Difference between revisions of "Part:BBa K1800002"
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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. | 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. | ||
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| + | <h3 style="margin-left: 0cm; text-indent: 0cm;"><a | ||
| + | name="_Toc275885922"></a><a name="_Toc275817881"><span | ||
| + | lang="EN-US">References</span></a><br> | ||
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| + | <p style="margin-left: 24pt; text-indent: -24pt;"><span | ||
| + | lang="EN-US">Natsoulis, G., United States Patent 5,622,856 (1997).</span></p> | ||
| + | <p style="margin-left: 24pt; text-indent: -24pt;"><span | ||
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<!-- Add more about the biology of this part here | <!-- Add more about the biology of this part here | ||
===Usage and Biology=== | ===Usage and Biology=== | ||
Revision as of 09:05, 29 October 2016
Horseradish Peroxidase
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.
<a
name="_Toc275885922"></a><a name="_Toc275817881">References</a>
Natsoulis, G., United States Patent 5,622,856 (1997).
Sequence and Features
Illegal XhoI site found at 480