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Information on EC 3.4.17.23 - angiotensin-converting enzyme 2 and Organism(s) Mus musculus and UniProt Accession Q8R0I0
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3.4.17.23 angiotensin-converting enzyme 2Specify your search results
Word Map
- 3.4.17.23
- sars-cov-2
- covid-19
- coronavirus
- spike
- pandemic
-
renin-angiotensin
- cardiovascular
- hypertension
- ras
- pulmonary
-
outbreak
-
receptor-binding
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distress
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storm
-
comorbidities
- tmprss2
-
blocker
- endothelial
- viruses
- cardiac
-
december
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wuhan
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renin-angiotensin-aldosterone
-
angiotensin-1-7
- renin
- drug development
- pharmacology
- analysis
- medicine
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aceis
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declared
- diagnostics
-
covid
- 3clpro
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angii
- anosmia
- pseudovirus
- mers-cov
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covid-19-related
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counter-regulatory
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contagious
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anti-sars-cov-2
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disease-2019
- favipiravir
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convalescent
- corona
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covid-19-associated
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lockdown
- camostat
-
pseudotyped
- cough
- hydroxychloroquine
- s-proteins
- furin
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
angiotensin-converting enzyme 2, tmprss2, ace-2, angiotensin converting enzyme 2, hace2, angiotensin converting enzyme-2, sace2, ace 2, angiotensin converting enzyme ii, angiotensin-converting enzyme type 2, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ACE2
-
-
angiotensin converting enzyme 2
-
-
CAS REGISTRY NUMBER
COMMENTARY
328404-18-8
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(7-methoxycoumarin-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-YVADAPK-(2,4-dinitrophenyl)-OH + H2O
(7-methoxycoumarin-4-yl)-acetyl-YVADAP + N6-(2,4-dinitrophenyl)-L-Lys
-
-
-
-
?
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 II + H2O
angiotensin-(1-7) + 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
-
-
?
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 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 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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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 II + H2O
angiotensin(1-7) + L-Phe
-
-
Ang(1-7) is a vasodilator peptide
-
?
angiotensin II + H2O
angiotensin(1-7) + L-Phe
-
angiotensin II has many adverse cardiovascular effects when acting through the AT1 receptor
-
-
?
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 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 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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
DX600
-
a decrease in thrombus ACE2 activity is associated with increased thrombus formation in nude mice
additional information
ACE2 activity in plasma is not altered by ibuprofen treatment
-
additional information
-
ACE-2 mRNA and activity are severely downregulated in lung fibrosis
-
additional information
-
not inhibited by captopril and benzyloxycarbonyl-Pro-Pro
-
additional information
-
the Spike protein of the SARS-coronavirus reduces ACE2 expression
-
additional information
-
central angiotensin II type 1 receptors reduce ACE2 expression/activity in hypertensive mice
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
losartan
-
an angiotensin II type 1 receptor blocker, increases central ACE2 activity. Losartan also restores brain ACE2 activity in transgenic RA mice, overview
XNT
-
activates ACE2, reduces platelet attachment to injured vessels, reduces thrombus size, and prolonges the time for complete vessel occlusion in mice. Thrombus area is reduced by 60%, whereas time for thrombus formation is prolonged by 45% in XNT-treated mice
additional information
ACE2 activity in plasma is not altered by ibuprofen treatment
-
additional information
-
no activation by PD123319, an angiotensin II type 2 antagonist
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
ACE2 is shedded in mouse proximal tubular cells at positions 18-706 and 18-577, respectively
additional information
overexpression to the forebrain, essentially the subfornical organ, inhibits both pressor and drinking responses resulting from intracerebroventricular administration of Ang-II
-
ACE and ACE2 co-localized strongly in the apical brush border of the proximal tubule
-
