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Literature summary for 3.4.21.91 extracted from

  • Huang, Q.; Li, Q.; Joy, J.; Chen, A.S.; Ruiz-Carrillo, D.; Hill, J.; Lescar, J.; Kang, C.
    Lyso-myristoyl phosphatidylcholine micelles sustain the activity of Dengue non-structural (NS) protein 3 protease domain fused with the full-length NS2B (2013), Protein Expr. Purif., 92, 156-162.
    View publication on PubMed

Application

Application Comment Organism
synthesis expression and purification of a natural form of DENV protease containing the full-length NS2B protein and the protease domain of NS3. The protease is expressed in Escherichia coli and purified in detergent micelles necessary for its folding. This purified protein is active in detergent micelles such as lyso-myristoyl phosphatidylcholine Dengue virus

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Dengue virus

Organism

Organism UniProt Comment Textmining
Dengue virus
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Purification (Commentary)

Purification (Comment) Organism
expression and purification of a natural form of DENV protease containing the full-length NS2B protein and the protease domain of NS3. Purified protein in lyso-myristoyl phosphatidylcholine, Fos-14 and Fos15 exhibits protease activity, while almost no activity is observed in Lyso-myristoyl phosphatidylglycerol micelles. The purified protease also exhibits self-cleavage activity when it is purified in lyso-myristoyl phosphatidylcholine micelles, but not in other detergent micelles Dengue virus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
benzoyl-Nle-Lys-Arg-Arg-4-methylcoumarin 7-amide + H2O
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Dengue virus benzoyl-Nle-Lys-Arg-Arg + 7-amino-4-methylcoumarin
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