Difference between revisions of "Part:BBa K4719003"
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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 simple sugars such as glucose, fructose, and saccharose in the growth medium [https://parts.igem.org/Part:BBa_K4719014 BBa_K4719014]. | + | 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 the 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 simple 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=== | ||
| − | UAP1 is UDP-GlcNAc pyrophosphorylase. This protein is involved in UDP-GlcNAc synthesis by converting N-acetylglucosamine-6-phosphate into UDP-GlcNAc. The cellulose synthase can recognize both UDP-N-acetylglucosamine and UDP-glucose as substrates resulting in the formation of bacterial cellulose-chitin polymer. This part is used in [https://parts.igem.org/Part:BBa_K4719013 BBa_K4719013] and [https://parts.igem.org/Part:BBa_K4719014 BBa_K4719014]. | + | ''UAP1'' is UDP-GlcNAc pyrophosphorylase. This protein is involved in UDP-GlcNAc synthesis by converting N-acetylglucosamine-6-phosphate into UDP-GlcNAc. The cellulose synthase can recognize both UDP-N-acetylglucosamine and UDP-glucose as substrates resulting in the formation of bacterial cellulose-chitin polymer. This part is used in [https://parts.igem.org/Part:BBa_K4719013 BBa_K4719013] and [https://parts.igem.org/Part:BBa_K4719014 BBa_K4719014]. |
Revision as of 16:53, 16 September 2023
UAP1
Introduction
Vilnius Lithuania iGEM 2023 team's goal was to create a universal synthetic biology system in Komagataeibacter xylinus for in vivo bacterial cellulose polymer composition modification. Firstly, we chose to produce a cellulose-chitin polymer 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 bacterial cellulose-chitosan polymer allows for specific functionalizations in the biomedicine field, such as scaffold design.
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 the 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 simple sugars such as glucose, fructose, and saccharose in the growth medium BBa_K4719014.
Usage and Biology
UAP1 is UDP-GlcNAc pyrophosphorylase. This protein is involved in UDP-GlcNAc synthesis by converting N-acetylglucosamine-6-phosphate into UDP-GlcNAc. The cellulose synthase can recognize both UDP-N-acetylglucosamine and UDP-glucose as substrates resulting in the formation of bacterial cellulose-chitin polymer. This part is used in BBa_K4719013 and BBa_K4719014.
Sequence and Features
- 10INCOMPATIBLE WITH RFC[10]Illegal EcoRI site found at 573
Illegal EcoRI site found at 735
Illegal SpeI site found at 511
Illegal SpeI site found at 1399 - 12INCOMPATIBLE WITH RFC[12]Illegal EcoRI site found at 573
Illegal EcoRI site found at 735
Illegal SpeI site found at 511
Illegal SpeI site found at 1399 - 21INCOMPATIBLE WITH RFC[21]Illegal EcoRI site found at 573
Illegal EcoRI site found at 735 - 23INCOMPATIBLE WITH RFC[23]Illegal EcoRI site found at 573
Illegal EcoRI site found at 735
Illegal SpeI site found at 511
Illegal SpeI site found at 1399 - 25INCOMPATIBLE WITH RFC[25]Illegal EcoRI site found at 573
Illegal EcoRI site found at 735
Illegal SpeI site found at 511
Illegal SpeI site found at 1399 - 1000COMPATIBLE WITH RFC[1000]