Literature summary for 3.4.22.44 extracted from

Sun, P.; Austin, B.P.; Toezser, J.; Waugh, D.S.
Structural determinants of tobacco vein mottling virus protease substrate specificity (2010), Protein Sci., 19, 2240-2251.

Search for more literature for 3.4.22.44

Cloned(Commentary)

Cloned (Comment)	Organism
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)	tobacco vein mottling virus

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant mutant TVMV protease K65A/K67A/C151A in complex with a canonical peptide substrate RETVRFQSD, mixing of protein solution with 10 mg/ml protein with a fivefold molar excess of the peptide substrate RETVRFQSD, crystallization from a solution consisting of 0.2 M potassium formate and 20% PEG 3350, space group P212121, X-ray diffraction structure determination and analysis at 1.7 A resolution, the 20-residue C-terminus of TVMV protease is disordered, molecular replacement, using the crystal structure of TEV protease, PDB code 1Q31	tobacco vein mottling virus

Crystallization (Comment)

Organism

purified recombinant mutant TVMV protease K65A/K67A/C151A in complex with a canonical peptide substrate RETVRFQSD, mixing of protein solution with 10 mg/ml protein with a fivefold molar excess of the peptide substrate RETVRFQSD, crystallization from a solution consisting of 0.2 M potassium formate and 20% PEG 3350, space group P212121, X-ray diffraction structure determination and analysis at 1.7 A resolution, the 20-residue C-terminus of TVMV protease is disordered, molecular replacement, using the crystal structure of TEV protease, PDB code 1Q31

tobacco vein mottling virus

Protein Variants

Protein Variants	Comment	Organism
C151A	catalytically inactive mutant TVMV protease	tobacco vein mottling virus
K65A/K67A/C151A	catalytically inactive mutant TVMV protease	tobacco vein mottling virus
additional information	a truncation mutant of TVMV protease lacking the 20 C-terminal amino acid residues, TVMV1-217 protease, shows reduced activity compared to the wild-type enzyme	tobacco vein mottling virus

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.082	-	TETVRFQSGTRR	recombinant wild-type TVMV protease, pH 7.0, 30°C	tobacco vein mottling virus
0.108	-	TETVRFQSGTRR	recombinant mutant TVMV1-217 protease, pH 7.0, 30°C	tobacco vein mottling virus

Organism

Organism	UniProt	Comment	Textmining
tobacco vein mottling virus	Q9J0W2	TVMV	-

Source Tissue

Source Tissue	Comment	Organism	Textmining

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
additional information	the S3 and S4 pockets are mainly responsible for the substrate specificity, comparison to the specificity of the tobacco etch virus, TEV, protease, structural determinants of substrate specificity, overview. The TVMV protease is less tolerant of variation at the P1' position than TEV protease, and substitutions in the P6 position are more readily tolerated by TVMV than TEV protease	tobacco vein mottling virus	?	-	?
RETVRFQSD + H2O	-	tobacco vein mottling virus	?	-	?
TETVRFQSGTRR + H2O	-	tobacco vein mottling virus	?	-	?

Subunits

Subunits	Comment	Organism
More	three-dimensional structure of TVMV protease, overview	tobacco vein mottling virus

Synonyms

Synonyms	Comment	Organism
tobacco vein mottling virus protease	-	tobacco vein mottling virus

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
30	-	assay at	tobacco vein mottling virus

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
0.092	-	TETVRFQSGTRR	recombinant wild-type TVMV protease, pH 7.0, 30°C	tobacco vein mottling virus
0.094	-	TETVRFQSGTRR	recombinant mutant TVMV1-217 protease, pH 7.0, 30°C	tobacco vein mottling virus

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7	-	assay at	tobacco vein mottling virus

General Information

General Information	Comment	Organism
physiological function	the TVMV genome is translated into a single large polyprotein that is subsequently processed by three virally encoded proteases. Seven of the nine cleavage events are carried out by the NIa protease	tobacco vein mottling virus

kcat/KM [mM/s]

kcat/KM Value [1/mMs^-1]	kcat/KM Value Maximum [1/mMs^-1]	Substrate	Comment	Organism	Structure
0.87	-	TETVRFQSGTRR	recombinant mutant TVMV1-217 protease, pH 7.0, 30°C	tobacco vein mottling virus
1.12	-	TETVRFQSGTRR	recombinant wild-type TVMV protease, pH 7.0, 30°C	tobacco vein mottling virus