Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Chen, Y.; Guo, Y.; Pan, Y.; Zhao, Z.
    Structure analysis of the receptor binding of 2019-nCoV (2020), Biochem. Biophys. Res. Commun., 525, 135-140.
    View publication on PubMed

Application

EC Number Application Comment Organism
3.4.17.23 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 Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
3.4.17.23 Callorhinchus milii XP_007889845.1
-
-
3.4.17.23 Homo sapiens Q9BYF1
-
-
3.4.17.23 Nipponia nippon A0A091UR55
-
-
3.4.17.23 Paguma larvata Q56NL1
-
-
3.4.17.23 Protobothrops mucrosquamatus XP_029140508.1
-
-
3.4.17.23 Rhinolophus sinicus E2DHI7
-
-
3.4.17.23 Xenopus laevis XP_018104311.1
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.17.23 intestine predominantly expressed in intestines, testis, and kidney Homo sapiens
-
3.4.17.23 kidney predominantly expressed in intestines, testis, and kidney Homo sapiens
-
3.4.17.23 lung expression level of ACE2 in the lung is minimal Homo sapiens
-
3.4.17.23 testis predominantly expressed in intestines, testis, and kidney Homo sapiens
-

Synonyms

EC Number Synonyms Comment Organism
3.4.17.23 ACE2
-
 Homo sapiens
3.4.17.23 ACE2
-
 Paguma larvata
3.4.17.23 ACE2
-
 Rhinolophus sinicus
3.4.17.23 ACE2
-
 Nipponia nippon
3.4.17.23 ACE2
-
 Protobothrops mucrosquamatus
3.4.17.23 ACE2
-
 Xenopus laevis
3.4.17.23 ACE2
-
 Callorhinchus milii

General Information

EC Number General Information Comment Organism
3.4.17.23 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 Homo sapiens
3.4.17.23 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 Homo sapiens
3.4.17.23 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 Paguma larvata
3.4.17.23 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 Rhinolophus sinicus
3.4.17.23 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 Nipponia nippon
3.4.17.23 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 Protobothrops mucrosquamatus
3.4.17.23 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 Xenopus laevis
3.4.17.23 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 Callorhinchus milii
3.4.17.23 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 Homo sapiens
3.4.17.23 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 Paguma larvata
3.4.17.23 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 Rhinolophus sinicus
3.4.17.23 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 Nipponia nippon
3.4.17.23 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 Protobothrops mucrosquamatus
3.4.17.23 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 Xenopus laevis
3.4.17.23 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 Callorhinchus milii