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

BRENDA support

Literature summary for 3.4.22.B80 extracted from

  • Quimque, M.T.J.; Notarte, K.I.R.; Fernandez, R.A.T.; Mendoza, M.A.O.; Liman, R.A.D.; Lim, J.A.K.; Pilapil, L.A.E.; Ong, J.K.H.; Pastrana, A.M.; Khan, A.; Wei, D.Q.; Macabeo, A.P.G.
    Virtual screening-driven drug discovery of SARS-CoV2 enzyme inhibitors targeting viral attachment, replication, post-translational modification and host immunity evasion infection mechanisms (2020), J. Biomol. Struct. Dyn., 2020, 1-18 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.22.B80

Application

Application Comment Organism
drug development virtual screening-driven drug discovery of SARS-CoV2 enzyme inhibitors targeting viral attachment, replication, post-translational modification and host immunity evasion infection mechanisms. Scedapin C, quinadoline B, norquinadoline A, isochaetochromin D1 and 11alpha-dehydroxyisoterreulactone A exhibit high binding affinities on papain-like protease. Molecular dynamics simulation and subsequent totalfree energy calculation reveal that the complexes formed between the top-ranked ligands and their respective protein targets are dynamically stable with high total free energy of binding. Therefore, these compounds can be utilized as templates or prototypes for further development of multitargeting ligands against SARS-CoV2 Severe acute respiratory syndrome coronavirus 2

Inhibitors

Inhibitors Comment Organism Structure
additional information scedapin C, quinadoline B and norquinadoline A, isochaetochromin D1, 11alpha-dehydroxyisoterreulactone A exhibit high binding affinities on papain-like protease. Molecular dynamics simulation and subsequent total free energy calculation reveal that the complexes formed between the ligands and their respective protein targets are dynamically stable with high total free energy of binding. Therefore, these compounds can be utilized as templates or prototypes for further development of multitargeting ligands against SARS-CoV2 Severe acute respiratory syndrome coronavirus 2

Organism

Organism UniProt Comment Textmining
Severe acute respiratory syndrome coronavirus 2
-
 SARS-CoV-2
-

General Information

General Information Comment Organism
physiological function the enzyme is responsible for the cleavages located at the N-terminus of the replicase polyprotein Severe acute respiratory syndrome coronavirus 2