 with that of a civet (Paguma larvata), a bat (Rhinolophus sinicus), a bird (Nipponia nippon), a snake (Protobothrops mucrosquamatus), a frog (Xenopus laevis), and a fish (Callorhinchus milii) reveal amino acid sequence identity of 83%, 81%, 83%, 61%, 60%, and 59%, respectively
evolution
ACE2 is widely expressed in the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Remarkably, its structure is highly conserved. Comparison of human ACE2 with that of a civet (Paguma larvata), a bat (Rhinolophus sinicus), a bird (Nipponia nippon), a snake (Protobothrops mucrosquamatus), a frog (Xenopus laevis), and a fish (Callorhinchus milii) reveal amino acid sequence identity of 83%, 81%, 83%, 61%, 60%, and 59%, respectively
evolution
ACE2 is widely expressed in the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Remarkably, its structure is highly conserved. Comparison of human ACE2 with that of a civet (Paguma larvata), a bat (Rhinolophus sinicus), a bird (Nipponia nippon), a snake (Protobothrops mucrosquamatus), a frog (Xenopus laevis), and a fish (Callorhinchus milii) reveal amino acid sequence identity of 83%, 81%, 83%, 61%, 60%, and 59%, respectively
evolution
ACE2 is widely expressed in the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Remarkably, its structure is highly conserved. Comparison of human ACE2 with that of a civet (Paguma larvata), a bat (Rhinolophus sinicus), a bird (Nipponia nippon), a snake (Protobothrops mucrosquamatus), a frog (Xenopus laevis), and a fish (Callorhinchus milii) reveal amino acid sequence identity of 83%, 81%, 83%, 61%, 60%, and 59%, respectively
evolution
XP_029140508.1
ACE2 is widely expressed in the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Remarkably, its structure is highly conserved. Comparison of human ACE2 with that of a civet (Paguma larvata), a bat (Rhinolophus sinicus), a bird (Nipponia nippon), a snake (Protobothrops mucrosquamatus), a frog (Xenopus laevis), and a fish (Callorhinchus milii) reveal amino acid sequence identity of 83%, 81%, 83%, 61%, 60%, and 59%, respectively
evolution
XP_018104311.1
ACE2 is widely expressed in the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Remarkably, its structure is highly conserved. Comparison of human ACE2 with that of a civet (Paguma larvata), a bat (Rhinolophus sinicus), a bird (Nipponia nippon), a snake (Protobothrops mucrosquamatus), a frog (Xenopus laevis), and a fish (Callorhinchus milii) reveal amino acid sequence identity of 83%, 81%, 83%, 61%, 60%, and 59%, respectively
evolution
XP_007889845.1
ACE2 is widely expressed in the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Remarkably, its structure is highly conserved. Comparison of human ACE2 with that of a civet (Paguma larvata), a bat (Rhinolophus sinicus), a bird (Nipponia nippon), a snake (Protobothrops mucrosquamatus), a frog (Xenopus laevis), and a fish (Callorhinchus milii) reveal amino acid sequence identity of 83%, 81%, 83%, 61%, 60%, and 59%, respectively
evolution
Spike protein of SARS-CoV-2 exhibits the highest binding to human (h)ACE2 of all the species tested, forming the highest number of hydrogen bonds with hACE2. Pangolin (Manis javanica) ACE2 shows the next highest binding affinity despite having a relatively low sequence homology, whereas the affinity of monkey ACE2 is much lower despite its high sequence similarity to hACE2. ACE2 species in the upper half of the predicted affinity range (Macaca fascicularis, Mesocricetus auratus, Canis luparis, Mustela putorius furot, Felis catus) are permissive to SARS-CoV-2 infection, supporting a correlation between binding affinity and infection susceptibility
evolution
Spike protein of SARS-CoV-2 exhibits the highest binding to human (h)ACE2 of all the species tested, forming the highest number of hydrogen bonds with hACE2. Pangolin (Manis javanica) ACE2 shows the next highest binding affinity despite having a relatively low sequence homology, whereas the affinity of monkey ACE2 is much lower despite its high sequence similarity to hACE2. ACE2 species in the upper half of the predicted affinity range (Macaca fascicularis, Mesocricetus auratus, Canis luparis, Mustela putorius furot, Felis catus) are permissive to SARS-CoV-2 infection, supporting a correlation between binding affinity and infection susceptibility
evolution
Spike protein of SARS-CoV-2 exhibits the highest binding to human (h)ACE2 of all the species tested, forming the highest number of hydrogen bonds with hACE2. Pangolin (Manis javanica) ACE2 shows the next highest binding affinity despite having a relatively low sequence homology, whereas the affinity of monkey ACE2 is much lower despite its high sequence similarity to hACE2. ACE2 species in the upper half of the predicted affinity range (Macaca fascicularis, Mesocricetus auratus, Canis luparis, Mustela putorius furot, Felis catus) are permissive to SARS-CoV-2 infection, supporting a correlation between binding affinity and infection susceptibility
evolution
Spike protein of SARS-CoV-2 exhibits the highest binding to human (h)ACE2 of all the species tested, forming the highest number of hydrogen bonds with hACE2. Pangolin (Manis javanica) ACE2 shows the next highest binding affinity despite having a relatively low sequence homology, whereas the affinity of monkey ACE2 is much lower despite its high sequence similarity to hACE2. ACE2 species in the upper half of the predicted affinity range (Macaca fascicularis, Mesocricetus auratus, Canis luparis, Mustela putorius furot, Felis catus) are permissive to SARS-CoV-2 infection, supporting a correlation between binding affinity and infection susceptibility
evolution
XP_017505752.1
Spike protein of SARS-CoV-2 exhibits the highest binding to human (h)ACE2 of all the species tested, forming the highest number of hydrogen bonds with hACE2. Pangolin (Manis javanica) ACE2 shows the next highest binding affinity despite having a relatively low sequence homology, whereas the affinity of monkey ACE2 is much lower despite its high sequence similarity to hACE2. ACE2 species in the upper half of the predicted affinity range (Macaca fascicularis, Mesocricetus auratus, Canis luparis, Mustela putorius furot, Felis catus) are permissive to SARS-CoV-2 infection, supporting a correlation between binding affinity and infection susceptibility
evolution
Spike protein of SARS-CoV-2 exhibits the highest binding to human (h)ACE2 of all the species tested, forming the highest number of hydrogen bonds with hACE2. Pangolin (Manis javanica) ACE2 shows the next highest binding affinity despite having a relatively low sequence homology, whereas the affinity of monkey ACE2 is much lower despite its high sequence similarity to hACE2. ACE2 species in the upper half of the predicted affinity range (Macaca fascicularis, Mesocricetus auratus, Canis luparis, Mustela putorius furot, Felis catus) are permissive to SARS-CoV-2 infection, supporting a correlation between binding affinity and infection susceptibility
evolution
Spike protein of SARS-CoV-2 exhibits the highest binding to human (h)ACE2 of all the species tested, forming the highest number of hydrogen bonds with hACE2. Pangolin (Manis javanica) ACE2 shows the next highest binding affinity despite having a relatively low sequence homology, whereas the affinity of monkey ACE2 is much lower despite its high sequence similarity to hACE2. ACE2 species in the upper half of the predicted affinity range (Macaca fascicularis, Mesocricetus auratus, Canis luparis, Mustela putorius furot, Felis catus) are permissive to SARS-CoV-2 infection, supporting a correlation between binding affinity and infection susceptibility
evolution
XP_007090142
Spike protein of SARS-CoV-2 exhibits the highest binding to human (h)ACE2 of all the species tested, forming the highest number of hydrogen bonds with hACE2. Pangolin (Manis javanica) ACE2 shows the next highest binding affinity despite having a relatively low sequence homology, whereas the affinity of monkey ACE2 is much lower despite its high sequence similarity to hACE2. ACE2 species in the upper half of the predicted affinity range (Macaca fascicularis, Mesocricetus auratus, Canis luparis, Mustela putorius furot, Felis catus) are permissive to SARS-CoV-2 infection, supporting a correlation between binding affinity and infection susceptibility
evolution
Spike protein of SARS-CoV-2 exhibits the highest binding to human (h)ACE2 of all the species tested, forming the highest number of hydrogen bonds with hACE2. Pangolin (Manis javanica) ACE2 shows the next highest binding affinity despite having a relatively low sequence homology, whereas the affinity of monkey ACE2 is much lower despite its high sequence similarity to hACE2. ACE2 species in the upper half of the predicted affinity range (Macaca fascicularis, Mesocricetus auratus, Canis luparis, Mustela putorius furot, Felis catus) are permissive to SARS-CoV-2 infection, supporting a correlation between binding affinity and infection susceptibility
evolution
Spike protein of SARS-CoV-2 exhibits the highest binding to human (h)ACE2 of all the species tested, forming the highest number of hydrogen bonds with hACE2. Pangolin (Manis javanica) ACE2 shows the next highest binding affinity despite having a relatively low sequence homology, whereas the affinity of monkey ACE2 is much lower despite its high sequence similarity to hACE2. ACE2 species in the upper half of the predicted affinity range (Macaca fascicularis, Mesocricetus auratus, Canis luparis, Mustela putorius furot, Felis catus) are permissive to SARS-CoV-2 infection, supporting a correlation between binding affinity and infection susceptibility
evolution
Spike protein of SARS-CoV-2 exhibits the highest binding to human (h)ACE2 of all the species tested, forming the highest number of hydrogen bonds with hACE2. Pangolin (Manis javanica) ACE2 shows the next highest binding affinity despite having a relatively low sequence homology, whereas the affinity of monkey ACE2 is much lower despite its high sequence similarity to hACE2. ACE2 species in the upper half of the predicted affinity range (Macaca fascicularis, Mesocricetus auratus, Canis luparis, Mustela putorius furot, Felis catus) are permissive to SARS-CoV-2 infection, supporting a correlation between binding affinity and infection susceptibility
evolution
Spike protein of SARS-CoV-2 exhibits the highest binding to human (h)ACE2 of all the species tested, forming the highest number of hydrogen bonds with hACE2. Pangolin (Manis javanica) ACE2 shows the next highest binding affinity despite having a relatively low sequence homology, whereas the affinity of monkey ACE2 is much lower despite its high sequence similarity to hACE2. ACE2 species in the upper half of the predicted affinity range (Macaca fascicularis, Mesocricetus auratus, Canis luparis, Mustela putorius furot, Felis catus) are permissive to SARS-CoV-2 infection, supporting a correlation between binding affinity and infection susceptibility
evolution
J9P7Y2
Spike protein of SARS-CoV-2 exhibits the highest binding to human (h)ACE2 of all the species tested, forming the highest number of hydrogen bonds with hACE2. Pangolin (Manis javanica) ACE2 shows the next highest binding affinity despite having a relatively low sequence homology, whereas the affinity of monkey ACE2 is much lower despite its high sequence similarity to hACE2. ACE2 species in the upper half of the predicted affinity range (Macaca fascicularis, Mesocricetus auratus, Canis luparis, Mustela putorius furot, Felis catus) are permissive to SARS-CoV-2 infection, supporting a correlation between binding affinity and infection susceptibility
evolution
Spike protein of SARS-CoV-2 exhibits the highest binding to human (h)ACE2 of all the species tested, forming the highest number of hydrogen bonds with hACE2. Pangolin (Manis javanica) ACE2 shows the next highest binding affinity despite having a relatively low sequence homology, whereas the affinity of monkey ACE2 is much lower despite its high sequence similarity to hACE2. ACE2 species in the upper half of the predicted affinity range (Macaca fascicularis, Mesocricetus auratus, Canis luparis, Mustela putorius furot, Felis catus) are permissive to SARS-CoV-2 infection, supporting a correlation between binding affinity and infection susceptibility
evolution
the binding surface of ACE2 from several important animal species is analyzed to understand the parameters for the ACE2 recognition by the SARSCoV-2 spike protein receptor binding domain (RBD). Recombinant ACE2 from human, hamster, horseshoe bat, cat, ferret, and cow are evaluated for RBD binding. A gradient of binding affinities are seen where human and hamster ACE2 are similarly in the low nanomolar range, followed by cat and cow. Horseshoe bat (Rhinolophus sinicus) and ferret (Mustela putorius) ACE2s have poor binding activity compared with the ACE2s from other species. The residue differences and binding properties between the species' variants provide a framework for understanding ACE2-RBD binding and virus tropism
evolution
the binding surface of ACE2 from several important animal species is analyzed to understand the parameters for the ACE2 recognition by the SARSCoV-2 spike protein receptor binding domain (RBD). Recombinant ACE2 from human, hamster, horseshoe bat, cat, ferret, and cow are evaluated for RBD binding. A gradient of binding affinities are seen where human and hamster ACE2 are similarly in the low nanomolar range, followed by cat and cow. Horseshoe bat (Rhinolophus sinicus) and ferret (Mustela putorius) ACE2s have poor binding activity compared with the ACE2s from other species. The residue differences and binding properties between the species' variants provide a framework for understanding ACE2-RBD binding and virus tropism
evolution
