Literature summary for 3.4.22.69 extracted from

Yin, J.; Niu, C.; Cherney, M.M.; Zhang, J.; Huitema, C.; Eltis, L.D.; Vederas, J.C.; James, M.N.
A mechanistic view of enzyme inhibition and peptide hydrolysis in the active site of the SARS-CoV 3C-like peptidase (2007), J. Mol. Biol., 371, 1060-1074.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Severe acute respiratory syndrome-related coronavirus

Crystallization (Commentary)

Crystallization (Comment)	Organism
SARS 3CLpro bound to two phthalhydrazide-charged peptidyl inhibitors, acetyl-valyl-(O-benzyloxy)threonyl-leucyl-ketomethyl(cycloglutamine)-phthalhydrazide and acetyl-leucylalanyl-alanyl-ketomethyl(cycloglutamine)-phthalhydrazide. The inhibitors are covalently attached to SARS 3CLpro in crystals	Severe acute respiratory syndrome-related coronavirus

Inhibitors

Inhibitors	Comment	Organism	Structure
acetyl-leucylalanyl-alanyl-ketomethyl(cycloglutamine)-phthalhydrazide	-	Severe acute respiratory syndrome-related coronavirus
acetyl-valyl-(O-benzyloxy)threonyl-leucyl-ketomethyl(cycloglutamine)-phthalhydrazide	-	Severe acute respiratory syndrome-related coronavirus

Organism

Organism	UniProt	Comment	Textmining
Severe acute respiratory syndrome-related coronavirus	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Severe acute respiratory syndrome-related coronavirus

Synonyms

Synonyms	Comment	Organism
SARS-CoV 3C-like peptidase	-	Severe acute respiratory syndrome-related coronavirus

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Release 2023.1 (January 2023)