Difference between revisions of "Part:BBa K4879000"
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Plant acyl-ACP thioesterases are enzymes that play a crucial role in various metabolic processes in plants. They function by catalyzing the hydrolysis of thioester bonds specifically between an acyl group and an acyl carrier protein (ACP). This hydrolysis reaction results in the release of the acyl group from ACP, producing a free fatty acid. Thus, acyl-ACP thioesterases are pivotal in regulating the chain length of fatty acids in de novo fatty acid biosynthesis by cleaving them from ACP. | Plant acyl-ACP thioesterases are enzymes that play a crucial role in various metabolic processes in plants. They function by catalyzing the hydrolysis of thioester bonds specifically between an acyl group and an acyl carrier protein (ACP). This hydrolysis reaction results in the release of the acyl group from ACP, producing a free fatty acid. Thus, acyl-ACP thioesterases are pivotal in regulating the chain length of fatty acids in de novo fatty acid biosynthesis by cleaving them from ACP. | ||
− | + | This regulatory function of thioesterases in fatty acids' chain lengths significantly affects the free fatty acid as well as the triglyceride compositions in plant seed oils, affecting their value in terms of nutrition or biofuel potential. This has made thioesterases a focus in industries, with research aimed at manipulating them to give favourable lipid compositions for further processing. | |
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+ | In <i>Jatropha curcas</i>, fatty acyl-ACP thioesterase A primarily acts on linoleoyl-ACP and oleoyl-ACP to give linoleic acid (C 18:2) and oleic acid (C 18:1). The ability of this enzyme to give unsaturated fatty acids–a feedstock much desired for the production of aviation biofuel– at a rate similar to that of its original organism was one of the reasons we had for its expression in our chassis <i>Yarrowia lipolytica</i>. | ||
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+ | <html><img src="https://static.igem.wiki/teams/4879/wiki/bba-k4879000-jcfata.png"alt ="Protein Structure of JcFATA"width="250"height="250"></html> | ||
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+ | The protein structure of JcFATA, as predicted by [https://alphafold.ebi.ac.uk/entry/A0A0M4BUI7 Alphafold] | ||
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+ | ===Design=== | ||
+ | The transcriptional unit for JcFATA [https://parts.igem.org/Part:BBa_K4879006 (BBa_K4879006)] is designed with the coding sequence flanked by the TEF1 promoter [https://parts.igem.org/Part:BBa_K3629001 (BBa_K3629001)] upstream and the XPR2 terminator [https://parts.igem.org/Part:BBa_K3629004 (BBa_K3629004)] downstream. | ||
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− | <!-- Uncomment this to enable Functional Parameter display | + | <!-- Uncomment this to enable Functional Parameter display |
===Functional Parameters=== | ===Functional Parameters=== | ||
<partinfo>BBa_K4879000 parameters</partinfo> | <partinfo>BBa_K4879000 parameters</partinfo> |
Latest revision as of 11:33, 11 October 2023
JcFATA
The fatty acyl-ACP thioesterase A, from the plant Jatropha curcas. [1]
-
Usage and Biology
Plant acyl-ACP thioesterases are enzymes that play a crucial role in various metabolic processes in plants. They function by catalyzing the hydrolysis of thioester bonds specifically between an acyl group and an acyl carrier protein (ACP). This hydrolysis reaction results in the release of the acyl group from ACP, producing a free fatty acid. Thus, acyl-ACP thioesterases are pivotal in regulating the chain length of fatty acids in de novo fatty acid biosynthesis by cleaving them from ACP.
This regulatory function of thioesterases in fatty acids' chain lengths significantly affects the free fatty acid as well as the triglyceride compositions in plant seed oils, affecting their value in terms of nutrition or biofuel potential. This has made thioesterases a focus in industries, with research aimed at manipulating them to give favourable lipid compositions for further processing.
In Jatropha curcas, fatty acyl-ACP thioesterase A primarily acts on linoleoyl-ACP and oleoyl-ACP to give linoleic acid (C 18:2) and oleic acid (C 18:1). The ability of this enzyme to give unsaturated fatty acids–a feedstock much desired for the production of aviation biofuel– at a rate similar to that of its original organism was one of the reasons we had for its expression in our chassis Yarrowia lipolytica.
The protein structure of JcFATA, as predicted by Alphafold
Design
The transcriptional unit for JcFATA (BBa_K4879006) is designed with the coding sequence flanked by the TEF1 promoter (BBa_K3629001) upstream and the XPR2 terminator (BBa_K3629004) downstream.
Sequence and Features
- 10INCOMPATIBLE WITH RFC[10]Illegal PstI site found at 331
Illegal PstI site found at 938 - 12INCOMPATIBLE WITH RFC[12]Illegal PstI site found at 331
Illegal PstI site found at 938 - 21INCOMPATIBLE WITH RFC[21]Illegal BglII site found at 780
- 23INCOMPATIBLE WITH RFC[23]Illegal PstI site found at 331
Illegal PstI site found at 938 - 25INCOMPATIBLE WITH RFC[25]Illegal PstI site found at 331
Illegal PstI site found at 938 - 1000COMPATIBLE WITH RFC[1000]
References
1. Liu, Y.; Han, J.; Li, Z.; Jiang, Z.; Luo, L.; Zhang, Y.; Chen, M.; Yang, Y.; Liu, Z. Heterologous Expression of Jatropha curcas Fatty Acyl-ACP Thioesterase A (JcFATA) and B (JcFATB) Affects Fatty Acid Accumulation and Promotes Plant Growth and Development in Arabidopsis. Int. J. Mol. Sci. 2022, 23, 4209. https://doi.org/10.3390/ijms23084209