the binding surface of ACE2 from several important animal species is analyzed to understand the parameters for the ACE2 recognition by the SARSCoV-2 spike protein receptor binding domain (RBD). Recombinant ACE2 from human, hamster, horseshoe bat, cat, ferret, and cow are evaluated for RBD binding. A gradient of binding affinities are seen where human and hamster ACE2 are similarly in the low nanomolar range, followed by cat and cow. Horseshoe bat (Rhinolophus sinicus) and ferret (Mustela putorius) ACE2s have poor binding activity compared with the ACE2s from other species. The residue differences and binding properties between the species' variants provide a framework for understanding ACE2-RBD binding and virus tropism
evolution
XP_003503283.12
the binding surface of ACE2 from several important animal species is analyzed to understand the parameters for the ACE2 recognition by the SARSCoV-2 spike protein receptor binding domain (RBD). Recombinant ACE2 from human, hamster, horseshoe bat, cat, ferret, and cow are evaluated for RBD binding. A gradient of binding affinities are seen where human and hamster ACE2 are similarly in the low nanomolar range, followed by cat and cow. Horseshoe bat (Rhinolophus sinicus) and ferret (Mustela putorius) ACE2s have poor binding activity compared with the ACE2s from other species. The residue differences and binding properties between the species' variants provide a framework for understanding ACE2-RBD binding and virus tropism
evolution
the binding surface of ACE2 from several important animal species is analyzed to understand the parameters for the ACE2 recognition by the SARSCoV-2 spike protein receptor binding domain (RBD). Recombinant ACE2 from human, hamster, horseshoe bat, cat, ferret, and cow are evaluated for RBD binding. A gradient of binding affinities are seen where human and hamster ACE2 are similarly in the low nanomolar range, followed by cat and cow. Horseshoe bat (Rhinolophus sinicus) and ferret (Mustela putorius) ACE2s have poor binding activity compared with the ACE2s from other species. The residue differences and binding properties between the species' variants provide a framework for understanding ACE2-RBD binding and virus tropism
evolution
XP_024843618.1
the binding surface of ACE2 from several important animal species is analyzed to understand the parameters for the ACE2 recognition by the SARSCoV-2 spike protein receptor binding domain (RBD). Recombinant ACE2 from human, hamster, horseshoe bat, cat, ferret, and cow are evaluated for RBD binding. A gradient of binding affinities are seen where human and hamster ACE2 are similarly in the low nanomolar range, followed by cat and cow. Horseshoe bat (Rhinolophus sinicus) and ferret (Mustela putorius) ACE2s have poor binding activity compared with the ACE2s from other species. The residue differences and binding properties between the species' variants provide a framework for understanding ACE2-RBD binding and virus tropism
malfunction
-
angiotensin II type 1 receptor-mediated reduction of angiotensin-converting enzyme 2 activity in the brain impairs baroreflex function in hypertensive mice
malfunction
-
inhibition of angiotensin-converting enzyme 2 exacerbates cardiac hypertrophy and fibrosis in Ren-2 hypertensive rats
malfunction
-
loss of ACE2 accelerates maladaptive left ventricular remodeling in response to myocardial infarction, MI, overview. ACE2 deficiency leads to increased matrix metalloproteinases 2 and 9 levels with MMP2 activation in the infarct and peri-infarct regions, as well as increased gelatinase activity leading to a disrupted extracellular matrix structure after MI. Loss of ACE2 also leads to increased neutrophilic infiltration in the infarct and peri-infarct regions, resulting in upregulation of inflammatory cytokines, interferon-gamma, interleukin-6, and the chemokine, monocyte chemoattractant protein-1, as well as increased phosphorylation of ERK1/2 and JNK1/2 signaling pathways
malfunction
loss of ACE2 function is implicated in severe acute respiratory syndrome, SARS, pathogenesis
malfunction
-
postural tachycardia syndrome is associated with increased plasma angiotensin-II. ACE2 effects are blunted in low flow postural tachycardia syndrome, POTS, and restored by the ACE2 product angiotensin-(1-7)
malfunction
-
ACE2 activity shows a tendency to decrease in the serum of Alzheimer disease patients compared with normal controls
malfunction
-
ACE2 deficiency increases the severity of H7N9-induced lung injury in a mouse model
malfunction
-
ACE2 knockout mice are more susceptible than the wild-type mice to high-fat diet-induced beta cell dysfunction. The TUNEL-positive area of the pancreatic islets and the expression levels of IL-1beta and iNOS are markedly increased in the ACE2 knockout mice compared with their wild-type littermates. The Mas-silenced MS-1 cells are more sensitive to palmitate-induced dysfunction and apoptosis in vitro
malfunction
-
ACE2 over-expression in the brain decreases Ang-II mediated cardiac hypertrophy and collagen deposition, reduces urinary norepinephrine levels and partially protectes syn-hACE2 transgenic (SA) mice, in which the human ACE2 transgene is selectively targeted to neurons, from sympathetic-mediated cardiac hypertrophy and fibrosis
malfunction
-
genetic inactivation of ACE2 causes severe lung injury in H5N1-challenged mice. Administration of recombinant ACE2 ameliorates avian influenza H5N1 virus-induced lung injury in mice
malfunction
-
mice infected with influenza H7N9 virus downregulate ACE2 protein markedly on day 3 after infection
metabolism
-
ACE2 ia a component of the renin-angiotensin system, RAS
metabolism
the enzyme is involved in the renin-angiotensin system (RAS), which includes angiotensin I, angiotensin (Ang)II, and peptides angiotensin-(1-9) and angiotensin-(1-7) derived by C-terminal cleavage of their particular antecessors by angiotensin converting enzyme (ACE)1 or ACE2, overview
metabolism
induced dysregulation of the enzyme (ACE2) by SARS-CoV-2 plays a key role in COVID-19 severity. Downregulation of ACE2 can be one of the main causes of SARS-CoV-2 symptoms. COVID-19 severity can be changed by reduction in ACE2 products such as Ang (1-7), Ang (1-9), apelin (1-12) and accumulation of substrates such as apelin (1-13) and Ang II. The downregulation of ACE2, accumulated apelin (1-13) can stimulate the pulmonary embolism
physiological function
-
ACE 2 balances the status of the renin-angiotensin system by degrading angiotensin II and generating angiotensin-(1-7). ACE2 induces overexpression of connective tissue growth factor, which is inhibited by blockade of theMas receptor with A779, overview
physiological function
-
ACE2 is a component of the brain renin-angiotensin system participating in the central regulation of blood pressure
physiological function
-
ACE2 is a monocarboxypeptidase that metabolizes Ang II into Ang 1-7, thereby functioning as a negative regulator of the renin-angiotensin system
physiological function
-
ACE2 is a regulator of the renin-angiotensin system
physiological function
-
ACE2 is a regulator of the renin-angiotensin system
physiological function
-
ACE2 is a regulator of the renin-angiotensin system,. Losartan, a specific angiotensin II receptor antagonist, is a well-known antihypertensive drug with a potential role in regulating ACE2
physiological function
-
ACE2 is involved in the angiotensin-II-mediated vasodilation
physiological function
ACE2 reduces the generation of Ang II by catalyzing the conversion of Ang I to angiotensin-(1-9) and facilitating the hydrolysis of Ang II to angiotensin-(1-7)
physiological function
-
angiotensin II is a critical factor for stimulating cardiocyte hypertrophy, fibroblast proliferation and extracellular matrix production in left ventricular remodeling. ACE2 overexpression attenuates left ventricular myocardial fibrosis and improves left ventricular remodeling and systolic function, overview
physiological function
-
angiotensin-converting enzyme 2 is the receptor for severe acute respiratory syndrome coronavirus, SARS-CoV
physiological function
-
role of ACE2 in the regulation of cardiac structure and function, as well as maintenance of systemic blood pressure, overview
physiological function
soluble sACE2 may play a role in modifying peptides in airway surface liquid involved in processes such as inflammation. The membrane-associated form of ACE2 serves as a SARS-CoV receptor in vitro, and shedding is not required for infection to occur
physiological function
-
ACE2 plays a critical role in influenzaA(H7N9) virus-induced acute lung injury
physiological function
-
ACE2 plays an important role in H5N1 virus-induced ALI
physiological function
-
ACE2/Ang-(1-7)/Mas axis has a crucial role in preventing LPS-induced apoptosis and inflammation of pulmonary artery endothelial cells, by inhibiting the JNK/NFkappaB pathways
physiological function
-
ACE2/angiotensin (1-7)/Mas axis protects the function of pancreatic beta cells by improving the function of islet microvascular endothelial cells
physiological function
ACE2 is significantly increased in thapsigargin or palmitic acid-induced cultured hepatocytes. Activation of ACE2 can ameliorate ER stress, accompanied by decreased thapsigargin content, increased intracellular glycogen, and downregulated expression of hepatic lipogenic proteins and enzymes for gluconeogenesis in thapsigargin or palmitic acid-induced hepatocytes
physiological function
ACE2 knockout mice display elevated levels of ER stress, while ACE2 overexpressing db/db mice show reduced ER stress in liver
physiological function
angiotensin (1-7)/ACE2 ameliorate hepatic steatosis, oxidative stress and inflammation in free fatty acid-induced Hep-G2 cells, and Akt inhibitors reduce ACE2-mediated lipid metabolism. The ACE2-mediated Akt activation can be attenuated by blockade of ATP/P2 receptor/Calmodulin (CaM) pathway
physiological function
angiotensin converting enzyme 2 (ACE2) is the receptor of SARS-CoV-2, but only ACE2 of certain species can be utilized by SARS-CoV-2. SARS-CoV-2 tends to utilize ACE2 of various mammals, except murines, and some birds, such as pigeon. This prediction may help to screen the intermediate hosts of SARS-CoV-2. SARS-CoV-2 has a high genetic relationship with a bat coronavirus (BatCoV RaTG13) with a 96% genomic nucleotide sequence identity. The close phylogenetic relationship to Bat RaTG13 provides evidence for a bat origin of SARS-CoV-2. Direct transmission of the virus from bats to humans is unlikely due to the lack of direct contact between bats and humans (in Wuhan, China). There are probably intermediate hosts transmitting SARS-CoV-2 to humans. Combined phylogenetic analysis and critical site marking is used to predict the utilizing capability of ACE2 from different animal species by SARS-CoV-2. It is confirmed that pangolin (Manis javanica), cat (Felis catus), cow (Bos taurus), buffalo (Bubalus bubalis), goat (Capra hircus), sheep (Ovis aries) and pigeon (Columba livia) ACE2 might be utilized by SARS-CoV-2, indicating potential interspecies transmission of the virus from bats to these animals and among these animals
physiological function
angiotensin converting enzyme 2 (ACE2) is the receptor of SARS-CoV-2, but only ACE2 of certain species can be utilized by SARS-CoV-2. SARS-CoV-2 tends to utilize ACE2 of various mammals, except murines, and some birds, such as pigeon. This prediction may help to screen the intermediate hosts of SARS-CoV-2. SARS-CoV-2 has a high genetic relationship with a bat coronavirus (BatCoV RaTG13) with a 96% genomic nucleotide sequence identity. The close phylogenetic relationship to Bat RaTG13 provides evidence for a bat origin of SARS-CoV-2. Direct transmission of the virus from bats to humans is unlikely due to the lack of direct contact between bats and humans (in Wuhan, China). There are probably intermediate hosts transmitting SARS-CoV-2 to humans. Combined phylogenetic analysis and critical site marking is used to predict the utilizing capability of ACE2 from different animal species by SARS-CoV-2. It is confirmed that pangolin (Manis javanica), cat (Felis catus), cow (Bos taurus), buffalo (Bubalus bubalis), goat (Capra hircus), sheep (Ovis aries) and pigeon (Columba livia) ACE2 might be utilized by SARS-CoV-2, indicating potential interspecies transmission of the virus from bats to these animals and among these animals
physiological function
angiotensin converting enzyme 2 (ACE2) is the receptor of SARS-CoV-2, but only ACE2 of certain species can be utilized by SARS-CoV-2. SARS-CoV-2 tends to utilize ACE2 of various mammals, except murines, and some birds, such as pigeon. This prediction may help to screen the intermediate hosts of SARS-CoV-2. SARS-CoV-2 has a high genetic relationship with a bat coronavirus (BatCoV RaTG13) with a 96% genomic nucleotide sequence identity. The close phylogenetic relationship to Bat RaTG13 provides evidence for a bat origin of SARS-CoV-2. Direct transmission of the virus from bats to humans is unlikely due to the lack of direct contact between bats and humans (in Wuhan, China). There are probably intermediate hosts transmitting SARS-CoV-2 to humans. Combined phylogenetic analysis and critical site marking is used to predict the utilizing capability of ACE2 from different animal species by SARS-CoV-2. It is confirmed that pangolin (Manis javanica), cat (Felis catus), cow (Bos taurus), buffalo (Bubalus bubalis), goat (Capra hircus), sheep (Ovis aries) and pigeon (Columba livia) ACE2 might be utilized by SARS-CoV-2, indicating potential interspecies transmission of the virus from bats to these animals and among these animals
physiological function