ACE2 and the AT2 receptor protect against lung injury. Exogenous recombinant human ACE2 attenuates acute lung failure in Ace knockout as well as in wild-type mice. Acute lung injury results in a marked downregulation of ACE2. Loss of ACE2 expression in acute lung injury leads to leaky pulmonary blood vessels through AT1 receptor stimulation
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
ACE2 is a type I membrane-anchored protein with a catalytically active ectodomain, that undergoes shedding
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
physiological function
malfunction
physiological function
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 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
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
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
malfunction
-
angiotensin II type 1 receptor-mediated reduction of angiotensin-converting enzyme 2 activity in the brain impairs baroreflex function in hypertensive mice
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
-
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
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 plays a critical role in influenzaA(H7N9) virus-induced acute lung injury
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
-
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ACE2_MOUSE
805
1
92368
Swiss-Prot
Secretory Pathway (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
ACE2 is a type I membrane-anchored protein with a catalytically active ectodomain, that undergoes shedding involving tumor necrosis factor alpha-converting enzyme, TACE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
ACE2 mRNA and protein expression in murine lung, heart and aorta is not influenced by ibuprofen
expression of ACE2 increases during aging in lungs. ACE2 expression increases upon telomere shortening or dysfunction. This increase is controlled at the transcriptional level, and ACE2 promoter activity is DNA damage response-dependent
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
SARS-CoV downregulates ACE2 protein by binding its spike protein, contributing to severe lung injury
central angiotensin II type 1 receptors reduce ACE2 expression/activity in hypertensive mice
-
infection with highly pathogenic avian influenza A H5N1 virus results in downregulation of angiotensin-converting enzyme 2 (ACE2) expression in the lung
-
infection with highly pathogenic avian influenza A H5N1 virus results in increased expression of angiotensin-converting enzyme 2 (ACE2) in serum
-
mice infected with influenza H7N9 virus downregulate ACE2 protein markedly on day 3 after infection
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
medicine
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
medicine
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
medicine
ACE2 offers a new target for the treatment of hypertension and other cardiovascular diseases
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
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
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
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
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
-
ACE-2 protects against lung fibrogenesis by limiting the local accumulation of the profibrotic peptide angiotensin II
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Elased, K.M.; Cunha, T.S.; Gurley, S.B.; Coffman, T.M.; Morris, M.
New mass spectrometric assay for angiotensin-converting enzyme 2 activity
Hypertension
47
1010-1017
2006
Homo sapiens, Mus musculus
Kuba, K.; Imai, Y.; Rao, S.; Gao, H.; Guo, F.; Guan, B.; Huan, Y.; Yang, P.; Zhang, Y.; Deng, W.; Bao, L.; Zhang, B.; Liu, G.; Wang, Z.; Chappell, M.; Liu, Y.; Zheng, D.; Leibbrandt, A.; Wada, T.; Slutsky, A.S.; Liu, D.; Qin, C.; Jiang, C.; Penninger, J.M.
A crucial role of angiotensin converting enzyme 2 (ACE2) in SARS coronavirus-induced lung injury
Nat. Med.
11
875-879
2005
Mus musculus
Imai, Y.; Kuba, K.; Rao, S.; Huan, Y.; Guo, F.; Guan, B.; Yang, P.; Sarao, R.; Wada, T.; Leong-Poi, H.; Crackower, M.A.; Fukamizu, A.; Hui, C.C.; Hein, L.; Uhlig, S.; Slutsky, A.S.; Jiang, C.; Penninger, J.M.
Angiotensin-converting enzyme 2 protects from severe acute lung failure
Nature
436
112-116
2005
Mus musculus
Li, X.; Molina-Molina, M.; Abdul-Hafez, A.; Uhal, V.; Xaubet, A.; Uhal, B.D.
Angiotensin converting enzyme-2 is protective but downregulated in human and experimental lung fibrosis
Am. J. Physiol. Lung Cell Mol. Physiol.
295
L178-185
2008
Homo sapiens, Mus musculus, Rattus norvegicus
Lambert, D.W.; Hooper, N.M.; Turner, A.J.
Angiotensin-converting enzyme 2 and new insights into the renin-angiotensin system
Biochem. Pharmacol.
75
781-786
2008
Homo sapiens, Mus musculus
Keidar, S.; Kaplan, M.; Gamliel-Lazarovich, A.
ACE2 of the heart: From angiotensin I to angiotensin (1-7)
Cardiovasc. Res.
73
463-469
2007
Mus musculus, Rattus norvegicus
Imai, Y.; Kuba, K.; Penninger, J.M.
Angiotensin-converting enzyme 2 in acute respiratory distress syndrome
Cell. Mol. Life Sci.
64
2006-2012
2007
Mus musculus
Imai, Y.; Kuba, K.; Penninger, J.M.
The discovery of angiotensin-converting enzyme 2 and its role in acute lung injury in mice
Exp. Physiol.
