Literature summary for 3.4.22.69 extracted from

Wu, C.G.; Cheng, S.C.; Chen, S.C.; Li, J.Y.; Fang, Y.H.; Chen, Y.H.; Chou, C.Y.
Mechanism for controlling the monomer-dimer conversion of SARS coronavirus main protease (2013), Acta Crystallogr. Sect. D, 69, 747-755.

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Application

Application	Comment	Organism
drug development	the enzyme is an attractive target for the development of anti-SARS drugs	Severe acute respiratory syndrome-related coronavirus

Cloned(Commentary)

Cloned (Comment)	Organism
recombinant expression of His-tagged mutant R298A enzyme in Escherichia coli strain BL21(DE3) from pET-28a(+) vector	Severe acute respiratory syndrome-related coronavirus

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant mutant enzyme R298A with bound substrate, sitting drop vapour diffusion method, mixing of 15 mg/ml protein with substrate TSAVLQ-4-nitroanilide and reservoir solution containing 0.1 M Tris, pH 8.0, 30% w/v PEG 300, 5% w/v PEG 1000, 22°C, 3 days, X-ray diffraction structure determination and analysis at 2.09 A resolution, molecular replacement method	Severe acute respiratory syndrome-related coronavirus

Protein Variants

Protein Variants	Comment	Organism
R298A	site-directed mutagenesis, the enzyme mutant shows a reversible substrate-induced dimerization that is essential for catalysis. In substrate-bound mutant enzyme crystals, a dimer with a mutual orientation of the monomers that differs from that of the wild-type protease is present in the asymmetric unit. The presence of a complete substrate-binding pocket and oxyanion hole in both protomers suggests that they are both catalytically active, while the two domain IIIs show minor reorganization. Reorganization of the dimer in the R298A mutant, verview	Severe acute respiratory syndrome-related coronavirus

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining

Organism

Organism	UniProt	Comment	Textmining
Severe acute respiratory syndrome-related coronavirus	P0C6U8	polyprotein; SARS CoV	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant His-tagged mutant R298A enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, followed by gel filtration and ultrafiltration	Severe acute respiratory syndrome-related coronavirus

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
pp1a + H2O	cleavage of a viron polyprotein	Severe acute respiratory syndrome-related coronavirus	?	-	?
pp1ab + H2O	cleavage of a viron polyprotein	Severe acute respiratory syndrome-related coronavirus	?	-	?
TSAVLQ-4-nitroanilide + H2O	-	Severe acute respiratory syndrome-related coronavirus	TSAVLQ + 4-nitroaniline	-	?

Subunits

Subunits	Comment	Organism
homodimer	the coronaviral enzyme consists of three domains and the catalytic dyad His/Cys is located at the interface between domains I and II. The first two domains have an antiparallel beta-barrel structure that forms a folding scaffold similar to other viral chymotrypsin-like proteases. The functional unit of Mpro is a homodimer and each subunit contains a His41-Cys145 catalytic dyad	Severe acute respiratory syndrome-related coronavirus
More	molecular mechanism of substrate-induced dimerization, overview	Severe acute respiratory syndrome-related coronavirus

Synonyms

Synonyms	Comment	Organism
3cLpro	-	Severe acute respiratory syndrome-related coronavirus
SARS coronavirus main protease	-	Severe acute respiratory syndrome-related coronavirus
SARS coronavirus Mpro	-	Severe acute respiratory syndrome-related coronavirus
SARSCoV main protease	-	Severe acute respiratory syndrome-related coronavirus
SARSCoV Mpro	-	Severe acute respiratory syndrome-related coronavirus
severe acute respiratory syndrome coronavirus main protease	-	Severe acute respiratory syndrome-related coronavirus
severe acute respiratory syndrome coronavirus Mpro	-	Severe acute respiratory syndrome-related coronavirus

General Information

General Information	Comment	Organism
additional information	the functional unit of Mpro is a homodimer and each subunit contains a His41-Cys145 catalytic dyad. Presence of a complete substrate-binding pocket and oxyanion hole in both protomers. Reversible substrate-induced dimerization is essential for catalysis, molecular mechanism, overview	Severe acute respiratory syndrome-related coronavirus

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Release 2023.1 (January 2023)