angiotensin converting enzyme 2 (ACE2) is the receptor of SARS-CoV-2, but only ACE2 of certain species can be utilized by SARS-CoV-2. SARS-CoV-2 tends to utilize ACE2 of various mammals, except murines, and some birds, such as pigeon. This prediction may help to screen the intermediate hosts of SARS-CoV-2. SARS-CoV-2 has a high genetic relationship with a bat coronavirus (BatCoV RaTG13) with a 96% genomic nucleotide sequence identity. The close phylogenetic relationship to Bat RaTG13 provides evidence for a bat origin of SARS-CoV-2. Direct transmission of the virus from bats to humans is unlikely due to the lack of direct contact between bats and humans (in Wuhan, China). There are probably intermediate hosts transmitting SARS-CoV-2 to humans. Combined phylogenetic analysis and critical site marking is used to predict the utilizing capability of ACE2 from different animal species by SARS-CoV-2. It is confirmed that pangolin (Manis javanica), cat (Felis catus), cow (Bos taurus), buffalo (Bubalus bubalis), goat (Capra hircus), sheep (Ovis aries) and pigeon (Columba livia) ACE2 might be utilized by SARS-CoV-2, indicating potential interspecies transmission of the virus from bats to these animals and among these animals
physiological function
XP_017505752.1
angiotensin converting enzyme 2 (ACE2) is the receptor of SARS-CoV-2, but only ACE2 of certain species can be utilized by SARS-CoV-2. SARS-CoV-2 tends to utilize ACE2 of various mammals, except murines, and some birds, such as pigeon. This prediction may help to screen the intermediate hosts of SARS-CoV-2. SARS-CoV-2 has a high genetic relationship with a bat coronavirus (BatCoV RaTG13) with a 96% genomic nucleotide sequence identity. The close phylogenetic relationship to Bat RaTG13 provides evidence for a bat origin of SARS-CoV-2. Direct transmission of the virus from bats to humans is unlikely due to the lack of direct contact between bats and humans (in Wuhan, China). There are probably intermediate hosts transmitting SARS-CoV-2 to humans. Combined phylogenetic analysis and critical site marking is used to predict the utilizing capability of ACE2 from different animal species by SARS-CoV-2. It is confirmed that pangolin (Manis javanica), cat (Felis catus), cow (Bos taurus), buffalo (Bubalus bubalis), goat (Capra hircus), sheep (Ovis aries) and pigeon (Columba livia) ACE2 might be utilized by SARS-CoV-2, indicating potential interspecies transmission of the virus from bats to these animals and among these animals
physiological function
angiotensin converting enzyme 2 (ACE2) is the receptor of SARS-CoV-2, but only ACE2 of certain species can be utilized by SARS-CoV-2. SARS-CoV-2 tends to utilize ACE2 of various mammals, except murines, and some birds, such as pigeon. This prediction may help to screen the intermediate hosts of SARS-CoV-2. SARS-CoV-2 has a high genetic relationship with a bat coronavirus (BatCoV RaTG13) with a 96% genomic nucleotide sequence identity. The close phylogenetic relationship to Bat RaTG13 provides evidence for a bat origin of SARS-CoV-2. Direct transmission of the virus from bats to humans is unlikely due to the lack of direct contact between bats and humans (in Wuhan, China). There are probably intermediate hosts transmitting SARS-CoV-2 to humans. Combined phylogenetic analysis and critical site marking is used to predict the utilizing capability of ACE2 from different animal species by SARS-CoV-2. It is confirmed that pangolin (Manis javanica), cat (Felis catus), cow (Bos taurus), buffalo (Bubalus bubalis), goat (Capra hircus), sheep (Ovis aries) and pigeon (Columba livia) ACE2 might be utilized by SARS-CoV-2, indicating potential interspecies transmission of the virus from bats to these animals and among these animals
physiological function
XP_005228485.1
angiotensin converting enzyme 2 (ACE2) is the receptor of SARS-CoV-2, but only ACE2 of certain species can be utilized by SARS-CoV-2. SARS-CoV-2 tends to utilize ACE2 of various mammals, except murines, and some birds, such as pigeon. This prediction may help to screen the intermediate hosts of SARS-CoV-2. SARS-CoV-2 has a high genetic relationship with a bat coronavirus (BatCoV RaTG13) with a 96% genomic nucleotide sequence identity. The close phylogenetic relationship to Bat RaTG13 provides evidence for a bat origin of SARS-CoV-2. Direct transmission of the virus from bats to humans is unlikely due to the lack of direct contact between bats and humans (in Wuhan, China). There are probably intermediate hosts transmitting SARS-CoV-2 to humans. Combined phylogenetic analysis and critical site marking is used to predict the utilizing capability of ACE2 from different animal species by SARS-CoV-2. It is confirmed that pangolin (Manis javanica), cat (Felis catus), cow (Bos taurus), buffalo (Bubalus bubalis), goat (Capra hircus), sheep (Ovis aries) and pigeon (Columba livia) ACE2 might be utilized by SARS-CoV-2, indicating potential interspecies transmission of the virus from bats to these animals and among these animals
physiological function
XP_006041602.1
angiotensin converting enzyme 2 (ACE2) is the receptor of SARS-CoV-2, but only ACE2 of certain species can be utilized by SARS-CoV-2. SARS-CoV-2 tends to utilize ACE2 of various mammals, except murines, and some birds, such as pigeon. This prediction may help to screen the intermediate hosts of SARS-CoV-2. SARS-CoV-2 has a high genetic relationship with a bat coronavirus (BatCoV RaTG13) with a 96% genomic nucleotide sequence identity. The close phylogenetic relationship to Bat RaTG13 provides evidence for a bat origin of SARS-CoV-2. Direct transmission of the virus from bats to humans is unlikely due to the lack of direct contact between bats and humans (in Wuhan, China). There are probably intermediate hosts transmitting SARS-CoV-2 to humans. Combined phylogenetic analysis and critical site marking is used to predict the utilizing capability of ACE2 from different animal species by SARS-CoV-2. It is confirmed that pangolin (Manis javanica), cat (Felis catus), cow (Bos taurus), buffalo (Bubalus bubalis), goat (Capra hircus), sheep (Ovis aries) and pigeon (Columba livia) ACE2 might be utilized by SARS-CoV-2, indicating potential interspecies transmission of the virus from bats to these animals and among these animals
physiological function
angiotensin converting enzyme 2 (ACE2) is the receptor of SARS-CoV-2, but only ACE2 of certain species can be utilized by SARS-CoV-2. SARS-CoV-2 tends to utilize ACE2 of various mammals, except murines, and some birds, such as pigeon. This prediction may help to screen the intermediate hosts of SARS-CoV-2. SARS-CoV-2 has a high genetic relationship with a bat coronavirus (BatCoV RaTG13) with a 96% genomic nucleotide sequence identity. The close phylogenetic relationship to Bat RaTG13 provides evidence for a bat origin of SARS-CoV-2. Direct transmission of the virus from bats to humans is unlikely due to the lack of direct contact between bats and humans (in Wuhan, China). There are probably intermediate hosts transmitting SARS-CoV-2 to humans. Combined phylogenetic analysis and critical site marking is used to predict the utilizing capability of ACE2 from different animal species by SARS-CoV-2. It is confirmed that pangolin (Manis javanica), cat (Felis catus), cow (Bos taurus), buffalo (Bubalus bubalis), goat (Capra hircus), sheep (Ovis aries) and pigeon (Columba livia) ACE2 might be utilized by SARS-CoV-2, indicating potential interspecies transmission of the virus from bats to these animals and among these animals
physiological function
XP_011961657.1
angiotensin converting enzyme 2 (ACE2) is the receptor of SARS-CoV-2, but only ACE2 of certain species can be utilized by SARS-CoV-2. SARS-CoV-2 tends to utilize ACE2 of various mammals, except murines, and some birds, such as pigeon. This prediction may help to screen the intermediate hosts of SARS-CoV-2. SARS-CoV-2 has a high genetic relationship with a bat coronavirus (BatCoV RaTG13) with a 96% genomic nucleotide sequence identity. The close phylogenetic relationship to Bat RaTG13 provides evidence for a bat origin of SARS-CoV-2. Direct transmission of the virus from bats to humans is unlikely due to the lack of direct contact between bats and humans (in Wuhan, China). There are probably intermediate hosts transmitting SARS-CoV-2 to humans. Combined phylogenetic analysis and critical site marking is used to predict the utilizing capability of ACE2 from different animal species by SARS-CoV-2. It is confirmed that pangolin (Manis javanica), cat (Felis catus), cow (Bos taurus), buffalo (Bubalus bubalis), goat (Capra hircus), sheep (Ovis aries) and pigeon (Columba livia) ACE2 might be utilized by SARS-CoV-2, indicating potential interspecies transmission of the virus from bats to these animals and among these animals
physiological function
angiotensin converting enzyme 2 (ACE2) is the receptor of SARS-CoV-2, but only ACE2 of certain species can be utilized by SARS-CoV-2. SARS-CoV-2 tends to utilize ACE2 of various mammals, except murines, and some birds, such as pigeon. This prediction may help to screen the intermediate hosts of SARS-CoV-2. SARS-CoV-2 has a high genetic relationship with a bat coronavirus (BatCoV RaTG13) with a 96% genomic nucleotide sequence identity. The close phylogenetic relationship to Bat RaTG13 provides evidence for a bat origin of SARS-CoV-2. Direct transmission of the virus from bats to humans is unlikely due to the lack of direct contact between bats and humans (in Wuhan, China). There are probably intermediate hosts transmitting SARS-CoV-2 to humans. Combined phylogenetic analysis and critical site marking is used to predict the utilizing capability of ACE2 from different animal species by SARS-CoV-2. It is confirmed that pangolin (Manis javanica), cat (Felis catus), cow (Bos taurus), buffalo (Bubalus bubalis), goat (Capra hircus), sheep (Ovis aries) and pigeon (Columba livia) ACE2 might be utilized by SARS-CoV-2, indicating potential interspecies transmission of the virus from bats to these animals and among these animals
physiological function
-
at pH values below 6, formation of angiotensin (1-7) in ACE2 knockout mice is similar to that in wild-type mice. The prolyl carboxypeptidase-prolyl endopeptidase inhibitor Z-prolyl-prolinal reduces angiotensin (1-7) formation in ACE2 knockout mice. ACE2 metabolizes angiotensin II in the kidney at neutral and basic pH, while prolyl carboxypeptidase catalyzes the same reaction at acidic pH
physiological function
-
atrial ACE2 overexpression attenuates rapid atrial pacing-induced increase in activated extracellular signal-regulated kinases and mitogen-activated protein kinases levels, and decrease in MAPK phosphatase 1 level, resulting in attenuation of atrial fibrosis collagen protein markers and transforming growth factor-beta1. ACE2 overexpression also modulates the tachypacing-induced up-regulation of connexin 40, down-regulation of connexin 43 and Kv4.2, and significantly decreases the inducibility and duration of atrial fibrillation
physiological function
deletion of ACE2 aggravates liver steatosis, which is correlated with the increased expression of hepatic lipogenic genes and the decreased expression of fatty acid oxidation-related genes in the liver of ACE2 knockout mice. Oxidative stress and inflammation are also aggravated in ACE2 knockout mice. Overexpression of ACE2 improves fatty liver in db/db mice, and the mRNA levels of fatty acid oxidation-related genes are up-regulated
physiological function
exogenous ACE2 attenuates bleomycin-induced lung fibrosis by reversing the reduction of local ACE2 and by suppressing the elevation of angiotensinogen. ACE2 decreases the apoptosis index and leukocyte common antigen levels and ameliorates the dynamic change in surfactant-associated protein SP-A level. Reductions of TGF-beta1 and alpha-SMA are also found in ACE2-treated mice
physiological function
in ACE2 knockout mice, hypotensive action of peptides pyr-apelin 13 and apelin 17 is potentiated, with a corresponding greater elevation in plasma apelin levels. Pyr-apelin 13 and apelin 17 rescue contractile function in a myocardial ischemia-reperfusion model, while ACE2 cleavage products, pyr-apelin 12 and 16, are devoid of these cardioprotective effects. Pharmacological inhibition of ACE2 potentiates the vasodepressor action of apelin peptides. Loss of C-terminal phenylalanine attenuates apelin peptide physiological effects
physiological function
in vitro, AngII significantly increases the NOX4 level and ROS production in lung fibroblasts, which stimulates cell migration and alpha-collagen I synthesis through the RhoA/Rock pathway. These effects are attenuated by N-acetylcysteine, diphenylene iodonium, and NOX4 RNA interference. Angiotensin (1-7) and lentivirus-mediated ACE2 suppress angiotensin II-induced migration and alpha-collagen I synthesis by inhibiting the NOX4-derived ROS-mediated RhoA/Rock pathway. In vivo, constant infusion with angiotensin (1-7) or intratracheal instillation with lentivirus-mediated ACE2 shift the renin-angiotensin system balance toward the ACE2/angiotensin (1-7)/Mas axis, alleviate bleomycin-induced lung fibrosis, and inhibit the RhoA/Rock pathway by reducing NOX4-derived ROS
physiological function
lipopolysaccharide-induced lung injury and inflammatory response are significantly prevented by ACE2 overexpression in lung and deteriorated by Ace2 shRNA. Mas receptor antagonist A779 or ACE2 inhibitor MLN-4760 pretreatment abolish the protective effects of ACE2. Overexpression of ACE2 significantly reduces the angiotensin II/angiotensin -(1-7) ratio in broncho-alveolar lavage fluid and up-regulated Mas mRNA expression in lung. The blockade of ACE2 on lipopolysaccharide-induced phosphorylation of ERK1/2, p38 and p50/p65 is also abolished by A779. Only the ERK1/2 inhibitor significantly attenuates lung injury in ACE2 overexpressing rats pretreated with A779
physiological function
recombinant human ACE2 can cleave pyr-apelin 13 and apelin 17 efficiently, and apelin peptides are degraded slower in ACE2-deficient plasma
physiological function
-
