Team:Berkeley/Parts

From 2013.igem.org

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<div class = "heading"><a name="Undergraduates">Parts Submitted to Registry</a></div>
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<div class = "heading"><a name="Undergraduates">Characterized Parts Submitted to Registry</a></div>
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                     <a target="_new" href="http://parts.igem.org/Part:BBa_K1131004">BBa_K1131004</a></td>
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                     <a target="_new" href="http://parts.igem.org/Part:BBa_K1131006">BBa_K1131006</a></td>
                   <td class = "names" style="text-align: left;"> <i> S. antibioticus </i> oleD Glucosyltransferase</td>
                   <td class = "names" style="text-align: left;"> <i> S. antibioticus </i> oleD Glucosyltransferase</td>
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                     <a target="_new" href="http://parts.igem.org/Part:BBa_K1131005">BBa_K1131005</a></td>
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                     <a target="_new" href="http://parts.igem.org/Part:BBa_K1131007">BBa_K1131007</a></td>
                   <td class = "names" style="text-align: left;"> <i> S. antibioticus </i> oleD 'ASP'-mutated Glucosyltransferase</td>
                   <td class = "names" style="text-align: left;"> <i> S. antibioticus </i> oleD 'ASP'-mutated Glucosyltransferase</td>
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<td style="text-align: left;">This is the mutant version of oleD glucosyltransferase part BBa_K1131004. Mutations identified by Thorston et. al. 2010 at P67T, S132F, and A242V were introduced to oleD generating the 'ASP' version of the protein. OleD 'ASP' is reported to have a much larger set of substrates it can glucosylate compared to the non mutated oleD.</td>
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<td style="text-align: left;">This is the mutant version of oleD glucosyltransferase part BBa_K1131006. Mutations identified by Thorson et. al. 2010 at P67T, S132F, and A242V were introduced to oleD generating the 'ASP' version of the protein. OleD 'ASP' is reported to have a much larger set of substrates it can glucosylate compared to the non mutated oleD.</td>
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Revision as of 22:47, 27 October 2013

Characterized Parts Submitted to Registry
BBa_K1131000 M. aminisulfidivorans FMO
This Flavin-containing monooxygenase (FMO) from M. aminisulfidivorans can be expressed in many strains of E. coli to produce indigo dye. In the presence of indole and oxygen, FMO can catalyze the addition of a hydroxyl group to indole generating the intermediate indoxyl. Indoxyl then naturally oxidizes to generate indigo which, due to its hydrophobicity, crashes out of solution. The part submitted is the ORF of FMO only.
BBa_K1131001 M. aminisulfidivorans mutant FMO
As a corollary to the FMO from M. aminisulfidivorans submitted, this part has three specific mutations at F179A, G181A, F189A that eradicate FMO activity. This specific FMO converted indole to indoxyl which then oxidized to indigo, the well known dye. With these mutations, indigo was not observed, and was used as a control in several studies. This part contains the ORF of the mutated FMO only.
BBa_K1131002 B. circulans B-glucosidase
The beta-Glucosidase from B. Circulans cleaves the glycosidic linkage of our substrate of interest, indican, via hydrolysis. This enzyme is expressed well in E. coli and shows activity with a variety of substrates including indican and X-Gal, offering a potential alternative in the latter case to the lacZ beta-galactosidase in a blue-white screen. This sequence corresponds to the ORF of the enzyme only.
BBa_K1131006 S. antibioticus oleD Glucosyltransferase
This oleandomycin glucosyltransferase was found to glucosylate kaempferol generating kaempferol glucoside. It is known to highly promiscuous in substrate specificity and glucosylates a variety of phenolics and anthrocyanins. The sequence shown here corresponds to that of UniProt ID Q53685, and encodes the ORF only.
BBa_K1131007 S. antibioticus oleD 'ASP'-mutated Glucosyltransferase
This is the mutant version of oleD glucosyltransferase part BBa_K1131006. Mutations identified by Thorson et. al. 2010 at P67T, S132F, and A242V were introduced to oleD generating the 'ASP' version of the protein. OleD 'ASP' is reported to have a much larger set of substrates it can glucosylate compared to the non mutated oleD.

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