Difference between revisions of "Part:BBa K3192017"
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[[File:T--Virginia--styCfigure.png|500px|thumb|left|Pathway of styrene degradation into phenylacetic acid. Obtained from Substrate specificity and reaction mechanism of recombinant styrene oxide isomerase from Pseudomonas putida S12<sup>1</sup>]] | [[File:T--Virginia--styCfigure.png|500px|thumb|left|Pathway of styrene degradation into phenylacetic acid. Obtained from Substrate specificity and reaction mechanism of recombinant styrene oxide isomerase from Pseudomonas putida S12<sup>1</sup>]] | ||
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<h3>References:</h3> | <h3>References:</h3> | ||
<p> 1) Sazinsky, M., Morrison, E., Kantz, A. & Gassner, G. Structure of the Styrene Monooxygenase Flavin Reductase (SMOB) from Pseudomonas putida S12. (2013). doi:10.2210/pdb4f07/pdb </p> | <p> 1) Sazinsky, M., Morrison, E., Kantz, A. & Gassner, G. Structure of the Styrene Monooxygenase Flavin Reductase (SMOB) from Pseudomonas putida S12. (2013). doi:10.2210/pdb4f07/pdb </p> |
Latest revision as of 22:21, 21 October 2019
styC
This part contains the sequence for the styC gene, which codes for Styrene oxide isomerase. This is a catalytic enzyme that metabolizes styrene oxide into phenylacetaldehyde. This gene originated from Pseudomonas putida S12, an organism found to be capable of metabolizing styrene. This is done through the opening of the epoxide and subsequent oxidation to yield an aldehyde group. This is the second step to the metabolism of styrene to phenylacetic acid in the styABCDE cluster.1
References:
1) Sazinsky, M., Morrison, E., Kantz, A. & Gassner, G. Structure of the Styrene Monooxygenase Flavin Reductase (SMOB) from Pseudomonas putida S12. (2013). doi:10.2210/pdb4f07/pdb
Sequence and Features
Assembly Compatibility:
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]