93
543-548
2008
Mus musculus
Garabelli, P.J.; Modrall, J.G.; Penninger, J.M.; Ferrario, C.M.; Chappell, M.C.
Distinct roles for angiotensin-converting enzyme 2 and carboxypeptidase A in the processing of angiotensins within the murine heart
Exp. Physiol.
93
613-621
2008
Mus musculus
Elased, K.M.; Cunha, T.S.; Marcondes, F.K.; Morris, M.
Brain angiotensin-converting enzymes: role of angiotensin-converting enzyme 2 in processing angiotensin II in mice
Exp. Physiol.
93
665-675
2008
Mus musculus
Ye, M.; Wysocki, J.; William, J.; Soler, M.J.; Cokic, I.; Batlle, D.
Glomerular localization and expression of angiotensin-converting enzyme 2 and angiotensin-converting enzyme: implications for albuminuria in diabetes
J. Am. Soc. Nephrol.
17
3067-3075
2006
Mus musculus
Wiener, R.S.; Cao, Y.X.; Hinds, A.; Ramirez, M.I.; Williams, M.C.
Angiotensin converting enzyme 2 is primarily epithelial and is developmentally regulated in the mouse lung
J. Cell. Biochem.
101
1278-1291
2007
Mus musculus (Q8R0I0), Mus musculus
Guo, H.; Guo, A.; Wang, C.; Yan, B.; Lu, H.; Chen, H.
Expression of feline angiotensin converting enzyme 2 and its interaction with SARS-CoV S1 protein
Res. Vet. Sci.
84
494-496
2008
Felis silvestris (Q56H28), Rattus norvegicus (Q5EGZ1), Mus musculus (Q8R0I0), Homo sapiens (Q9BYF1), Homo sapiens
Feng, Y.; Yue, X.; Xia, H.; Bindom, S.M.; Hickman, P.J.; Filipeanu, C.M.; Wu, G.; Lazartigues, E.
Angiotensin-converting enzyme 2 overexpression in the subfornical organ prevents the angiotensin II-mediated pressor and drinking responses and is associated with angiotensin II type 1 receptor downregulation
Circ. Res.
102
729-736
2008
Mus musculus (Q8R0I0), Mus musculus
Xia, H.; Lazartigues, E.
Angiotensin-converting enzyme 2 in the brain: properties and future directions
J. Neurochem.
107
1482-1494
2008
Rattus norvegicus (Q5EGZ1), Mus musculus (Q8R0I0), Homo sapiens (Q9BYF1)
Iwata, M.; Silva Enciso, J.E.; Greenberg, B.H.
Selective and specific regulation of ectodomain shedding of angiotensin-converting enzyme 2 by tumor necrosis factor alpha-converting enzyme
Am. J. Physiol. Cell Physiol.
297
C1318-C1329
2009
Cricetulus griseus, Mus musculus
Kassiri, Z.; Zhong, J.; Guo, D.; Basu, R.; Wang, X.; Liu, P.P.; Scholey, J.W.; Penninger, J.M.; Oudit, G.Y.
Loss of angiotensin-converting enzyme 2 accelerates maladaptive left ventricular remodeling in response to myocardial infarction
Circ. Heart Fail.
2
446-455
2009
Mus musculus
Xia, H.; Feng, Y.; Obr, T.D.; Hickman, P.J.; Lazartigues, E.
Angiotensin II type 1 receptor-mediated reduction of angiotensin-converting enzyme 2 activity in the brain impairs baroreflex function in hypertensive mice
Hypertension
53
210-216
2009
Mus musculus
Fraga-Silva, R.A.; Sorg, B.S.; Wankhede, M.; Dedeugd, C.; Jun, J.Y.; Baker, M.B.; Li, Y.; Castellano, R.K.; Katovich, M.J.; Raizada, M.K.; Ferreira, A.J.
ACE2 activation promotes antithrombotic activity
Mol. Med.
16
210-215
2010
Mus musculus, Rattus norvegicus
Lu, C.L.; Wang, Y.; Yuan, L.; Li, Y.; Li, X.Y.
The angiotensin-converting enzyme 2/angiotensin (1-7)/Mas axis protects the function of pancreatic beta cells by improving the function of islet microvascular endothelial cells
Int. J. Mol. Med.
34
1293-1300
2014
Mus musculus
Liu, S.; Liu, J.; Miura, Y.; Tanabe, C.; Maeda, T.; Terayama, Y.; Turner, A.J.; Zou, K.; Komano, H.
