Difference between revisions of "Part:BBa K1800002"

Class III plant peroxidases catalyze various oxidative reactions in which electrons are transferred to peroxide species, and substrate molecules are oxidized (Krainer, 2015). Peroxidases can be found in most plants and have been proposed to influence various functions related to the degradation of indole-3-acetic acid (IAA) (Lamport, 1986) and cell wall elasticity (Goldberg et al., 1986). Horseradish peroxidases is a peroxidase that has been used exhaustively as a reporter enzyme in diagnostics and histochemistry. In our lab, we designed an HRP part in accordance to RFC 10. HRP in our experiment will serve as a proof of concept for the Agrobacterium tumefaciens mediated transformation of tobacco plants with CBDA synthase. HRP will be inserted into the pORE vector for transformation of A. tumefaciens The A. tumafeciens will then be used to transform tobacco plants. The tobacco will then produce hairy roots suspended in the culture that contains the HRP part.

References

Krainer, F. W., & Glieder, A. (2015). An updated view on horseradish peroxidases: recombinant production and biotechnological applications. Applied microbiology and biotechnology, 99(4), 1611-1625.

Lamport, D.T.A. 1986. Roles for peroxidase in cell wall genesis, p. 199-208. In: H. Greppin, C. Penel, and T. Gasper (eds.). Molecular and physiological aspects of plant peroxidase. Univ. of Geneva Press, Switzerland.

Lamport, D.T.A. 1986. Roles for peroxidase in cell wall genesis, p. 199-208. In: H. Greppin, C. Penel, and T. Gasper (eds.). Goldberg, R., A. Imberty, M. Liberman, and R. Prat. 1986. Relationships between peroxidase activities and cell wall plasticity, p. 209-220. In: H. Greppin, C. Penel, and T. Gasper (eds.). Molecular and physiological aspects of plant peroxidase. Univ. of Geneva Press, Switzerland.

Sequence and Features