Team:Berkeley/Parts

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                <li id="TitleID"> <a id="TitleID" href="https://2013.igem.org/Team:Berkeley/Parts">Parts</a>
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                <li><a href="#1">FMO </a>
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                </li>
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                <li><a href="#2">Mutant FMO</a>
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                <li><a href="#3">B-GLU</a>
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                <li><a href="#4">oleD </a>
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                <li><a href="#5">oleD 'ASP'</a>
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<div class = "heading-large"><a name="Undergraduates">Characterized Parts Submitted to Registry</a></div>
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This is a template page. READ THESE INSTRUCTIONS.
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                    <a target="_new" href="http://parts.igem.org/Part:BBa_K1131000">BBa_K1131000  <i>M. aminisulfidivorans </i> FMO</a>
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                <p>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.</p>
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You <strong>MUST</strong> have all of the pages listed in the menu below with the names specified.   PLEASE keep all of your pages within your teams namespace.
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                      <a target="_new" href="http://parts.igem.org/Part:BBa_K1131001">BBa_K1131001  <i>M. aminisulfidivorans </i> Mutant FMO</a>
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                <p>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.</p>
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                      <a target="_new" href="http://parts.igem.org/Part:BBa_K1131002">BBa_K1131002 <i>B. circulans</i> B-glucosidase</a>
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                    </div>
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                <p>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.</p>
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                      <a target="_new" href="http://parts.igem.org/Part:BBa_K1131006">BBa_K1131006<i> S. antibioticus </i> oleD Glucosyltransferase</a>
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                <p>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.</p>
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                      <a target="_new" href="http://parts.igem.org/Part:BBa_K1131007">BBa_K1131007<i> S. antibioticus </i> oleD 'ASP'-mutated Glucosyltransferase</a>
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                <p>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.</p>
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{| style="color:#1b2c8a;background-color:#0c6;" cellpadding="3" cellspacing="1" border="1" bordercolor="#fff" width="62%" align="center"
 
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!align="center"|[[Team:Berkeley|Home]]
 
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!align="center"|[[Team:Berkeley/Team|Team]]
 
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!align="center"|[https://igem.org/Team.cgi?year=2013&team_name=Berkeley Official Team Profile]
 
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!align="center"|[[Team:Berkeley/Project|Project]]
 
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!align="center"|[[Team:Berkeley/Parts|Parts Submitted to the Registry]]
 
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!align="center"|[[Team:Berkeley/Modeling|Modeling]]
 
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!align="center"|[[Team:Berkeley/Notebook|Notebook]]
 
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!align="center"|[[Team:Berkeley/Safety|Safety]]
 
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!align="center"|[[Team:Berkeley/Attributions|Attributions]]
 
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An important aspect of the iGEM competition is the use and creation of standard  biological parts. Each team will make new parts during iGEM and will place them in the [http://partsregistry.org Registry of Standard Biological Parts]. The iGEM software provides an easy way to present the parts your team has created . The "groupparts" tag will generate a table with all of the parts that your team adds to your team sandbox.  Note that if you want to document a part you need to document it on the [http://partsregistry.org Registry], not on your team wiki.
 
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Remember that the goal of proper part documentation is to describe and define a part such that it can be used without a need to refer to the primary literature. The next iGEM team should be able to read your documentation and be able to use the part successfully. Also, you should provide proper references to acknowledge previous authors and to provide for  users who wish to know more.
 
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<groupparts>iGEM013 Berkeley</groupparts>
 

Latest revision as of 03:27, 29 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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