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?:abstract
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The novel severe acute respiratory syndrome coronavirus (SARS-CoV-2) has emerged to a pandemic and caused global public health crisis. Human angiotensin-converting enzyme 2(ACE2) was identified as the entry receptor for SARS-CoV-2. As a carboxypeptidase, ACE2 cleaves many biological substrates besides angiotensin II to control vasodilatation and vascular permeability. Given the nanomolar high affinity between ACE2 and SARS-CoV-2 spike protein, we investigated how this interaction would affect the enzymatic activity of ACE2. Surprisingly, SARS-CoV-2 trimeric spike protein increased ACE2 proteolytic activity ∼3-10 fold against model peptide substrates, such as caspase-1 substrate and Bradykinin-analog. The enhancement in ACE2 enzymatic function was mediated by the binding of SARS-CoV-2 spike RBD domain. These results highlighted the potential for SARS-CoV-2 infection to enhance ACE2 activity, which may be relevant to the cardiovascular symptoms associated with COVID-19.
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?:doi
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?:doi
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?:journal
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J_Biol_Chem
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The_Journal_of_biological_chemistry
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?:license
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?:pdf_json_files
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document_parses/pdf_json/4b0878cc12d2bc1114e93ac98209791ee40f5a3c.json
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document_parses/pmc_json/PMC7833600.xml.json
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of
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?:source
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Elsevier; Medline; PMC
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Medline
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?:title
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High affinity binding of SARS-CoV-2 spike protein enhances ACE2 carboxypeptidase activity
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High affinity binding of SARS-CoV-2 spike protein enhances ACE2 carboxypeptidase activity.
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