Team:WLC-Milwaukee/Parts
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+ | <SPAN style='font-size: 150%; font-weight: bold;color: #00582A'>endo-1,4-beta-xylanase xynA from Bacillus Subtilis Subtilis 168 </SPAN> | ||
+ | </p><p>The endo-1,4-beta-xylanase gene xynA cleaves xylan polysaccharide chains to form shorter xylan chains. This gene has been isolated from the bacterium Bacillus subtilis subtilis 168. | ||
+ | </p><p>Usage and Biology | ||
+ | </p> | ||
+ | Xylan is a molecule similar to cellulose, and after cellulose the most abundant biomass material on earth. It is a major structural component of plant cell walls. Furthermore, xylan crosslinks with cellulose and other cell wall components, inhibiting access of cellulases (1). Xylose is the sugar monomer of xylan as glucose is to cellulose. Xylose cannot be used in the human body as a source of energy. Endo-1,4-beta-xylanase (xynA) breaks the xylan chains into shorter chains, and may be stearically hindered by side chains (2). | ||
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+ | A beta-xylanase such as Endo-1,4-beta xylanase may be used to degrade xylan to facilitate cellulase activity. Another use may be in conjunction with an exo-xylanase to efficiently break down xylan into xylose monomers (a pentose sugar). | ||
+ | <p>Enzymatic Activity of Gene Product | ||
+ | </p> | ||
+ | As stated above, the function of the gene product is xylan degredation. The enzyme's catabolic activity results from endohydrolysis of 1,4-beta-D-xylosidic linkages in xylan molecules (4). | ||
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+ | <p>(1) <a href="http://newscenter.lbl.gov/feature-stories/2012/11/12/a-better-route-to-xylan/" class="external free" rel="nofollow">http://newscenter.lbl.gov/feature-stories/2012/11/12/a-better-route-to-xylan/</a> | ||
+ | (2) <a href="http://www.nutrex.be/sites/default/files/wysiwyg-upload/nutrase-xyla-nsp-enzyme.pdf" class="external free" rel="nofollow">http://www.nutrex.be/sites/default/files/wysiwyg-upload/nutrase-xyla-nsp-enzyme.pdf</a> | ||
+ | (3) <a href="http://subtiwiki.uni-goettingen.de/wiki/index.php/XynA" class="external free" rel="nofollow">http://subtiwiki.uni-goettingen.de/wiki/index.php/XynA</a> | ||
+ | (4) <a href="http://www.uniprot.org/uniprot/P18429" class="external free" rel="nofollow">http://www.uniprot.org/uniprot/P18429</a> | ||
+ | <img src="https://static.igem.org/mediawiki/2013/e/eb/WLC-XynA.png"> | ||
+ | </tr></td> | ||
+ | <tr><td> | ||
<p> | <p> | ||
<span style="font-size: 150%; font-weight: bold; color: #00582A">endo-beta-1,3-1,4 glucanase (BglS) from Bacillus Subtilis 168</span> | <span style="font-size: 150%; font-weight: bold; color: #00582A">endo-beta-1,3-1,4 glucanase (BglS) from Bacillus Subtilis 168</span> |
Revision as of 22:39, 27 September 2013
Submitted Parts
<groupparts>iGEM013 WLC-Milwaukee</groupparts>
endo-1,4-beta-xylanase xynA from Bacillus Subtilis Subtilis 168
The endo-1,4-beta-xylanase gene xynA cleaves xylan polysaccharide chains to form shorter xylan chains. This gene has been isolated from the bacterium Bacillus subtilis subtilis 168. Usage and Biology Xylan is a molecule similar to cellulose, and after cellulose the most abundant biomass material on earth. It is a major structural component of plant cell walls. Furthermore, xylan crosslinks with cellulose and other cell wall components, inhibiting access of cellulases (1). Xylose is the sugar monomer of xylan as glucose is to cellulose. Xylose cannot be used in the human body as a source of energy. Endo-1,4-beta-xylanase (xynA) breaks the xylan chains into shorter chains, and may be stearically hindered by side chains (2). A beta-xylanase such as Endo-1,4-beta xylanase may be used to degrade xylan to facilitate cellulase activity. Another use may be in conjunction with an exo-xylanase to efficiently break down xylan into xylose monomers (a pentose sugar).Enzymatic Activity of Gene Product As stated above, the function of the gene product is xylan degredation. The enzyme's catabolic activity results from endohydrolysis of 1,4-beta-D-xylosidic linkages in xylan molecules (4).(1) http://newscenter.lbl.gov/feature-stories/2012/11/12/a-better-route-to-xylan/ (2) http://www.nutrex.be/sites/default/files/wysiwyg-upload/nutrase-xyla-nsp-enzyme.pdf (3) http://subtiwiki.uni-goettingen.de/wiki/index.php/XynA (4) http://www.uniprot.org/uniprot/P18429 |