regulation of NF-kappaB and ACE2 by specific Ang II type 1 receptor AT1 and Ang II type 2 receptor AT2 antagonists in a nongenetic model of type 2 diabetic nephropathy. The AT1 receptor and AT2 receptor antagonists lead to the repression and activation of the NF-kappaB signalling pathway, respectively. The blockade of AT2 receptor leads to an increase in ACE2 expression
physiological function
the angiotensin-converting enzyme-2 is the receptor for the SARS-coronavirus (SARS-CoV), the human respiratory coronavirus NL63 and Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). Comparative genetic analysis of SARS-CoV-2 coronavirus receptor ACE2 in different populations. Systematic analysis of coding-region variants in ACE2 and the expression quantitative trait loci (eQTL) variants, which may affect the expression of ACE2 using the Genotype Tissue Expression database to compare the genomic characteristics of ACE2 among different populations. No direct evidence is identified genetically supporting the existence of coronavirus S-protein binding-resistant ACE2 mutants in different populations
physiological function
the angiotensin-converting enzyme-2 is the receptor for the SARS-coronavirus (SARS-CoV). The spike protein of SARS-CoV attaches the virus to its cellular receptor, angiotensin-converting enzyme 2. A defined receptor binding domain on the spike protein mediates this interaction
physiological function
the enzyme is involved in the renin-angiotensin system (RAS), which includes angiotensin I, angiotensin (Ang)II, and peptides angiotensin-(1-9) and angiotensin-(1-7) derived by C-terminal cleavage of their particular antecessors by angiotensin converting enzyme (ACE)1 or ACE2, overview
physiological function
the receptor binding domain (RBD) of spike glycoprotein is responsible for entry of coronaviruses (SARS-CoV-2 and SARS-CoV) into host cells. The RBDs from the two viruses share 72% identity in amino acid sequences, and molecular simulation reveals highly similar ternary structures. Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has a distinct loop with flexible glycyl residues replacing rigid prolyl residues in SARS-CoV. Molecular modeling reveals that SARS-CoV-2 RBD has a stronger interaction with angiotensin converting enzyme 2 (ACE2). A unique phenylalanine F486 in the flexible loop likely plays a major role because its penetration into a deep hydrophobic pocket in ACE2. ACE2 is widely expressed with conserved primary structures throughout the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Structural analysis suggests that ACE2 from these animals can potentially bind RBD of SARS-CoV-2, making them all possible natural hosts for the virus
physiological function
the receptor binding domain (RBD) of spike glycoprotein is responsible for entry of coronaviruses (SARS-CoV-2 and SARS-CoV) into host cells. The RBDs from the two viruses share 72% identity in amino acid sequences, and molecular simulation reveals highly similar ternary structures. Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has a distinct loop with flexible glycyl residues replacing rigid prolyl residues in SARS-CoV. Molecular modeling reveals that SARS-CoV-2 RBD has a stronger interaction with angiotensin converting enzyme 2 (ACE2). A unique phenylalanine F486 in the flexible loop likely plays a major role because its penetration into a deep hydrophobic pocket in ACE2. ACE2 is widely expressed with conserved primary structures throughout the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Structural analysis suggests that ACE2 from these animals can potentially bind RBD of SARS-CoV-2, making them all possible natural hosts for the virus
physiological function
the receptor binding domain (RBD) of spike glycoprotein is responsible for entry of coronaviruses (SARS-CoV-2 and SARS-CoV) into host cells. The RBDs from the two viruses share 72% identity in amino acid sequences, and molecular simulation reveals highly similar ternary structures. Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has a distinct loop with flexible glycyl residues replacing rigid prolyl residues in SARS-CoV. Molecular modeling reveals that SARS-CoV-2 RBD has a stronger interaction with angiotensin converting enzyme 2 (ACE2). A unique phenylalanine F486 in the flexible loop likely plays a major role because its penetration into a deep hydrophobic pocket in ACE2. ACE2 is widely expressed with conserved primary structures throughout the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Structural analysis suggests that ACE2 from these animals can potentially bind RBD of SARS-CoV-2, making them all possible natural hosts for the virus
physiological function
the receptor binding domain (RBD) of spike glycoprotein is responsible for entry of coronaviruses (SARS-CoV-2 and SARS-CoV) into host cells. The RBDs from the two viruses share 72% identity in amino acid sequences, and molecular simulation reveals highly similar ternary structures. Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has a distinct loop with flexible glycyl residues replacing rigid prolyl residues in SARS-CoV. Molecular modeling reveals that SARS-CoV-2 RBD has a stronger interaction with angiotensin converting enzyme 2 (ACE2). A unique phenylalanine F486 in the flexible loop likely plays a major role because its penetration into a deep hydrophobic pocket in ACE2. ACE2 is widely expressed with conserved primary structures throughout the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Structural analysis suggests that ACE2 from these animals can potentially bind RBD of SARS-CoV-2, making them all possible natural hosts for the virus
physiological function
XP_029140508.1
the receptor binding domain (RBD) of spike glycoprotein is responsible for entry of coronaviruses (SARS-CoV-2 and SARS-CoV) into host cells. The RBDs from the two viruses share 72% identity in amino acid sequences, and molecular simulation reveals highly similar ternary structures. Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has a distinct loop with flexible glycyl residues replacing rigid prolyl residues in SARS-CoV. Molecular modeling reveals that SARS-CoV-2 RBD has a stronger interaction with angiotensin converting enzyme 2 (ACE2). A unique phenylalanine F486 in the flexible loop likely plays a major role because its penetration into a deep hydrophobic pocket in ACE2. ACE2 is widely expressed with conserved primary structures throughout the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Structural analysis suggests that ACE2 from these animals can potentially bind RBD of SARS-CoV-2, making them all possible natural hosts for the virus
physiological function
XP_018104311.1
the receptor binding domain (RBD) of spike glycoprotein is responsible for entry of coronaviruses (SARS-CoV-2 and SARS-CoV) into host cells. The RBDs from the two viruses share 72% identity in amino acid sequences, and molecular simulation reveals highly similar ternary structures. Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has a distinct loop with flexible glycyl residues replacing rigid prolyl residues in SARS-CoV. Molecular modeling reveals that SARS-CoV-2 RBD has a stronger interaction with angiotensin converting enzyme 2 (ACE2). A unique phenylalanine F486 in the flexible loop likely plays a major role because its penetration into a deep hydrophobic pocket in ACE2. ACE2 is widely expressed with conserved primary structures throughout the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Structural analysis suggests that ACE2 from these animals can potentially bind RBD of SARS-CoV-2, making them all possible natural hosts for the virus
physiological function
XP_007889845.1
the receptor binding domain (RBD) of spike glycoprotein is responsible for entry of coronaviruses (SARS-CoV-2 and SARS-CoV) into host cells. The RBDs from the two viruses share 72% identity in amino acid sequences, and molecular simulation reveals highly similar ternary structures. Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has a distinct loop with flexible glycyl residues replacing rigid prolyl residues in SARS-CoV. Molecular modeling reveals that SARS-CoV-2 RBD has a stronger interaction with angiotensin converting enzyme 2 (ACE2). A unique phenylalanine F486 in the flexible loop likely plays a major role because its penetration into a deep hydrophobic pocket in ACE2. ACE2 is widely expressed with conserved primary structures throughout the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Structural analysis suggests that ACE2 from these animals can potentially bind RBD of SARS-CoV-2, making them all possible natural hosts for the virus
physiological function
the receptor critical for SARS-CoV entry into host cells is the angiotensin-converting enzyme 2 (ACE2). The S1 domain of the spike protein of SARS-CoV attaches the virus to its cellular receptor ACE2 on the host cells. Functionally, there are two forms of ACE2. The full-length ACE2 contains a structural transmembrane domain, which anchors its extracellular domain to the plasma membrane. The extracellular domain is a receptor for the spike (S) protein of SARS-CoV, and for the SARS-CoV-2. The soluble form of ACE2 lacks the membrane anchor and circulates in small amounts in the blood. It is proposed that this soluble form may act as a competitive interceptor of SARS-CoV and other coronaviruses by preventing binding of the viral particle to the surface-bound, full-length ACE2
physiological function
the SARS-CoV-2 spike protein directly binds with the host cell surface ACE2 receptor facilitating virus entry and replication
physiological function
ACE2 functions as a carboxypeptidase that can cleave several endogenous substrates, including angiotensin II, thus regulating blood pressure and vascular tone
physiological function
ACE2 is the dominant host receptor of SARS-CoV-2
physiological function
ACE2 is the reported entry receptor for SARS-CoV-2
physiological function
angiotensin-converting enzyme 2 (ACE2) is the cellular receptor for severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), the etiological agent of the COVID-19 disease
physiological function
angiotensin-converting enzyme 2 (ACE2) is the entry receptor for severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2), the cause of Coronavirus Disease-2019 (COVID-19) in humans. ACE2 mediates the interaction between host cells and SARS-CoV-2 spike (S) protein. ACE2 is also an important homeostatic function regulating renin-angiotensin system (RAS), which is pivotal for both the cardiovascular and immune systems. ACE2 is the key link between SARS-CoV-2 infection, cardiovascular diseases (CVDs) and immune response
physiological function
human angiotensin-converting enzyme 2 acts as the host cell receptor for SARS-CoV-2 and the other members of the Coronaviridae family SARS-CoV-1 and HCoV-NL63
physiological function
key role of the enzyme (ACE2) as a functional receptor for SARSCoV-2
physiological function
SARS-CoV-2 binds to the angiotensin converting enzyme 2 (ACE2) receptor of the host cells through the viral surface spike glycoprotein (S-protein). ACE2 is expressed in the oral mucosa and can therefore constitute an essential route for entry of SARS-CoV-2 into hosts through the tongue and lung epithelial cells
physiological function
SARS-CoV-2 binds to the angiotensin I converting enzyme 2 (ACE2) to enable its entry into host cells and establish infection
physiological function
SARS-CoV-2 binds to the angiotensin I converting enzyme 2 (ACE2) to enable its entry into host cells and establish infection
physiological function
SARS-CoV-2 binds to the angiotensin I converting enzyme 2 (ACE2) to enable its entry into host cells and establish infection
physiological function
XP_003503283.12
SARS-CoV-2 binds to the angiotensin I converting enzyme 2 (ACE2) to enable its entry into host cells and establish infection
physiological function
SARS-CoV-2 binds to the angiotensin I converting enzyme 2 (ACE2) to enable its entry into host cells and establish infection
physiological function
XP_024843618.1
SARS-CoV-2 binds to the angiotensin I converting enzyme 2 (ACE2) to enable its entry into host cells and establish infection
physiological function
SARS-CoV-2 infection occurs by the recognition and binding of the spike glycoprotein (S-protein) receptor binding domain (RBD) on the virus envelope to the human cellular receptor angiotensin-converting enzyme 2 (ACE2). Seven mutational sites (K417, L455, A475, G476, E484, Q498 and V503) on SARS-CoV-2 weaken the RBD-ACE2 binding
physiological function
SARS-CoV-2 spike (S) protein plays a crucial role in the receptor recognition and cell membrane fusion process by interacting with the human angiotensin-converting enzyme 2 (hACE2) receptor. Acid exchanges S477G and S477N strengthen the binding of the SARS-COV-2 spike with the hACE2 receptor
physiological function
SARS-CoV-2 spike protein uses the angiotensin converting enzyme 2 (ACE2) as a cellular receptor to initiate infection
physiological function
SARS-CoV-2 utilizes angiotensin-converting enzyme 2 (ACE2) as the receptor required for viral entry
physiological function
SARS-CoV-2 virus anchors the host cells by the interaction of the S protein with the human ACE2 receptor, triggering the pre/postfusion conformational change responsible for the virus entry into the host cell
physiological function
SARS-CoV-2 virus and its homolog SARS-CoV penetrate human cells by binding of viral spike protein and human angiotensin converting enzyme II (ACE2). The binding affinity of SARS-CoV-2 to human ACE2 receptor is temperature-dependent
physiological function
severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) (the virus causing COVID-19) is known to use the receptor-binding domain (RBD) at viral surface spike (S) protein to interact with the angiotensin-converting enzyme 2 (ACE2) receptor expressed on many human cell types. The RBD-ACE2 interaction is a crucial step to mediate the host cell entry of SARS-CoV-2.
