Literature summary for 3.4.22.69 extracted from

Chu, L.H.; Choy, W.Y.; Tsai, S.N.; Rao, Z.; Ngai, S.M.
Rapid peptide-based screening on the substrate specificity of severe acute respiratory syndrome (SARS) coronavirus 3C-like protease by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (2006), Protein Sci., 15, 699-709.

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Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
additional information	Severe acute respiratory syndrome-related coronavirus	SARS-CoV 3CLpro mediates extensive proteolytic processing of two overlapping replicase polyproteins, pp1a (486000 Da) and pp1ab (790000 Da), to yield the corresponding functional polypeptides that are essential for SARSCoV replication and transcription processes	?	-	?

Organism

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

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	SARS-CoV 3CLpro mediates extensive proteolytic processing of two overlapping replicase polyproteins, pp1a (486000 Da) and pp1ab (790000 Da), to yield the corresponding functional polypeptides that are essential for SARSCoV replication and transcription processes	Severe acute respiratory syndrome-related coronavirus	?	-	?
additional information	comprehensive overview of SARS-CoV 3CLpro substrate specificity. The hydrophobic pocket in the P2 position at the protease cleavage site is crucial to SARS-CoV 3CLpro-specific binding, which is limited to substitution by hydrophobic residue. The binding interface of SARS-CoV 3CLpro that is facing the P1' position is suggested to be occupied by acidic amino acids, thus the P1' position is intolerant to acidic residue substitution, owing to electrostatic repulsion. Steric hindrance caused by some bulky or branching amino acids in P3 and P2' positions may also hinder the binding of SARS-CoV 3CLpro. In addition to the conserved Gln residue in the P1 position at the SARS-CoV 3CLpro cleavage site, the P2 position, which is exclusively occupied by Leu residue, also serves as another important determinant of substrate specificity. Peptide substrate with Phe replacement in the P2 position is also favorable for SARSCoV 3CLpro cleavage. Ile is intolerant in the P2 position. P1' position, which is frequently occupied by Ser residue, also contributes to the substrate specificity of SARS-CoV 3CLpro considerably. The P1' position is highly unfavorable to the substitution by Pro, Asp, and Glu residues. The substrate specificity of SARS-CoV 3CLpro is less dependent on the P2' and P3 positions at the cleavage site. The peptide cleavage results show that the P3' and P4 positions have no effect on determining the substrate specificity preferences of SARS-CoV 3CLpro	Severe acute respiratory syndrome-related coronavirus	?	-	?

Synonyms

Synonyms	Comment	Organism
severe acute respiratory syndrome coronavirus 3C-like protease	-	Severe acute respiratory syndrome-related coronavirus

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Release 2023.1 (January 2023)