Difference between revisions of "Part:BBa K4719004"
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<partinfo>BBa_K4719004 short</partinfo> | <partinfo>BBa_K4719004 short</partinfo> | ||
− | + | ==Introduction== | |
− | Vilnius Lithuania iGEM 2023 team's goal was to create | + | <b>Vilnius-Lithuania iGEM 2023</b> team's goal was to create <b> synthetic biology tools for <i>in vivo</i> alterations of <i>Komagataeibacter xylinus</i> bacterial cellulose polymer composition</b>. Firstly, we chose to produce a <b>cellulose-chitin copolymer</b> that would later be deacetylated, creating <b>bacterial cellulose-chitosan</b>. This polymer is an easily modifiable platform when compared to bacterial cellulose. The enhanced chemical reactivity of the bacterial cellulose-chitosan polymer allows for specific functionalizations in the biomedicine field, such as scaffold design. As a second approach, we designed <b>indigo-dyed cellulose</b> that could be used as a green chemistry way to apply cellulose in the textile industry. Lastly, we have achieved a of <b>bacterial cellulose and polyhydroxybutyrate (PHB) composite</b>, which is synthesized by <i>K. xylinus</i>. |
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− | Bacterial cellulose-chitin polymer was achieved by increasing the production of UDP-N-acetylglucosamine (UDP-GlcNAc), which can be recognized as a viable substrate for cellulose synthase and incorporated in bacterial cellulose polymer. We employed two strategies to produce this material. The first approach was to add N-acetylglucosamine into the growth medium [https://parts.igem.org/Part:BBa_K4719013 BBa_K4719013], and the second one was the production of N-acetylglucosamine by ''K. xylinus'' from | + | Bacterial cellulose-chitin polymer was achieved by increasing the production of UDP-N-acetylglucosamine (UDP-GlcNAc), which can be recognized as a viable substrate for cellulose synthase and incorporated in bacterial cellulose polymer. We employed two strategies to produce this material. The first approach was to add N-acetylglucosamine into the growth medium [https://parts.igem.org/Part:BBa_K4719013 BBa_K4719013], and the second one was the production of N-acetylglucosamine by ''K. xylinus'' from other sugars such as glucose, fructose, and saccharose in the growth medium [https://parts.igem.org/Part:BBa_K4719014 BBa_K4719014]. |
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===Usage and Biology=== | ===Usage and Biology=== | ||
− | GFA1 is glutamine-fructose-6-phosphate aminotransferase. This enzyme catalyzes the formation of glucosamine-6-phosphate and glutamate from fructose-6-phosphate and glutamine. This is a crucial step in our system, that produces bacterial cellulose-chitin polymer from simple sugars in the growth medium. GFA1 is used as a part in [https://parts.igem.org/Part:BBa_K4719014 BBa_K4719014]. | + | ''GFA1'' is glutamine-fructose-6-phosphate aminotransferase. The protein sequence is from ''Candida albicans''. This enzyme catalyzes the formation of glucosamine-6-phosphate and glutamate from fructose-6-phosphate and glutamine [https://parts.igem.org/Part:BBa_K4719004#References (1)]. This is a crucial step in our system, that produces bacterial cellulose-chitin polymer from simple sugars in the growth medium. ''GFA1'' is used as a part in [https://parts.igem.org/Part:BBa_K4719014 BBa_K4719014]. |
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<partinfo>BBa_K4719004 parameters</partinfo> | <partinfo>BBa_K4719004 parameters</partinfo> | ||
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+ | ===References=== | ||
+ | 1.Dummitt, B., Micka, W.S. and Chang, Y.-H. (2005) ‘Yeast Glutamine-fructose-6-phosphate Aminotransferase (Gfa1) Requires Methionine Aminopeptidase Activity for Proper Function’, Journal of Biological Chemistry, 280(14), pp. 14356–14360. doi:10.1074/jbc.m501059200. |
Latest revision as of 15:06, 12 October 2023
GFA1
Introduction
Vilnius-Lithuania iGEM 2023 team's goal was to create synthetic biology tools for in vivo alterations of Komagataeibacter xylinus bacterial cellulose polymer composition. Firstly, we chose to produce a cellulose-chitin copolymer that would later be deacetylated, creating bacterial cellulose-chitosan. This polymer is an easily modifiable platform when compared to bacterial cellulose. The enhanced chemical reactivity of the bacterial cellulose-chitosan polymer allows for specific functionalizations in the biomedicine field, such as scaffold design. As a second approach, we designed indigo-dyed cellulose that could be used as a green chemistry way to apply cellulose in the textile industry. Lastly, we have achieved a of bacterial cellulose and polyhydroxybutyrate (PHB) composite, which is synthesized by K. xylinus.
Bacterial cellulose-chitin polymer was achieved by increasing the production of UDP-N-acetylglucosamine (UDP-GlcNAc), which can be recognized as a viable substrate for cellulose synthase and incorporated in bacterial cellulose polymer. We employed two strategies to produce this material. The first approach was to add N-acetylglucosamine into the growth medium BBa_K4719013, and the second one was the production of N-acetylglucosamine by K. xylinus from other sugars such as glucose, fructose, and saccharose in the growth medium BBa_K4719014.
Usage and Biology
GFA1 is glutamine-fructose-6-phosphate aminotransferase. The protein sequence is from Candida albicans. This enzyme catalyzes the formation of glucosamine-6-phosphate and glutamate from fructose-6-phosphate and glutamine (1). This is a crucial step in our system, that produces bacterial cellulose-chitin polymer from simple sugars in the growth medium. GFA1 is used as a part in BBa_K4719014.
Sequence and Features
- 10INCOMPATIBLE WITH RFC[10]Illegal EcoRI site found at 361
Illegal EcoRI site found at 859
Illegal XbaI site found at 1459 - 12INCOMPATIBLE WITH RFC[12]Illegal EcoRI site found at 361
Illegal EcoRI site found at 859 - 21INCOMPATIBLE WITH RFC[21]Illegal EcoRI site found at 361
Illegal EcoRI site found at 859
Illegal BglII site found at 1318 - 23INCOMPATIBLE WITH RFC[23]Illegal EcoRI site found at 361
Illegal EcoRI site found at 859
Illegal XbaI site found at 1459 - 25INCOMPATIBLE WITH RFC[25]Illegal EcoRI site found at 361
Illegal EcoRI site found at 859
Illegal XbaI site found at 1459 - 1000COMPATIBLE WITH RFC[1000]
References
1.Dummitt, B., Micka, W.S. and Chang, Y.-H. (2005) ‘Yeast Glutamine-fructose-6-phosphate Aminotransferase (Gfa1) Requires Methionine Aminopeptidase Activity for Proper Function’, Journal of Biological Chemistry, 280(14), pp. 14356–14360. doi:10.1074/jbc.m501059200.