Literature summary for 3.4.22.28 extracted from

Wang, J.; Fan, T.; Yao, X.; Wu, Z.; Guo, L.; Lei, X.; Wang, J.; Wang, M.; Jin, Q.; Cui, S.
Crystal structures of enterovirus 71 3C protease complexed with rupintrivir reveal the roles of catalytically important residues (2011), J. Virol., 85, 10021-10030.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
high-resolution crystal structures of the EV71 3Cpro/rupintrivir complex is determined, showing that although rupintrivir interacts with EV71 3Cpro similarly to HRV 3Cpro, the C terminus of the inhibitor cannot accommodate the leaving-group pockets of EV71 3Cpro. EV71 3Cpro possesses a surface-recessive S2' pocket that is not present in HRV 3Cpro that contributes to the additional substrate binding affinity	Enterovirus A71

Crystallization (Comment)

Organism

high-resolution crystal structures of the EV71 3Cpro/rupintrivir complex is determined, showing that although rupintrivir interacts with EV71 3Cpro similarly to HRV 3Cpro, the C terminus of the inhibitor cannot accommodate the leaving-group pockets of EV71 3Cpro. EV71 3Cpro possesses a surface-recessive S2' pocket that is not present in HRV 3Cpro that contributes to the additional substrate binding affinity

Enterovirus A71

Protein Variants

Protein Variants	Comment	Organism
E71D	enzyme is void of catalytic activity. Structure of mutant E71D is determined: The structure shows that when Glu71 is replaced by Asp, the side chain is simply too short to reach the catalytic histidine and thus cannot provide enough electrostatic stabilization to the residue	Enterovirus A71
H133G	mutant H133G has close-to-wild-type enzyme activity and substrate specificity. Due to the practical difficulty in obtaining the measurable crystals from the wild-type, H133G mutant is used	Enterovirus A71
N69D	kcat/Km values are significantly reduced in mutant compared to wild-type	Enterovirus A71
N69S	kcat/Km values are significantly reduced in mutant compared to wild-type	Enterovirus A71
R39E	kcat/Km values are significantly reduced in mutant compared to wild-type	Enterovirus A71
R39K	kcat/Km values are significantly reduced in mutant compared to wild-type	Enterovirus A71
R39T	kcat/Km values are significantly reduced in mutant compared to wild-type	Enterovirus A71

Inhibitors

Inhibitors	Comment	Organism	Structure
rupintrivir	-	Enterovirus A71

Organism

Organism	UniProt	Comment	Textmining
Enterovirus A71	E9LTP4	3C pro	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
Dabcyl-RTATVQGPSLDFE-EDANS + H2O	-	Enterovirus A71	Dabcyl-RTATVQ + GPSLDFE-EDANS	-	?

Synonyms

Synonyms	Comment	Organism
3C protease	-	Enterovirus A71
3Cpro	-	Enterovirus A71

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
30	-	assay at	Enterovirus A71

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7	-	assay at	Enterovirus A71

IC50 Value

IC50 Value	IC50 Value Maximum	Comment	Organism	Inhibitor	Structure
0.0023	-	pH 7.0, 30°C	Enterovirus A71	rupintrivir