endo-beta-1,3-1,4 glucanase (BglS) from Bacillus Subtilis 168 BglS This gene encodes an endo-beta-1,3-1,4-glucanase (bglS), which is from the bacterium Bacillus subtilis subtilis 168. The enzyme will hydrolyze and thereby cleave internal 1,4 linkages adjacent to 1,3 linkages. BglS Usage and Biology The substrates vulnerable to the bglS encoded enzyme are mixed linked beta-glucans. These glucans would have 1,3 and 1,4 beta linkages within the polysaccharide linking together the glucose monomers. Examples of these glucans can be found in oats, maize, and barley. (1) http://mic.sgmjournals.org/content/141/2/281.long (2) http://onlinelibrary.wiley.com/doi/10.1002/j.2050-0416.1984.tb04259.x/pdf |
beta-galacturonidase (YesZ) from Bacillus Subtilis 168
yesZ The enzyme acts on the terminal end of side chains of Rhamnogalacturonan I Pectin, releasing the free galactose. This gene has been isolated from the bacterium Bacillus subtilis subtilis 168. The enzyme yesZ has beta-galactosidase (beta-galacturonidase) activity, cleaving (1→4)-β-D-galactans to produce single galactose molecules from RG I Pectin. Usage and Biology Pectin is a component of the primary cell wall of plants. As galactose can be metabolized by the human body and by animals, it is an alternative to the usual target of nutrition/energy boosts in biotechnology, glucose. (1) http://www.ncbi.nlm.nih.gov/pubmed/17449691 (2) http://subtiwiki.uni-goettingen.de/wiki/index.php/YesZ (3) http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1694227/ (4) http://aem.asm.org/content/73/12/3803 (5) http://www.tandfonline.com/doi/full/10.1080/15583724.2011.615962#tabModule
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Strong pBAD promoter BBa_K206000 attached to SecI pump BBa_K215104
These are the three essential parts prtD, prtE, prtF, that make up the Type I secretion system from Erwinia chrysanthemi.This part is made of 3 genes: prtD, prtE, and prtF, that constitute a type I Erwinia chrysanthemi secretion system. The Pump is expressed from a strong constitutive promoter, BBa_k206000, and has the translational terminator BBa_B0014. In pSB1C3. Used to secrete proteins containing prtB C-terminal tag. The prtB C-terminal tag is built into the protein generator [BBa_K215002]. Any protein of interest can be inserted into the protein generator and then secreted when used in conjunction with this secretion system. For full characterization data on this part, please see the University of Washington 2009 iGEM project page and Wisconsin Lutheran College 2013 iGEM project page.
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BBa_K1175028 pBAD Promoter and SecI pump attached to Composite norvirus antibody BBa_K875004
These are the three essential parts prtD, prtE, prtF, that make up the Type I secretion system from Erwinia chrysanthemi.This part is made of 3 genes: prtD, prtE, and prtF, that constitute a type I Erwinia chrysanthemi secretion system. The Pump is expressed from a strong constitutive promoter, BBa_k206000, and has the translational terminator BBa_B0014. In pSB1C3. Used to secrete proteins containing prtB C-terminal tag. The prtB C-terminal tag is built into the protein generator [BBa_K215002]. Any protein of interest can be inserted into the protein generator and then secreted when used in conjunction with this secretion system. This construct is designed for the expression of an already descibed engeneered antinorovirus (NoV) monoclonal antibody (mAb 54.6) in fusion with LPP-OmpA. The antibody is expressed in a single chain fragment variable (scFv) format containing light (VL) and heavy (VH) variable domains separeted by a flexible peptide linker. It has already been reported that the scFv 54.6 binds a native recombinant NoV particles (VLPs) and inhibits VLP interaction with cells. LPP-OmpA functions as a leader sequence and an anchor to display the scFv ot the bacterial surface.The construct consistes of T5 Lac Operator (Bba_K875002), ribosomal binding site, LPP-OmpA-scFv 54.6 antinorovirus, Histidine tag (6HIS), Terminator (B0015). The part combines a strongly expressed secretion pump with a antinoroviral antibody that is expressed in the outer-membrane can/will be combined with BBa_K1175012 A composite part formed between BBa_K206000 strong pBAD promoter, BBa_B0034 strong RBS, and BBa_K215001 a purification and secretion tag. For full characterization data on this part, please see the University of Washington 2009 iGEM project page, Team Trieste iGEM 2012 and, Wisconsin Lutheran College 2013 iGEM project page.
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BBa_K1175400 |