physiological function
severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is the cause of coronavirus disease, it binds to angiotensin-converting enzyme 2 (ACE2) to enter into human cells. The expression level of ACE2 potentially determines the susceptibility and severity of COVID-19
physiological function
the ability of SARS-CoV-2 virions to enter and infect human cells is dependent upon a number of ACE2 properties: the binding affinity for the SARS-CoV-2 spike, the amount of ACE2 that migrates through the endoplasmic reticulum (ER) to reach the cell surface, and the turnover rate of ACE2 at the cell membrane. Mutations in ACE2 residues distal to the SARS-CoV-2 spike-binding interface may alter ACE2 properties relevant to SARS-CoV-2 recognition
physiological function
the SARS-CoV S glycoprotein has a high affinity to the ACE2 receptor, and participates in viral entry into host cells and spreads among people
physiological function
ACE2 binds the prototype SARS-CoV-2 receptor-binding domain with a dissociation constant (KD) of 24.63 nM. Receptor-binding domains from SARS-CoV-2 variants alpha, beta, and gamma demonstrate enhanced affinities, ranging from 1.78- to 4.56fold increase. Variant omicron, along with delta receptor-binding domain, shows no significant change in binding affinities when compared with those of the prototype domain
physiological function
interaction between SARS-CoV-2 and ACE2. Most mouse ACE2 receptors (including rats and mice) show higher binding free energies than the human ACE2, indicating weaker binding to the SARS-CoV-2 spike. The mole ACE2 has a similar binding free energy to the human ACE2 due to their high sequence identity at the binding interface to the SARS-CoV-2 spike protein
physiological function
interaction between SARS-CoV-2 and ACE2. The binding free energy of SARS-CoV-2 spike protein to the civet ACE2 is -5.11 kcal/mol, i.e. a lower binding affinity than human ACE2. Compared with the human ACE2 molecule, the civet ACE2 has a substitution from phenylalanine to serine at position 40 in the first helix at the N-terminal lobe region. This mutation breaks the pi-pi stacking interactions between the N-terminal helices, resulting in the side-chain rearrangement and loose helix-packing structures
physiological function
interaction between SARS-CoV-2 and ACE2. The binding free energy of SARS-CoV-2 spike protein to the human ACE2 is -60.64 kcal/mol on average. ACE2 residues Tyr41 and Tyr83 contribute most to the spike binding affinity for both SARS-CoV-2 and SARS-CoV. Residues Met82, Gly354, and Asp355 also have substantial contributions to the binding free energy between spike protein and ACE2
physiological function
-
interaction between SARS-CoV-2 and ACE2. The binding free energy of SARS-CoV-2 spike protein to the pangolin ACE2 is -54.78 kcal/mol, i.e. a lower binding affinity than human ACE2. Compared with the human ACE2 molecule, the pangolin ACE2 has a substitution from Aso to Glu at position 38. This transformation has a significant impact on the hydrogen bond network in the left recognition region
physiological function
interaction with Sars-CoV2 spike protein mutants. The N501Y receptor-binding domain mutant binds to ACE2 with higher affinity due to improved pi-pi stacking and pi-cation interactions. The higher binding affinity of the E484K mutant is caused by the formation of additional hydrogen bond and salt-bridge interactions with ACE2. Both the mutants bind to the B38 neutralizing antibody with reduced affinity due to the loss of several hydrogen-bonding interactions
physiological function
the SARS-CoV-2 spike protein binds to ACE2. The spike protein samples at least four different conformational states, of which three are defined via different ACE2-bound states
physiological function
yeast display-based comparison of the binding of SARS-CoV-2 spike protein to ACE2, the decreasing binding order is human > cat = pig > dog
physiological function
yeast display-based comparison of the binding of SARS-CoV-2 spike protein to ACE2, the decreasing binding order is human > cat = pig > dog
physiological function
yeast display-based comparison of the binding of SARS-CoV-2 spike protein to ACE2, the decreasing binding order is human > cat = pig > dog
physiological function
E2RR65
yeast display-based comparison of the binding of SARS-CoV-2 spike protein to ACE2, the decreasing binding order is human > cat = pig > dog
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
L79I
E2RR65
mutation increases binding of SARS-CoV-2 spike protein
Q42L
E2RR65
mutation increases binding of SARS-CoV-2 spike protein
L79I
mutation increases binding of SARS-CoV-2 spike protein
Q42L
mutation increases binding of SARS-CoV-2 spike protein
analysis
receptor binding domain-ACE2 binding assay based on time-resolved FRET, which reliably monitors the interaction in a physiologically relevant and cellular context. The modular assay can monitor the impact of different cellular components, such as heparan sulfate, lipids, and membrane proteins on the receptor binding domain-ACE2 interaction and it can be extended to the full-length spike protein. The assay is high throughput compatible and can detect small-molecule competitive and allosteric modulators of the receptor binding domain-ACE2 interaction
D206G
deleterious missense variant
D355N
variant exhibits lower binding to SARS-CoV-2 S protein
D38V
variant exhibits lower binding to SARS-CoV-2 S protein
D509Yr
variant exhibits lower binding to SARS-CoV-2 S protein
E23K
the variant in the binding region increases disease susceptibility towards SARS-CoV-2
E329G
variant shows a strong binding affinity with SARS-CoV-2 spike protein variants with very strong E329G-V483A, E329G-G476S, strong E329G-A419S, E329G-A348T and moderate E329G-S383C,E329G-F486L interaction
E37K
non-synonymous single nucleotide polymorphism
E484K
mutation forms high-affinity complexes (~40% more than wild-type)
E484K/N501Y
variant possesses both enhanced affinity and antibody resistance
F72V
variant exhibits lower binding to SARS-CoV-2 S protein
G326E
variant exhibits lower binding to SARS-CoV-2 S protein
G352V
variant exhibits lower binding to SARS-CoV-2 S protein
G726R
non-synonymous single nucleotide polymorphism
H345A
-
no activity with (7-methoxycoumarin-4-yl)acetyl-APK-2,4-dinitrophenyl
H345L
-
no activity with (7-methoxycoumarin-4-yl)acetyl-APK-2,4-dinitrophenyl
H34R
variant exhibits lower binding to SARS-CoV-2 S protein
H505A
-
1.5% of wild-type activity with (7-methoxycoumarin-4-yl)acetyl-APK-2,4-dinitrophenyl as substrate
H505L
-
no activity with (7-methoxycoumarin-4-yl)acetyl-APK-2,4-dinitrophenyl
I21V
the variant in the binding region increases disease susceptibility towards SARS-CoV-2
I468V
deleterious missense variant
K31R
variant exhibits lower binding to SARS-CoV-2 S protein
K341R
deleterious missense variant
K417T/E484K/N501Y
variant possesses both enhanced affinity and antibody resistance
K481Q
angiotensin I cleavage activity is 21% of wild-type activity, angiotensin II cleavage activity is 71.8% of wild-type activity
K68E
variant exhibits lower binding to SARS-CoV-2 S protein
L584A
the point mutation in the ACE2 ectodomain markedly attenuates shedding. The resultant ACE2-L584A mutant trafficks to the cell membrane and facilitates SARS-CoV entry into target cells
L595V
non-synonymous single nucleotide polymorphism
L731F
deleterious missense variant
L79I
mutation increases binding of SARS-CoV-2 spike protein
M62V
variant exhibits lower binding to SARS-CoV-2 S protein
N33I
variant exhibits lower binding to SARS-CoV-2 S protein
N501Y
mutation forms high-affinity complexes (~40% more than wild-type)
N51S
variant exhibits lower binding to SARS-CoV-2 S protein
N580A
the mutation in the ectodomain has no effect on sACE2 release
N64K
the variant in the binding region increases disease susceptibility towards SARS-CoV-2
P263S
non-synonymous single nucleotide polymorphism
P284S
non-synonymous single nucleotide polymorphism
P583A
the mutation in the ectodomain has no effect on sACE2 release
Q102P
the variant in the binding region increases disease susceptibility towards SARS-CoV-2
Q35K
variant exhibits lower binding to SARS-CoV-2 S protein
Q37K
variant exhibits lower binding to SARS-CoV-2 S protein
Q388L
variant exhibits lower binding to SARS-CoV-2 S protein
Q42L
mutation increases binding of SARS-CoV-2 spike protein
R169QK481QR514Q
angiotensin I cleavage activity is 53.2% of wild-type activity, angiotensin II cleavage activity is 203.4% of wild-type activity
R219C
deleterious missense variant
R219H
deleterious missense variant
R273K
-
no activity with (7-methoxycoumarin-4-yl)acetyl-APK-2,4-dinitrophenyl
R273Q
-
no activity with (7-methoxycoumarin-4-yl)acetyl-APK-2,4-dinitrophenyl
R582A
the mutation in the ectodomain has no effect on sACE2 release
R697G
deleterious missense variant
R768W
non-synonymous single nucleotide polymorphism
S477N
mutation forms high-affinity complexes (~40% more than wild-type)
S477N/E484K
variant possesses both enhanced affinity and antibody resistance
S547C
deleterious missense variant
S563L
non-synonymous single nucleotide polymorphism
S692P
deleterious missense variant
T27A
the variant in the binding region increases disease susceptibility towards SARS-CoV-2
T92I
the variant in the binding region increases disease susceptibility towards SARS-CoV-2
V581A
the mutation in the ectodomain has no effect on sACE2 release
V604A
the mutation in the ectodomain has no effect on sACE2 release
W271A
angiotensin I cleavage activity is 5.3% of wild-type activity, angiotensin II cleavage activity is 0.9% of wild-type activity. Lacks any significant chloride sensitivity with the substrate angiotensin I
W459C
non-synonymous single nucleotide polymorphism
Y252N
non-synonymous single nucleotide polymorphism
Y50F
variant exhibits lower binding to SARS-CoV-2 S protein
Y83H
variant exhibits lower binding to SARS-CoV-2 S protein
Q42L
mutation increases binding of SARS-CoV-2 spike protein
G211R
deleterious missense variant
G211R
missense variant, mutation affect protein structure and stability
H378R
deleterious missense variant
H378R
the variant in the binding region increases disease susceptibility towards SARS-CoV-2
H378R
non-synonymous single nucleotide polymorphism
K26R
missense variant, mutation affect protein structure and stability
K26R
the variant in the binding region increases disease susceptibility towards SARS-CoV-2
N720D
missense variant, mutation affect protein structure and stability
N720D
non-synonymous single nucleotide polymorphism
R169Q
-
as active as wild-type enzyme with (7-methoxycoumarin-4-yl)acetyl-APK-2,4-dinitrophenyl as substrate
R169Q
angiotensin I cleavage activity is 5.2% of wild-type activity, angiotensin II cleavage activity is 1.1% of wild-type activity. The mutant enzyme does not show any activity with angiotensin I in the absence of chloride ions
R514Q
-
about 10% of wild-type activity with (7-methoxycoumarin-4-yl)acetyl-APK-2,4-dinitrophenyl as substrate
R514Q
angiotensin I cleavage activity is 52% of wild-type activity, angiotensin II cleavage activity is 179.3% of wild-type activity, enhancement of angiotensin II cleavage is a result of a 2.5-fold increase in Vmax compared with the wild-type
S19P
deleterious missense variant
S19P
the variant in the binding region increases disease susceptibility towards SARS-CoV-2
additional information
-
M2-mutant CHO cells, mutated in tumor necrosis factor alpha-converting enzyme, TACE, show reduced shedding of the ectodomain of ACE2 and increased release of the larger soluble enzyme form, compared to the smaller one, overview. Tandem mutation in the juxtamembrane region also causes a decreaee in the small soluble enzyme form
additional information
construction of a soluble truncated mutant enzyme lacking the transmembrane and cytosolic domains
additional information
construction of a soluble truncated mutant enzyme lacking the transmembrane and cytosolic domains
additional information
construction of cytoplasmic tail deletion mutants by introduction of a stop codon at position amino acid 763. Construction of chimeric proteins containing portions of human ACE2 and portions of human CD4 or human beta-defensin-2, both showing loss of domain shedding
additional information
-
construction of cytoplasmic tail deletion mutants by introduction of a stop codon at position amino acid 763. Construction of chimeric proteins containing portions of human ACE2 and portions of human CD4 or human beta-defensin-2, both showing loss of domain shedding
additional information
-
construction of several transgenic linages with differential virological and immunological outcome of severe acute respiratory syndrome coronavirus infection in susceptible and resistant transgenic mice expressing human ACE2, overview. Transgenic lineages AC70 and AC22, representing those susceptible and resistant to the lethal SARS-CoV infection, respectively, are both permissive to SARS-CoV infection, causing elevated secretion of many inflammatory mediators within the lungs and brains, viral infection appears to be more intense in AC70 than in AC22 mice, especially in the brain, differential SARS-CoV-induced morbidity and mortality between AC70 and AC22 mice, overview