Conversion of Abeta43 to Abeta40 by the successive action of angiotensin-converting enzyme 2 and angiotensin-converting enzyme
J. Neurosci. Res.
92
1178-1186
2014
Homo sapiens, Mus musculus
Zou, Z.; Yan, Y.; Shu, Y.; Gao, R.; Sun, Y.; Li, X.; Ju, X.; Liang, Z.; Liu, Q.; Zhao, Y.; Guo, F.; Bai, T.; Han, Z.; Zhu, J.; Zhou, H.; Huang, F.; Li, C.; Lu, H.; Li, N.; Li, D.; Jin, N.; Penninger, J.M.; Jiang, C.
Angiotensin-converting enzyme 2 protects from lethal avian influenza A H5N1 infections
Nat. Commun.
5
3594
2014
Mus musculus
Feng, Y.; Hans, C.; McIlwain, E.; Varner, K.J.; Lazartigues, E.
Angiotensin-converting enzyme 2 over-expression in the central nervous system reduces angiotensin-II-mediated cardiac hypertrophy
PLoS ONE
7
e48910
2012
Mus musculus
Xiao, F.; Zimpelmann, J.; Agaybi, S.; Gurley, S.B.; Puente, L.; Burns, K.D.
Characterization of angiotensin-converting enzyme 2 ectodomain shedding from mouse proximal tubular cells
PLoS ONE
9
e85958
2014
Mus musculus
Yang, P.; Gu, H.; Zhao, Z.; Wang, W.; Cao, B.; Lai, C.; Yang, X.; Zhang, L.; Duan, Y.; Zhang, S.; Chen, W.; Zhen, W.; Cai, M.; Penninger, J.M.; Jiang, C.; Wang, X.
Angiotensin-converting enzyme 2 (ACE2) mediates influenza H7N9 virus-induced acute lung injury
Sci. Rep.
4
7027
2014
Mus musculus
Grobe, N.; Weir, N.M.; Leiva, O.; Ong, F.S.; Bernstein, K.E.; Schmaier, A.H.; Morris, M.; Elased, K.M.
Identification of prolyl carboxypeptidase as an alternative enzyme for processing of renal angiotensin II using mass spectrometry
Am. J. Physiol. Cell Physiol.
304
C945-C953
2013
Mus musculus
Wang, L.; Wang, Y.; Yang, T.; Guo, Y.; Sun, T.
Angiotensin-converting enzyme 2 attenuates bleomycin-induced lung fibrosis in mice
Cell. Physiol. Biochem.
36
697-711
2015
Mus musculus (Q8R0I0), Mus musculus
Cao, X.; Song, L.; Zhang, Y.; Li, Q.; Shi, T.; Yang, F.; Yuan, M.; Xin, Z.; Yang, J.
Angiotensin-converting enzyme 2 inhibits endoplasmic reticulum stress-associated pathway to preserve nonalcoholic fatty liver disease
Diabetes Metab. Res. Rev.
35
e3123
2019
Mus musculus (Q8R0I0), Homo sapiens (Q9BYF1)
Tian, X.; Li, C.; Huang, A.; Xia, S.; Lu, S.; Shi, Z.; Lu, L.; Jiang, S.; Yang, Z.; Wu, Y.; Ying, T.
Potent binding of 2019 novel coronavirus spike protein by a SARS coronavirus-specific human monoclonal antibody
Emerg. Microbes Infect.
9
382-385
2020
Mus musculus (Q8R0I0)
Wang, W.; McKinnie, S.; Farhan, M.; Paul, M.; McDonald, T.; McLean, B.; Llorens-Cortes, C.; Hazra, S.; Murray, A.; Vederas, J.; Oudit, G.
Angiotensin-converting enzyme 2 metabolizes and partially inactivates pyr-apelin-13 and apelin-17 Physiological effects in the cardiovascular system
Hypertension
68
365-377
2016
Mus musculus (Q8R0I0), Homo sapiens (Q9BYF1), Homo sapiens
Xiao, F.; Burns, K.D.
Measurement of angiotensin converting enzyme 2 activity in biological fluid (ACE2)
Methods Mol. Biol.
1527
101-115
2017
Mus musculus (Q8R0I0), Mus musculus, Homo sapiens (Q9BYF1), Homo sapiens
Sriramula, S.; Pedersen, K.B.; Xia, H.; Lazartigues, E.
