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Literature summary extracted from

  • Low-Gan, J.; Huang, R.; Kelley, A.; Jenkins, G.W.; McGregor, D.; Smider, V.V.
    Diversity of ACE2 and its interaction with SARS-CoV-2 receptor binding domain (2021), Biochem. J., 478, 3671-3684 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.17.23 30 M HEK293 Freestyle cells are transfected with 293fectin combined with 30 mg of pFuse-based vectors containing the ACE2 construct Homo sapiens
3.4.17.23 30 M HEK293 Freestyle cells are transfected with 293fectin combined with 30 mg of pFuse-based vectors containing the ACE2 construct Rhinolophus sinicus
3.4.17.23 30 M HEK293 Freestyle cells are transfected with 293fectin combined with 30 mg of pFuse-based vectors containing the ACE2 construct Felis catus
3.4.17.23 30 M HEK293 Freestyle cells are transfected with 293fectin combined with 30 mg of pFuse-based vectors containing the ACE2 construct Cricetulus griseus
3.4.17.23 30 M HEK293 Freestyle cells are transfected with 293fectin combined with 30 mg of pFuse-based vectors containing the ACE2 construct Mustela putorius
3.4.17.23 30 M HEK293 Freestyle cells are transfected with 293fectin combined with 30 mg of pFuse-based vectors containing the ACE2 construct Bos taurus

Organism

EC Number Organism UniProt Comment Textmining
3.4.17.23 Bos taurus XP_024843618.1
-
-
3.4.17.23 Cricetulus griseus XP_003503283.12
-
-
3.4.17.23 Felis catus Q56H28
-
-
3.4.17.23 Homo sapiens Q9BYF1
-
-
3.4.17.23 Mustela putorius Q2WG88
-
-
3.4.17.23 Rhinolophus sinicus U5WHY8
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.17.23 recombinant enzyme Homo sapiens
3.4.17.23 recombinant enzyme Rhinolophus sinicus
3.4.17.23 recombinant enzyme Felis catus
3.4.17.23 recombinant enzyme Cricetulus griseus
3.4.17.23 recombinant enzyme Mustela putorius
3.4.17.23 recombinant enzyme Bos taurus

Synonyms

EC Number Synonyms Comment Organism
3.4.17.23 ACE2
-
 Homo sapiens
3.4.17.23 ACE2
-
 Rhinolophus sinicus
3.4.17.23 ACE2
-
 Felis catus
3.4.17.23 ACE2
-
 Cricetulus griseus
3.4.17.23 ACE2
-
 Mustela putorius
3.4.17.23 ACE2
-
 Bos taurus

General Information

EC Number General Information Comment Organism
3.4.17.23 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 Homo sapiens
3.4.17.23 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 Rhinolophus sinicus
3.4.17.23 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 Felis catus
3.4.17.23 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 Cricetulus griseus
3.4.17.23 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 Mustela putorius
3.4.17.23 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 Bos taurus
3.4.17.23 physiological function SARS-CoV-2 binds to the angiotensin I converting enzyme 2 (ACE2) to enable its entry into host cells and establish infection Homo sapiens
3.4.17.23 physiological function SARS-CoV-2 binds to the angiotensin I converting enzyme 2 (ACE2) to enable its entry into host cells and establish infection Rhinolophus sinicus
3.4.17.23 physiological function SARS-CoV-2 binds to the angiotensin I converting enzyme 2 (ACE2) to enable its entry into host cells and establish infection Felis catus
3.4.17.23 physiological function SARS-CoV-2 binds to the angiotensin I converting enzyme 2 (ACE2) to enable its entry into host cells and establish infection Cricetulus griseus
3.4.17.23 physiological function SARS-CoV-2 binds to the angiotensin I converting enzyme 2 (ACE2) to enable its entry into host cells and establish infection Mustela putorius
3.4.17.23 physiological function SARS-CoV-2 binds to the angiotensin I converting enzyme 2 (ACE2) to enable its entry into host cells and establish infection Bos taurus