additional information
-
overexpression of ACE 2 might have a protective effect by inhibiting cell growth and vascular endothelial growth factor a production in vitro
additional information
-
generation of triple-transgenic-model mice with brain ACE2 overexpression on a chronically hypertensive, AngII-increased background. The transgenic mice show dramatically decreased baseline spontaneous baroreflex sensitivity and brain ACE2 activity compared with nontransgenic mice, whereas peripheral ACE2 activity/expression remains unaffected
additional information
-
ACE2 overexpression leads to markedly increased myocyte volume, assessed in primary rabbit myocytes
additional information
-
overexpression of ACE2 favorably affects the pathological process of left ventricular remodeling after myocardial infarction by inhibiting ACE activity, reducing AngII levels and upregulating Ang(1-7) expression
additional information
-
overexpression of ACE2, by usage of a recombinant adeno-associated virus 6 delivery system, in myocardium of stroke-prone spontaneously hypertensive rats mediates onset of experimental severe cardiac fibrosis
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
diagnostics
ACE2 levels is a putative early biomarker of SARS-CoV-2 infection severity
drug development
a super-potent tetramerized ACE2 protein displays enhanced neutralization of SARS-CoV-2 virus infection
analysis
-
mass spectrometric assay for angiotensin-converting enzyme 2 using angiotensin II as substrate will have applications in drug screening, antagonist development, and clinical investigations
analysis
-
mass spectrometric assay for angiotensin-converting enzyme 2 using angiotensin II as substrate will have applications in drug screening, antagonist development, and clinical investigations
analysis
easy-to-use method for determining ACE2 activity in brain tissue and cerebrospinal fluid, based on a quenched fluorescent substrate and presence and absence of inhibitor DX600. The method can be adapted for other tissues, plasma, cell extracts, and cell culture supernatants
analysis
method for measurement of ACE2 activity in biological fluids, using hydrolysis of an intramolecularly quenched fluorogenic ACE2 substrate, in the absence or presence of the ACE2 inhibitors MLN-4760 or DX600. ACE2 detection ranges from 1.56 to 50 ng/ml. MLN-4760 potently inhibits the activity of both human and mouse ACE2, DX600 (linear form) only effectively blocks human ACE2 activity in this assay. In biological samples of human and mouse urine, cell culture medium from mouse proximal tubular cells, and mouse plasma, the mean intra- and interassay coefficients of variation of the assay range from 1.43 to 4.39 %, and from 7.01 to 13.17 %, respectively
analysis
method for measurement of ACE2 activity in biological fluids, using hydrolysis of an intramolecularly quenched fluorogenic ACE2 substrate, in the absence or presence of the ACE2 inhibitors MLN-4760 or DX600. ACE2 detection ranges from 1.56 to 50 ng/ml. MLN-4760 potently inhibits the activity of both human and mouse ACE2, DX600 (linear form) only effectively blocks human ACE2 activity in this assay. In biological samples of human and mouse urine, cell culture medium from mouse proximal tubular cells, and mouse plasma, the mean intra- and interassay coefficients of variation of the assay range from 1.43 to 4.39%, and from 7.01 to 13.17%, respectively
analysis
ACE2-based biosensor designed to detect both SARS-CoV-2 S1 mutations and neutralizing antibodies. In binding mode, the biosensor works by detecting binding of the spike protein to an immobilized ACE2 receptor and is able to detect S1 proteins of the alpha (500 pg/ml) and beta variants (10 ng/ml), as well as wild-type S1 (10 ng/ml), of SARSCoV-2 and it distinguishes wild-type SARS-CoV-2 S1 from the S1 alpha and beta variants via color differences. A modification to the protocol enables the ACE2-based biosensor to operate in blocking mode to detect neutralizing antibodies in serum samples from COVID-19 patients
analysis
analysis of the interaction between ACE2 and SARS-CoV-2 spike protein using a surface plasmon resonance-based assay that reduces the heterogeneity introduced from multivalent binding interactions to enable the determination of the kinetic rate constants for multivalent binding interactions. Controlling the sensor surface heterogeneity enables the deconvolution of the avidity-induced affinity enhancement for the SARS-CoV-2 spike protein and ACE2 interaction
analysis
application of CEBIT, i.e. Condensate-aided Enrichment of Biomolecular Interactions in Test tubes for high-throughput screening of drugs to inhibit the interaction between the receptor-binding domain of SARS-CoV-2 spike protein and its obligate receptor ACE2
medicine
potential important target in cardio-renal disease
medicine
-
ACE2 protects against acute lung injury in several animal models of acute respiratory distress syndrome. Increasing ACE2 activity might be a novel approach for the treatment of acute lung failure in several diseases
medicine
-
angiotensin-converting enzyme 2 is a target for gene therapy for hypertension disorders
medicine
-
chronic treatment with the AT1R antagonist almesartan induces a fivefold increase in ACE2 mRNA in the aorta which leads to a significant increase in aortic angiotensin(1-7) protein expression. These effects are associated with significant decreases in aortic medial thickness and may represent an important protective mechanism in the prevention of cardiovascular events in hypertensive subjects
medicine
-
identification of ACE2 as a receptor for SARS-CoV will contribute to the development of antivirals and vaccines
medicine
-
recombinant ACE2 can protect mice from severe acute lung injury
medicine
-
ACE-2 protects against lung fibrogenesis by limiting the local accumulation of the profibrotic peptide angiotensin II
medicine
-
ACE-2 protects against lung fibrogenesis by limiting the local accumulation of the profibrotic peptide angiotensin II
medicine
-
ACE-2 protects against lung fibrogenesis by limiting the local accumulation of the profibrotic peptide angiotensin II
medicine
-
ACE2 is a functional receptor for the causative agent of severe acute repiratory syndrome, the SARS coronavirus, ACE2 also plays a role in the development of liver fibrosis and subsequent cirrhosis
medicine
-
ACE2 is a key factor for protection from ARDS/acute lung injury and it functions as a critical SARS receptor in vivo, recombinant ACE2 protein might not only be a treatment to block spreading of SARS but also to protect SARS patients from developing lung failure
medicine
-
ACE2 may be a target for therapeutic interventions that aim to reduce albuminuria and glomerular injury
medicine
-
ACE2 protects murine lungs from acute respiratory distress syndrome
medicine
ACE2 activators are a reliable approach which could lead to the development of a novel class of antihypertensive and cardioprotective drugs
medicine
ACE2 offers a new target for the treatment of hypertension and other cardiovascular diseases
medicine
administration of ACE2 activators may be a valid strategy for antihypertensive therapy
medicine
differential regulation of ACE2 activity during the progression of atherosclerosis suggest that this novel molecule of the reninangiotensin system may play a role in the pathogenesis of atherosclerosis
medicine
enhancing ACE2 action may serve to provide additional therapeutic benefits patients with cardiovascular and diabetic kidney disease. Increased ACE2 activity by the use of human recombinant ACE2 and/or a small molecule activator(xanthenone) of ACE2 may represent potential new therapies for lung, cardiovascular and kidney diseases by providing dual beneficial effects by antagonizing angiotensin II action while generating angiotensin-(1-7)
medicine
reduction of ACE2 expression by RNA interference promotes the proliferation of cultured pancreatic cancer cells. ACE2 may have clinical potential as a novel molecular target for the treatment of pancreatic ductal adenocarcinoma
medicine
soluble ACE2 activity is a biomarker in heart failure, and in hypertension
medicine
angiotensin converting enzyme 2 (ACE2) is the receptor of SARS-CoV-2, but only ACE2 of certain species can be utilized by SARS-CoV-2. SARS-CoV-2 tends to utilize ACE2 of various mammals, except murines, and some birds, such as pigeon. This prediction may help to screen the intermediate hosts of SARS-CoV-2. SARS-CoV-2 has a high genetic relationship with a bat coronavirus (BatCoV RaTG13) with a 96% genomic nucleotide sequence identity. The close phylogenetic relationship to Bat RaTG13 provides evidence for a bat origin of SARS-CoV-2. Direct transmission of the virus from bats to humans is unlikely due to the lack of direct contact between bats and humans (in Wuhan, China). There are probably intermediate hosts transmitting SARS-CoV-2 to humans. Combined phylogenetic analysis and critical site marking is used to predict the utilizing capability of ACE2 from different animal species by SARS-CoV-2. It is confirmed that pangolin (Manis javanica), cat (Felis catus), cow (Bos taurus), buffalo (Bubalus bubalis), goat (Capra hircus), sheep (Ovis aries) and pigeon (Columba livia) ACE2 might be utilized by SARS-CoV-2, indicating potential interspecies transmission of the virus from bats to these animals and among these animals
medicine
angiotensin converting enzyme 2 (ACE2) is the receptor of SARS-CoV-2, but only ACE2 of certain species can be utilized by SARS-CoV-2. SARS-CoV-2 tends to utilize ACE2 of various mammals, except murines, and some birds, such as pigeon. This prediction may help to screen the intermediate hosts of SARS-CoV-2. SARS-CoV-2 has a high genetic relationship with a bat coronavirus (BatCoV RaTG13) with a 96% genomic nucleotide sequence identity. The close phylogenetic relationship to Bat RaTG13 provides evidence for a bat origin of SARS-CoV-2. Direct transmission of the virus from bats to humans is unlikely due to the lack of direct contact between bats and humans (in Wuhan, China). There are probably intermediate hosts transmitting SARS-CoV-2 to humans. Combined phylogenetic analysis and critical site marking is used to predict the utilizing capability of ACE2 from different animal species by SARS-CoV-2. It is confirmed that pangolin (Manis javanica), cat (Felis catus), cow (Bos taurus), buffalo (Bubalus bubalis), goat (Capra hircus), sheep (Ovis aries) and pigeon (Columba livia) ACE2 might be utilized by SARS-CoV-2, indicating potential interspecies transmission of the virus from bats to these animals and among these animals
medicine
angiotensin converting enzyme 2 (ACE2) is the receptor of SARS-CoV-2, but only ACE2 of certain species can be utilized by SARS-CoV-2. SARS-CoV-2 tends to utilize ACE2 of various mammals, except murines, and some birds, such as pigeon. This prediction may help to screen the intermediate hosts of SARS-CoV-2. SARS-CoV-2 has a high genetic relationship with a bat coronavirus (BatCoV RaTG13) with a 96% genomic nucleotide sequence identity. The close phylogenetic relationship to Bat RaTG13 provides evidence for a bat origin of SARS-CoV-2. Direct transmission of the virus from bats to humans is unlikely due to the lack of direct contact between bats and humans (in Wuhan, China). There are probably intermediate hosts transmitting SARS-CoV-2 to humans. Combined phylogenetic analysis and critical site marking is used to predict the utilizing capability of ACE2 from different animal species by SARS-CoV-2. It is confirmed that pangolin (Manis javanica), cat (Felis catus), cow (Bos taurus), buffalo (Bubalus bubalis), goat (Capra hircus), sheep (Ovis aries) and pigeon (Columba livia) ACE2 might be utilized by SARS-CoV-2, indicating potential interspecies transmission of the virus from bats to these animals and among these animals
medicine
angiotensin converting enzyme 2 (ACE2) is the receptor of SARS-CoV-2, but only ACE2 of certain species can be utilized by SARS-CoV-2. SARS-CoV-2 tends to utilize ACE2 of various mammals, except murines, and some birds, such as pigeon. This prediction may help to screen the intermediate hosts of SARS-CoV-2. SARS-CoV-2 has a high genetic relationship with a bat coronavirus (BatCoV RaTG13) with a 96% genomic nucleotide sequence identity. The close phylogenetic relationship to Bat RaTG13 provides evidence for a bat origin of SARS-CoV-2. Direct transmission of the virus from bats to humans is unlikely due to the lack of direct contact between bats and humans (in Wuhan, China). There are probably intermediate hosts transmitting SARS-CoV-2 to humans. Combined phylogenetic analysis and critical site marking is used to predict the utilizing capability of ACE2 from different animal species by SARS-CoV-2. It is confirmed that pangolin (Manis javanica), cat (Felis catus), cow (Bos taurus), buffalo (Bubalus bubalis), goat (Capra hircus), sheep (Ovis aries) and pigeon (Columba livia) ACE2 might be utilized by SARS-CoV-2, indicating potential interspecies transmission of the virus from bats to these animals and among these animals
