Difference between revisions of "Part:BBa K4020003"
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==Usage and Biology==
 
==Usage and Biology==
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The DNA sequence encodes for a highly sequence-specific cysteine protease, a 27‐kDa catalytic domain of the polyprotein nuclear inclusion a (NIa) in tobacco etch virus (Nam et al., 2020). Its target substrate is the sequence ENLYFQS/G and it cleaves between Q and G/S (Nam et al., 2020), all the while requiring a Gly or Ser residue to be in the P1' position so as to process the substrate with reasonable efficiency (Kapust et al., 2002). Located at the interior of the domain, His46, Asp81, and Cys151 comprise the catalytic triad of the TEV protease (Nam et al., 2020). It was acquired from the DualMembrane Kit 3 (Thaminy et al., 2003).
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The DNA sequence encodes for a highly sequence-specific cysteine protease, a 27‐kDa catalytic domain of the polyprotein nuclear inclusion a (NIa) in tobacco etch virus (Nam et al., 2020). Its target substrate is the sequence ENLYFQS/G and it cleaves between Q and G/S (Nam et al., 2020), all the while requiring a Gly or Ser residue to be located in the vicinity of the cleavage site so as to process the substrate with reasonable efficiency (Kapust et al., 2002). Located at the interior of the domain, His46, Asp81, and Cys151 comprise the catalytic triad of the TEV protease (Nam et al., 2020). It was acquired from the DualMembrane Kit 3 (Thaminy et al., 2003).
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==References==
 
==References==
 
*Kapust, R. B., Tözsér, J., Copeland, T. D., & Waugh, D. S. (2002). The P1′ specificity of tobacco etch virus protease. Biochemical and Biophysical Research Communications, 294(5), 949–955. https://doi.org/https://doi.org/10.1016/S0006-291X(02)00574-0
 
*Kapust, R. B., Tözsér, J., Copeland, T. D., & Waugh, D. S. (2002). The P1′ specificity of tobacco etch virus protease. Biochemical and Biophysical Research Communications, 294(5), 949–955. https://doi.org/https://doi.org/10.1016/S0006-291X(02)00574-0
 
*Nam, H., Hwang, B. J., Choi, D., Shin, S., & Choi, M. (2020). Tobacco etch virus (TEV) protease with multiple mutations to improve solubility and reduce self‐cleavage exhibits enhanced enzymatic activity. FEBS Open Bio, 10(4), 619. https://doi.org/10.1002/2211-5463.12828
 
*Nam, H., Hwang, B. J., Choi, D., Shin, S., & Choi, M. (2020). Tobacco etch virus (TEV) protease with multiple mutations to improve solubility and reduce self‐cleavage exhibits enhanced enzymatic activity. FEBS Open Bio, 10(4), 619. https://doi.org/10.1002/2211-5463.12828
 
*Thaminy, S., Auerbach, D., Arnoldo, A., & Stagljar, I. (2003). Identification of Novel ErbB3-Interacting Factors Using the  Split-Ubiquitin Membrane Yeast Two-Hybrid System. Genome Research, 13(7), 1744. https://doi.org/10.1101/GR.1276503
 
*Thaminy, S., Auerbach, D., Arnoldo, A., & Stagljar, I. (2003). Identification of Novel ErbB3-Interacting Factors Using the  Split-Ubiquitin Membrane Yeast Two-Hybrid System. Genome Research, 13(7), 1744. https://doi.org/10.1101/GR.1276503

Latest revision as of 04:42, 21 October 2021

Usage and Biology

The DNA sequence encodes for a highly sequence-specific cysteine protease, a 27‐kDa catalytic domain of the polyprotein nuclear inclusion a (NIa) in tobacco etch virus (Nam et al., 2020). Its target substrate is the sequence ENLYFQS/G and it cleaves between Q and G/S (Nam et al., 2020), all the while requiring a Gly or Ser residue to be located in the vicinity of the cleavage site so as to process the substrate with reasonable efficiency (Kapust et al., 2002). Located at the interior of the domain, His46, Asp81, and Cys151 comprise the catalytic triad of the TEV protease (Nam et al., 2020). It was acquired from the DualMembrane Kit 3 (Thaminy et al., 2003).

References

  • Kapust, R. B., Tözsér, J., Copeland, T. D., & Waugh, D. S. (2002). The P1′ specificity of tobacco etch virus protease. Biochemical and Biophysical Research Communications, 294(5), 949–955. https://doi.org/https://doi.org/10.1016/S0006-291X(02)00574-0
  • Nam, H., Hwang, B. J., Choi, D., Shin, S., & Choi, M. (2020). Tobacco etch virus (TEV) protease with multiple mutations to improve solubility and reduce self‐cleavage exhibits enhanced enzymatic activity. FEBS Open Bio, 10(4), 619. https://doi.org/10.1002/2211-5463.12828
  • Thaminy, S., Auerbach, D., Arnoldo, A., & Stagljar, I. (2003). Identification of Novel ErbB3-Interacting Factors Using the  Split-Ubiquitin Membrane Yeast Two-Hybrid System. Genome Research, 13(7), 1744. https://doi.org/10.1101/GR.1276503