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Literature summary for 3.4.22.28 extracted from

  • Ullah, R.; Shah, M.A.; Tufail, S.; Ismat, F.; Imran, M.; Iqbal, M.; Mirza, O.; Rhaman, M.
    Activity of the human rhinovirus 3C protease studied in various buffers, additives and detergents solutions for recombinant protein production (2016), PLoS ONE, 11, e0153436 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.22.28

Cloned(Commentary)

Cloned (Comment) Organism
recombinant overexpression of 3C protease, containing a His8-tag, an extended linker (MSTLESSGAASG), maltose binding protein (MBP), and a TEV protease cleavable site upstream from the multiple cloning site, in Escherichia coli strains Rosetta 2 (DE3) or BL21(DE3) Human rhinovirus sp.

General Stability

General Stability Organism
HRV 3C protease activity is completely abolished in the presence of eight detergents: C-HEGA1-10, C-HEGA1-9, HEGA1-8, CYMAL1-2, n-decyl-N,N-dimethylglycine, MEGA-8, FOS-choline1-8 and ANAPOE1-20 Human rhinovirus sp.

Inhibitors

Inhibitors Comment Organism Structure
additional information HRV 3C protease activity is completely abolished in the presence of eight detergents (C-HEGA1-10, C-HEGA1-9, HEGA1-8, CYMAL1-2, n-decyl-N,N-dimethylglycine, MEGA-8, FOS-choline1-8 and ANAPOE1-20) Human rhinovirus sp.

Organism

Organism UniProt Comment Textmining
Human rhinovirus sp.
-
 HRV
-

Synonyms

Synonyms Comment Organism
HRV 3C protease
-
 Human rhinovirus sp.
Human rhinovirus 3C protease
-
 Human rhinovirus sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
-
 Human rhinovirus sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
 Human rhinovirus sp.

General Information

General Information Comment Organism
additional information analysis of effect of elution buffers used for common affinity based purifications, salt ions, stability/solubility and reducing agents, and detergents on the activity of the heterologously overexpressed human rhinovirus 3C protease using three different fusion proteins at 4°C, overview. The enzyme activity is insensitive to most of the experimental conditions tested. Optimization of cleavage conditions for HRV 3C and TEV protease Human rhinovirus sp.