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SARS coronavirus main proteinase (EC 3.4.22.69, 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) is an enzyme.^[1]^[2]^[3] This enzyme catalyses the following chemical reaction

TSAVLQ-SGFRK-NH2 and SGVTFQ-!GKFKK are the two peptides corresponding to the two self-cleavage sites of the SARS 3C-like proteinase

This protease is important in SARS coronavirus replicase polyprotein processing.

References[edit]

^ Goetz, D.H.; Choe, Y.; Hansell, E.; Chen, Y.T.; McDowell, M.; Jonsson, C.B.; Roush, W.R.; McKerrow, J.; Craik, C.S. (2007). "Substrate specificity profiling and identification of a new class of inhibitor for the major protease of the SARS coronavirus". Biochemistry. 46: 8744–8752. doi:10.1021/bi0621415. PMID 17605471.
^ Fan, K.; Wei, P.; Feng, Q.; Chen, S.; Huang, C.; Ma, L.; Lai, B.; Pei, J.; Liu, Y.; Chen, J.; Lai, L. (2004). "Biosynthesis, purification, and substrate specificity of severe acute respiratory syndrome coronavirus 3C-like proteinase". J. Biol. Chem. 279: 1637–1642. doi:10.1074/jbc.m310875200. PMID 14561748.{{cite journal}}: CS1 maint: unflagged free DOI (link)
^ Akaji, K.; Konno, H.; Onozuka, M.; Makino, A.; Saito, H.; Nosaka, K. (2008). "Evaluation of peptide-aldehyde inhibitors using R188I mutant of SARS 3CL protease as a proteolysis-resistant mutant". Bioorg. Med. Chem. 16: 9400–9408. doi:10.1016/j.bmc.2008.09.057. PMID 18845442.

External links[edit]

SARS+coronavirus+main+proteinase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

[1] Goetz, D.H.; Choe, Y.; Hansell, E.; Chen, Y.T.; McDowell, M.; Jonsson, C.B.; Roush, W.R.; McKerrow, J.; Craik, C.S. (2007). "Substrate specificity profiling and identification of a new class of inhibitor for the major protease of the SARS coronavirus". Biochemistry. 46: 8744–8752. doi:10.1021/bi0621415. PMID 17605471.

[2] Fan, K.; Wei, P.; Feng, Q.; Chen, S.; Huang, C.; Ma, L.; Lai, B.; Pei, J.; Liu, Y.; Chen, J.; Lai, L. (2004). "Biosynthesis, purification, and substrate specificity of severe acute respiratory syndrome coronavirus 3C-like proteinase". J. Biol. Chem. 279: 1637–1642. doi:10.1074/jbc.m310875200. PMID 14561748.{{cite journal}}: CS1 maint: unflagged free DOI (link)

[3] Akaji, K.; Konno, H.; Onozuka, M.; Makino, A.; Saito, H.; Nosaka, K. (2008). "Evaluation of peptide-aldehyde inhibitors using R188I mutant of SARS 3CL protease as a proteolysis-resistant mutant". Bioorg. Med. Chem. 16: 9400–9408. doi:10.1016/j.bmc.2008.09.057. PMID 18845442.

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v t e Proteases: cysteine proteases (EC 3.4.22)
Caspase	Caspase 1 Caspase 2 Caspase 3 Caspase 4 Caspase 5 Caspase 6 Caspase 7 Caspase 8 Caspase 9 Caspase 10 Caspase 12 Caspase 13 Caspase 14
Fruit-derived	Papain Ficain Bromelain Actinidain
Calpain	CAPN1 CAPN2 CAPN3 CAPN5 CAPN6 CAPN7 CAPN8 CAPN9 CAPN10 CAPN11 CAPN12 CAPN13 CAPN14 CAPNS1 CAPNS2
Cathepsin	B C F H K L1/L2 O S W Z
Other	Clostripain Cancer procoagulant Separase Autophagin Cruzipain 3C-like protease Gingipain R Gingipain K

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)