SARS coronavirus main proteinase;
3cLpro;
3C-like protease;
coronavirus 3C-like protease;
Mpro;
SARS 3C-like protease;
SARS coronavirus 3CL protease;
SARS coronavirus main peptidase;
SARS coronavirus main protease;
SARS-CoV 3CLpro enzyme;
SARS-CoV main protease;
SARS-CoV Mpro;
severe acute respiratory syndrome coronavirus main protease

Hydrolases;
Acting on peptide bonds (peptidases);
Cysteine endopeptidases

TSAVLQ!SGFRK-NH2 and SGVTFQ!GKFKK the two peptides corresponding to the two self-cleavage sites of the SARS 3C-like proteinase are the two most reactive peptide substrates. The enzyme exhibits a strong preference for substrates containing Gln at P1 position and Leu at P2 position.

SARS coronavirus main protease is the key enzyme in SARS coronavirus replicase polyprotein processing. In peptidase family C30.

1  [PMID:17605471]

Goetz DH, Choe Y, Hansell E, Chen YT, McDowell M, Jonsson CB, Roush WR, McKerrow J, Craik CS

Substrate specificity profiling and identification of a new class of inhibitor for the major protease of the SARS coronavirus.

Biochemistry. 46 (2007) 8744-52.

2  [PMID:14561748]

Fan K, Wei P, Feng Q, Chen S, Huang C, Ma L, Lai B, Pei J, Liu Y, Chen J, Lai L

Biosynthesis, purification, and substrate specificity of severe acute respiratory syndrome coronavirus 3C-like proteinase.

J. Biol. Chem. 279 (2004) 1637-42.

3  [PMID:18845442]

Akaji K, Konno H, Onozuka M, Makino A, Saito H, Nosaka K

Evaluation of peptide-aldehyde inhibitors using R188I mutant of SARS 3CL protease as a proteolysis-resistant mutant.

Bioorg. Med. Chem. 16 (2008) 9400-8.