medicine
angiotensin converting enzyme 2 (ACE2) is the receptor of SARS-CoV-2, but only ACE2 of certain species can be utilized by SARS-CoV-2. SARS-CoV-2 tends to utilize ACE2 of various mammals, except murines, and some birds, such as pigeon. This prediction may help to screen the intermediate hosts of SARS-CoV-2. SARS-CoV-2 has a high genetic relationship with a bat coronavirus (BatCoV RaTG13) with a 96% genomic nucleotide sequence identity. The close phylogenetic relationship to Bat RaTG13 provides evidence for a bat origin of SARS-CoV-2. Direct transmission of the virus from bats to humans is unlikely due to the lack of direct contact between bats and humans (in Wuhan, China). There are probably intermediate hosts transmitting SARS-CoV-2 to humans. Combined phylogenetic analysis and critical site marking is used to predict the utilizing capability of ACE2 from different animal species by SARS-CoV-2. It is confirmed that pangolin (Manis javanica), cat (Felis catus), cow (Bos taurus), buffalo (Bubalus bubalis), goat (Capra hircus), sheep (Ovis aries) and pigeon (Columba livia) ACE2 might be utilized by SARS-CoV-2, indicating potential interspecies transmission of the virus from bats to these animals and among these animals
medicine
XP_017505752.1
angiotensin converting enzyme 2 (ACE2) is the receptor of SARS-CoV-2, but only ACE2 of certain species can be utilized by SARS-CoV-2. SARS-CoV-2 tends to utilize ACE2 of various mammals, except murines, and some birds, such as pigeon. This prediction may help to screen the intermediate hosts of SARS-CoV-2. SARS-CoV-2 has a high genetic relationship with a bat coronavirus (BatCoV RaTG13) with a 96% genomic nucleotide sequence identity. The close phylogenetic relationship to Bat RaTG13 provides evidence for a bat origin of SARS-CoV-2. Direct transmission of the virus from bats to humans is unlikely due to the lack of direct contact between bats and humans (in Wuhan, China). There are probably intermediate hosts transmitting SARS-CoV-2 to humans. Combined phylogenetic analysis and critical site marking is used to predict the utilizing capability of ACE2 from different animal species by SARS-CoV-2. It is confirmed that pangolin (Manis javanica), cat (Felis catus), cow (Bos taurus), buffalo (Bubalus bubalis), goat (Capra hircus), sheep (Ovis aries) and pigeon (Columba livia) ACE2 might be utilized by SARS-CoV-2, indicating potential interspecies transmission of the virus from bats to these animals and among these animals
medicine
angiotensin converting enzyme 2 (ACE2) is the receptor of SARS-CoV-2, but only ACE2 of certain species can be utilized by SARS-CoV-2. SARS-CoV-2 tends to utilize ACE2 of various mammals, except murines, and some birds, such as pigeon. This prediction may help to screen the intermediate hosts of SARS-CoV-2. SARS-CoV-2 has a high genetic relationship with a bat coronavirus (BatCoV RaTG13) with a 96% genomic nucleotide sequence identity. The close phylogenetic relationship to Bat RaTG13 provides evidence for a bat origin of SARS-CoV-2. Direct transmission of the virus from bats to humans is unlikely due to the lack of direct contact between bats and humans (in Wuhan, China). There are probably intermediate hosts transmitting SARS-CoV-2 to humans. Combined phylogenetic analysis and critical site marking is used to predict the utilizing capability of ACE2 from different animal species by SARS-CoV-2. It is confirmed that pangolin (Manis javanica), cat (Felis catus), cow (Bos taurus), buffalo (Bubalus bubalis), goat (Capra hircus), sheep (Ovis aries) and pigeon (Columba livia) ACE2 might be utilized by SARS-CoV-2, indicating potential interspecies transmission of the virus from bats to these animals and among these animals
medicine
XP_005228485.1
angiotensin converting enzyme 2 (ACE2) is the receptor of SARS-CoV-2, but only ACE2 of certain species can be utilized by SARS-CoV-2. SARS-CoV-2 tends to utilize ACE2 of various mammals, except murines, and some birds, such as pigeon. This prediction may help to screen the intermediate hosts of SARS-CoV-2. SARS-CoV-2 has a high genetic relationship with a bat coronavirus (BatCoV RaTG13) with a 96% genomic nucleotide sequence identity. The close phylogenetic relationship to Bat RaTG13 provides evidence for a bat origin of SARS-CoV-2. Direct transmission of the virus from bats to humans is unlikely due to the lack of direct contact between bats and humans (in Wuhan, China). There are probably intermediate hosts transmitting SARS-CoV-2 to humans. Combined phylogenetic analysis and critical site marking is used to predict the utilizing capability of ACE2 from different animal species by SARS-CoV-2. It is confirmed that pangolin (Manis javanica), cat (Felis catus), cow (Bos taurus), buffalo (Bubalus bubalis), goat (Capra hircus), sheep (Ovis aries) and pigeon (Columba livia) ACE2 might be utilized by SARS-CoV-2, indicating potential interspecies transmission of the virus from bats to these animals and among these animals
medicine
XP_006041602.1
angiotensin converting enzyme 2 (ACE2) is the receptor of SARS-CoV-2, but only ACE2 of certain species can be utilized by SARS-CoV-2. SARS-CoV-2 tends to utilize ACE2 of various mammals, except murines, and some birds, such as pigeon. This prediction may help to screen the intermediate hosts of SARS-CoV-2. SARS-CoV-2 has a high genetic relationship with a bat coronavirus (BatCoV RaTG13) with a 96% genomic nucleotide sequence identity. The close phylogenetic relationship to Bat RaTG13 provides evidence for a bat origin of SARS-CoV-2. Direct transmission of the virus from bats to humans is unlikely due to the lack of direct contact between bats and humans (in Wuhan, China). There are probably intermediate hosts transmitting SARS-CoV-2 to humans. Combined phylogenetic analysis and critical site marking is used to predict the utilizing capability of ACE2 from different animal species by SARS-CoV-2. It is confirmed that pangolin (Manis javanica), cat (Felis catus), cow (Bos taurus), buffalo (Bubalus bubalis), goat (Capra hircus), sheep (Ovis aries) and pigeon (Columba livia) ACE2 might be utilized by SARS-CoV-2, indicating potential interspecies transmission of the virus from bats to these animals and among these animals
medicine
angiotensin converting enzyme 2 (ACE2) is the receptor of SARS-CoV-2, but only ACE2 of certain species can be utilized by SARS-CoV-2. SARS-CoV-2 tends to utilize ACE2 of various mammals, except murines, and some birds, such as pigeon. This prediction may help to screen the intermediate hosts of SARS-CoV-2. SARS-CoV-2 has a high genetic relationship with a bat coronavirus (BatCoV RaTG13) with a 96% genomic nucleotide sequence identity. The close phylogenetic relationship to Bat RaTG13 provides evidence for a bat origin of SARS-CoV-2. Direct transmission of the virus from bats to humans is unlikely due to the lack of direct contact between bats and humans (in Wuhan, China). There are probably intermediate hosts transmitting SARS-CoV-2 to humans. Combined phylogenetic analysis and critical site marking is used to predict the utilizing capability of ACE2 from different animal species by SARS-CoV-2. It is confirmed that pangolin (Manis javanica), cat (Felis catus), cow (Bos taurus), buffalo (Bubalus bubalis), goat (Capra hircus), sheep (Ovis aries) and pigeon (Columba livia) ACE2 might be utilized by SARS-CoV-2, indicating potential interspecies transmission of the virus from bats to these animals and among these animals
medicine
XP_011961657.1
angiotensin converting enzyme 2 (ACE2) is the receptor of SARS-CoV-2, but only ACE2 of certain species can be utilized by SARS-CoV-2. SARS-CoV-2 tends to utilize ACE2 of various mammals, except murines, and some birds, such as pigeon. This prediction may help to screen the intermediate hosts of SARS-CoV-2. SARS-CoV-2 has a high genetic relationship with a bat coronavirus (BatCoV RaTG13) with a 96% genomic nucleotide sequence identity. The close phylogenetic relationship to Bat RaTG13 provides evidence for a bat origin of SARS-CoV-2. Direct transmission of the virus from bats to humans is unlikely due to the lack of direct contact between bats and humans (in Wuhan, China). There are probably intermediate hosts transmitting SARS-CoV-2 to humans. Combined phylogenetic analysis and critical site marking is used to predict the utilizing capability of ACE2 from different animal species by SARS-CoV-2. It is confirmed that pangolin (Manis javanica), cat (Felis catus), cow (Bos taurus), buffalo (Bubalus bubalis), goat (Capra hircus), sheep (Ovis aries) and pigeon (Columba livia) ACE2 might be utilized by SARS-CoV-2, indicating potential interspecies transmission of the virus from bats to these animals and among these animals
medicine
angiotensin converting enzyme 2 (ACE2) is the receptor of SARS-CoV-2, but only ACE2 of certain species can be utilized by SARS-CoV-2. SARS-CoV-2 tends to utilize ACE2 of various mammals, except murines, and some birds, such as pigeon. This prediction may help to screen the intermediate hosts of SARS-CoV-2. SARS-CoV-2 has a high genetic relationship with a bat coronavirus (BatCoV RaTG13) with a 96% genomic nucleotide sequence identity. The close phylogenetic relationship to Bat RaTG13 provides evidence for a bat origin of SARS-CoV-2. Direct transmission of the virus from bats to humans is unlikely due to the lack of direct contact between bats and humans (in Wuhan, China). There are probably intermediate hosts transmitting SARS-CoV-2 to humans. Combined phylogenetic analysis and critical site marking is used to predict the utilizing capability of ACE2 from different animal species by SARS-CoV-2. It is confirmed that pangolin (Manis javanica), cat (Felis catus), cow (Bos taurus), buffalo (Bubalus bubalis), goat (Capra hircus), sheep (Ovis aries) and pigeon (Columba livia) ACE2 might be utilized by SARS-CoV-2, indicating potential interspecies transmission of the virus from bats to these animals and among these animals
medicine
angiotensin-converting enzyme 2 (ACE2) fused to the Fc portion of immunoglobulin neutralizes SARS-CoV-2 in vitro. Provision of soluble recombinant human ACE2 protein can be beneficial as a novel biologic therapeutic to combat or limit infection progression caused by coronaviruses that utilize ACE2 as a receptor. If given in its soluble form as an appropriate recombinant ACE2 protein, a new tool may be at hand to combat the spread of coronavirus in susceptible individuals by limiting coronavirus attachment to the cell membranes, cell entry, and replication
medicine
antibodies and small molecular inhibitors that can block the interaction of the enzyme (ACE2) with the receptor binding domain can to combat the virus SARS-CoV-2
medicine
-
plasma ACE2 activity independently increases the hazard of adverse long-term cardiovascular outcomes in patients with obstructive coronary artery disease. Above-median plasma ACE2 activity is associated with major adverse cardiovascular events and heart failure hospitalisation
medicine
-
plasma kininase II or ACE levels are significantly increased by 18% in untreated diabetics when compared with healthy volunteers. After treatment for 6 weeks with metformin hydrochloride 500 mg twice daily there is a significant decrease of 20% in their ACE levels. Plasma prekallikrein levels are raised significantly by 28% in diabetic patients in contrast with the control subjects and the levels are reduced by 44% after treatment with metformin hydrochloride. NO levels are significantly decreased in plasma by 56% and in urine by 62% in untreated diabetic patients as compared with the healthy subjects. In treated diabetic patients' samples, there is an increase of 50% in plasma and 37% in urine samples compared to untreated patients
medicine
potential therapeutic approach to ACE2-mediated COVID-19. Treatment with a soluble form of ACE2 may exert dual functions, slow viral entry into cells and hence viral spread and protect the lung from injury
medicine
-
regulation of NF-kappaB and ACE2 by specific Ang II type 1 receptor AT1 and Ang II type 2 receptor AT2 antagonists in a nongenetic model of type 2 diabetic nephropathy. The AT1 receptor and AT2 receptor antagonists lead to the repression and activation of the NF-kappaB signalling pathway, respectively. The blockade of AT2 receptor leads to an increase in ACE2 expression
medicine
investigation of reverse genetic-rescued SARS-CoV-2 viruses in K18-hACE2 mice. The genetic-rescued SARS-CoV-2 viruses will facilitate basic understanding of SARS-CoV-2 and the preclinical development of COVID-19 therapeutics
medicine