Determining the enzymatic activity of angiotensin-converting enzyme 2 (ACE2) in brain tissue and cerebrospinal fluid using a quenched fluorescent substrate
Methods Mol. Biol.
1527
117-126
2017
Mus musculus (Q8R0I0)
Qiu, Y.; Zhao, Y.B.; Wang, Q.; Li, J.Y.; Zhou, Z.J.; Liao, C.H.; Ge, X.Y.
Predicting the angiotensin converting enzyme 2 (ACE2) utilizing capability as the receptor of SARS-CoV-2
Microbes Infect.
22
221-225
2020
Columba livia (A0A2I0MLI2), Sus scrofa (K7GLM4), Felis catus (Q56H28), Paguma larvata (Q56NL1), Mus musculus (Q8R0I0), Homo sapiens (Q9BYF1), Homo sapiens, Rhinolophus sinicus (U5WHY8), Capra hircus (W6CG84), Bos taurus (XP_005228485.1), Bubalus bubalis (XP_006041602.1), Ovis aries (XP_011961657.1), Manis javanica (XP_017505752.1)
Cao, X.; Yang, F.; Shi, T.; Yuan, M.; Xin, Z.; Xie, R.; Li, S.; Li, H.; Yang, J.K.
Angiotensin-converting enzyme 2/angiotensin-(1-7)/Mas axis activates Akt signaling to ameliorate hepatic steatosis
Sci. Rep.
6
21592
2016
Mus musculus (Q8R0I0), Homo sapiens (Q9BYF1)
Piplani, S.; Singh, P.K.; Winkler, D.A.; Petrovsky, N.
In silico comparison of SARS-CoV-2 spike protein-ACE2 binding affinities across species and implications for virus origin
Sci. Rep.
11
13063
2021
Mesocricetus auratus (A0A1U7QTA1), Macaca fascicularis (A0A2K5X283), Equus caballus (F6V9L3), Canis lupus familiaris (J9P7Y2), Canis lupus familiaris, Bos taurus (Q2HJI5), Mustela putorius furo (Q2WG88), Mustela putorius furo, Felis catus (Q56H28), Paguma larvata (Q56NL1), Mus musculus (Q8R0I0), Homo sapiens (Q9BYF1), Homo sapiens, Rhinolophus sinicus (U5WHY8), Ophiophagus hannah (V8NIH2), Panthera tigris (XP_007090142), Manis javanica (XP_017505752.1)
Chen, P.; Wang, J.; Xu, X.; Li, Y.; Zhu, Y.; Li, X.; Li, M.; Hao, P.
Molecular dynamic simulation analysis of SARS-CoV-2 spike mutations and evaluation of ACE2 from pets and wild animals for infection risk
Comput. Biol. Chem.
96
107613
2022
Manis javanica, Paguma larvata (Q56NL1), Mus musculus (Q8R0I0), Homo sapiens (Q9BYF1)
Sepe, S.; Rossiello, F.; Cancila, V.; Iannelli, F.; Matti, V.; Cicio, G.; Cabrini, M.; Marinelli, E.; Alabi, B.R.; di Lillo, A.; Di Napoli, A.; Shay, A.W.; Tripodo, C.; d'Adda di Fagagna, F.
DNA damage response at telomeres boosts the transcription of SARS-CoV-2 receptor ACE2 during aging
EMBO Rep.
23
e53658
2022
Mus musculus (Q8R0I0), Homo sapiens (Q9BYF1)
de Bruin, N.; Schneider, A.K.; Reus, P.; Talmon, S.; Ciesek, S.; Bojkova, D.; Cinatl, J.; Lodhi, I.; Charlesworth, B.; Sinclair, S.; Pennick, G.; Laughey, W.F.; Gribbon, P.; Kannt, A.; Schiffmann, S.
Ibuprofen, flurbiprofen, etoricoxib or paracetamol do not influence ACE2 expression and activity in vitro or in mice and do not exacerbate in-vitro SARS-CoV-2 infection
Int. J. Mol. Sci.
23
1049
2022
Mus musculus (Q8R0I0), Homo sapiens (Q9BYF1)
EXTERNAL LINKS (specific for EC-Number 3.4.17.23)
Transporter Classification Database (TCDB): 2.A.22.6.3, 8.A.139.1.1
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