17-beta-estradiol may reduce SARS-CoV-2 infection of lung epithelial cells
medicine
ACE2-overexpressing A549 cell-derived microparticles are a potential therapeutic agent against SARS-CoV-2 infection. Intranasally administered microparticles dexterously navigate the anatomical and biological features of the lungs to enter the alveoli and are taken up by alveolar macrophages. Then, ACE2-overexpressing A549 cell-derived microparticles increase the endosomal pH but decrease the lysosomal pH in alveolar macrophages, thus escorting bound SARS-CoV-2 from phago-endosomes to lysosomes for degradation. In addition, ACE2-overexpressing A549 cell-derived microparticles also inhibit the proinflammatory phenotype of alveolar macrophages, leading to increased treatment efficacy in a SARS-CoV-2-infected mouse model without side effects
medicine
among 226000 SARSCoV-2 sequences, 1573 missense mutations are found in the spike gene, and 226 of them were within the receptor-binding domain region that directly interacts with human ACE2. Modeling shows that most of the 74 missense mutations in the receptor-binding domain region of the interaction interface have little impact on spike binding to ACE2, whereas several within the spike receptor-binding domain increase the binding affinity toward human ACE2 thus making the virus likely more contagious
medicine
among 226000 SARSCoV-2 sequences, 1573 missense mutations are found in the spike gene, and 226 of them were within the receptor-binding domain region that directly interacts with human ACE2. Modeling shows that most of the 74 missense mutations in the receptor-binding domain region of the interaction interface have little impact on spike binding to ACE2, whereas several within the spike receptor-binding domain increase the binding affinity toward human ACE2 thus making the virus likely more contagious
medicine
among 226000 SARSCoV-2 sequences, 1573 missense mutations are found in the spike gene, and 226 of them were within the receptor-binding domain region that directly interacts with human ACE2. Modeling shows that most of the 74 missense mutations in the receptor-binding domain region of the interaction interface have little impact on spike binding to ACE2, whereas several within the spike receptor-binding domain increase the binding affinity toward human ACE2 thus making the virus likely more contagious
medicine
-
among 226000 SARSCoV-2 sequences, 1573 missense mutations are found in the spike gene, and 226 of them were within the receptor-binding domain region that directly interacts with human ACE2. Modeling shows that most of the 74 missense mutations in the receptor-binding domain region of the interaction interface have little impact on spike binding to ACE2, whereas several within the spike receptor-binding domain increase the binding affinity toward human ACE2 thus making the virus likely more contagious
medicine
analysis of variations in SARS-CoV-2 spike protein and hACE2 receptor protein and their interaction in the infection scale. Interactions of hACE2 variants with SARS-CoV-2 variants are very strong for G726R-G476S, R768W-V367F, Y252N-V483A, Y252N-V367F, G726R-V367F, N720D-V367F and N720DF486L, and weak for P263S-S383C, RBD-H378R, G726R-A348T
medicine
binding of SARS-CoV-2 spike protein, variant omicron B.1.1.529, to ACE2 is inhibited by caffeic acid hexoside (-6.4 kcal/mol, RMSD 2.382 A) and phloretin (-6.3 kcal/mol, RMSD 0.061 A) from Sargassum wightii, which interact with crucial residues Asn417, Ser496, Tyr501, and His505 of the spike protein. 5alpha-Cholestan-3beta-ol, 2-methylene- (-6.0 kcal/mol, RMSD 3.074 A) from Corallina officinalis shows inhibitory effect against the omicron receptor-binding domain mutated residues Leu452 and Ala484
medicine
circulating extracellular vesicles that express ACE2 isolated from human plasma or cells neutralize SARS-CoV-2 infection by competing with cellular ACE2. Compared to vesicle-free recombinant human ACE2, ACE2 from extracellular vesicles shows a 135fold higher potency in blocking the binding of the viral spike protein receptor-binding domain, and a 60- to 80fold higher efficacy in preventing infections by both pseudotyped and authentic SARS-CoV-2. ACE2 from extracellular vesicles protects human ACE2 transgenic mice from SARS-CoV-2-induced lung injury and mortality. ACE2 from extracellular vesicles inhibits the infection of SARS-CoV-2 variants alpha, beta, and delta with equal or higher potency than for the wild-type strain
medicine
coexpression of intermediate filament protein vimentin with ACE2 increases SARS-CoV-2 entry in HEK-293 cells, and shRNA-mediated knockdown of vimentin significantly reduces SARS-CoV-2 infection of human endothelial cells. Incubation of A-549 cells expressing ACE2 with purified vimentin increases pseudotyped SARS-CoV-2 spike protein entry. The S-protein receptor-binding domain is sufficient for spike protein interaction with vimentin. Extracellular vimentin binds to SARS-CoV-2 spike protein and facilitates SARS-CoV-2 infection
medicine
compounds benzyl (6aS,9aS)-10-benzyl-4-[benzyl(methyl)amino]-8-(cyclopropanecarbonyl)-6a,7,8,9,9a,10-hexahydrocyclopenta[b]pyrimido[4,5-e][1,4]diazepine-6(5H)-carboxylate, benzyl (6aS,9aS)-4-[benzyl(methyl)amino]-8-(cyclopropanecarbonyl)-10-[(4-methylphenyl)methyl]-6a,7,8,9,9a,10-hexahydrocyclopenta[b]pyrimido[4,5-e][1,4]diazepine-6(5H)-carboxylate and benzyl (6aS,9aS)-4-[benzyl(methyl)amino]-10-[(4-chlorophenyl)methyl]-8-(cyclopropanecarbonyl)-6a,7,8,9,9a,10-hexahydrocyclopenta[b]pyrimido[4,5-e][1,4]diazepine-6(5H)-carboxylate inhibit the interactions between SARS-CoV-2 spike receptor-binding domain and ACE2 by modulating ACE2 without impairing its enzymatic activity necessary for normal physiological functions. The compounds suppress viral infection in cultured cells by inhibiting the entry of ancestral and variant SARS-CoV-2
medicine
expression of ACE2 increases during aging in human lungs. ACE2 expression increases upon telomere shortening or dysfunction in cultured mammalian cells. This increase is controlled at the transcriptional level, and ACE2 promoter activity is DNA damage response-dependent. Both pharmacological global DNA damage response inhibition of ATM kinase activity and selective telomeric DNA damage response inhibition by the use of antisense oligonucleotides prevent ACE2 upregulation following telomere damage
medicine
expression of ACE2 increases during aging in lungs. ACE2 expression increases upon telomere shortening or dysfunction in mice. This increase is controlled at the transcriptional level, and ACE2 promoter activity is DNA damage response-dependent. Both pharmacological global DNA damage response inhibition of ATM kinase activity and selective telomeric DNA damage response inhibition by the use of antisense oligonucleotides prevent ACE2 upregulation following telomere damage
medicine
expression of both ACE2 and TMPRSS2 genes is necessary to support SARS-CoV-2 infection and replication in DF1 cells and a nonpermissive sub-lineage of MDCK cells. Titers of SARS-CoV-2 in these cell lines are comparable to those observed in control Vero cells. Permissive replication of SARS-CoV-2 is not found in pig or horse. Cells expressing genes from either bat species tested demonstrate temporal replication of SARS-CoV-2 that peaks early and is not sustained
medicine
in lung tissues collected from mice that were sub-chronically exposed to air or 0.8 ppm ozone for three weeks, the ACE2 transcripts are significantly elevated in the parenchyma, but not in the extrapulmonary airways and alveolar macrophages. A significant proportion of additional known SARS-CoV-2 host susceptibility genes are upregulated in alveolar macrophages and parenchyma from ozone-exposed mice
medicine
inhibition of SARS-CoV-2 spike protein binding to ACE2 by a higher-affinity variant of the B38 monoclonal antibody, containing mutantion F27Q in the heavy chain (F27Q), which can bind to the rececptor-binding domain more tightly, and by Ty1 alpaca nanobody, i.e.a 38 amino acid peptide inhibitor taking components from Ty1. The peptide exhibits improved affinity for the rececptor-binding by up to 100fold, and like B38 mutant, it can outclass the binding affinity of ACE2 with the rececptor-binding domain
medicine
interaction of ACE2 and SARS-CoV-2 Omicron spike protein. The mutations in the Omicron variant at residues 493, 496, 498, and 501 restore ACE2 binding efficiency that would be lost as a result of other mutations such as K417N
medicine
interaction with Sars-CoV2 spike protein mutants. The N501Y receptor-binding domainmutant binds to ACE2 with higher affinity due to improved pi-pi stacking and pi-cation interactions. The higher binding affinity of the E484K mutant is caused by the formation of additional hydrogen bond and salt-bridge interactions with ACE2. Both the mutants bind to the B38 neutralizing antibody with reduced affinity due to the loss of several hydrogen-bonding interactions
medicine
patients younger than 70 years old, patients with eosinophilic asthma, and inhaled corticosteroids non-users are associated with higher levels of blood serum ACE2. Blood eosinophils and fractionated exhaled nitric oxide levels are positively correlated with serum ACE2
medicine
SARS-CoV and SARS-CoV-2 spike proteins have similar charge distributions and electrostatic features when binding with ACE2. The complex structures of ACE2 and the spike proteins of SARS-CoV/SARS-CoV-2 are stable at pH values ranging from 7.5 to 9. SARS-CoV-2 forms 19 pairs of hydrogen bonds with high occupancy to ACE2, compared to 16 pairs between SARS-CoV and ACE2. SARS-CoV viruses prefer sticking to the same hydrogen bond pairs, while SARS-CoV-2 tends to have a larger range of selections on hydrogen bonds acceptors
medicine
SARS-CoV-2 spike protein binds ACE2. A dimeric ACE2 peptide mimetic designed through side chain cross-linking and covalent dimerization has a binding affinity of 16 nM for the SARS-CoV-2 spike receptor-binding domain, and effectively inhibits the SARS-CoV-2 pseudovirus in Huh7-hACE2 cells with an IC50 of 190 nM and neutralizes the authentic SARS-CoV-2 in Caco2 cells with an IC50 of 2.4 microM
medicine
-
SARS-CoV-2 spike protein binds to ACE2. Bromelain-derived peptide DYGAVNEVK interacts with several critical receptor-binding domain binding residues responsible for the adhesion of the receptor-binding domain to hACE2. Molecular dynamics simulations reveal stable interactions between DYGAVNEVK and receptor-binding domain variants, as well as free binding energy calculations. The bromelain-derived peptide inhibition at the binding site of the receptor-binding domain and ACE2 is competitive
medicine
SARS-CoV-2 spike protein-ACE2 binding is strongly blocked by ritonavir and naloxegol. The two ligands stabilize both the entire receptor-binding domain and the binding site key residues, ensuring efficient blocking of the key receptor-binding domain residues which are involved in receptor-binding domain-ACE2 interaction. Naloxegol and ritonavir are the most potently blocking ligands, followed by far by sofosbuvir and remdesivir
medicine
values of 438.1 and 219 microM ibuprofen as well as 204.7 microM flurbiprofen significantly reduce viral load in Caco-2 cells, while etoricoxib and paracetamol have no consistent, significant effect on viral load
medicine
values of 438.1 and 219 microM ibuprofen as well as 204.7 microM flurbiprofen significantly reduce viral load in Caco-2 cells, while etoricoxib and paracetamol have no consistent, significant effect on viral load
pharmacology
design and synthesis of first potent and selective enzyme inhibitors may be useful as pharmacological tools to help understanding the biological relevance and potantial role of the enzyme in human disease
pharmacology
-
ACE 2 is a potential therapeutic target in the treatment of heart failure
pharmacology
-
ACE2 might be a target for treatment of non-small cell lung cancer
pharmacology
conserved residues at the interface of the spike protein from three strains of coronaviruses NL63, SARS-CoV, and SARS-CoV are identified, which might act as a recognition site for ACE2 receptor. The conserved interaction sites can help in effective targeting of the ACE2 binding site by therapeutics in SARS-CoV as well as SARS-CoV-2 strain
pharmacology
identification of compounds that bind to either the angiotensin converting enzyme 2 (ACE2) and/or the SARS-CoV-2 spike protein receptor binding domain (SARS-CoV-2 spike protein RBD). All 22 identified compounds provide scaffolds for the development of new chemical entities for the treatment of COVID-19
pharmacology
the binding of eighteen candidate drugs with ACE2 enzyme and [SARSCoV-2/ACE2] complex is examined by using docking analysis. The docking ranking shows that some of these ligands might have the ability to inhibit SARS-CoV-2. The study shows that Ramipril, Delapril and Lisinopril could bind with ACE2 receptor and [SARSCoV-2/ACE2] complex better than chloroquine and hydroxychloroquine