Difference between revisions of "Part:BBa K5255003"
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| − | <p>Basic parts <b>MLacs1 (<a href="https://parts.igem.org/Part:BBa_K5255003">BBa_K5255003</a>) is a mutant of wild-type Lacs1. Long-chain acyl-coenzyme A (CoA) synthetases (LACSs) activate free fatty acids to acyl-CoA thioesters and play critical roles in fatty acid metabolism. Lacs1 can use DHA, CoA and ATP as substrates to catalyze the synthesis of DHA-CoA, which is the precursor of DHA-PC. MLacs1 sequence was obtained by mutating the active site of its protein, and MLacs1 was introduced into <i>Saccharomyces cerevisiae INVSC1</i> and <i>E.coli BL21 (DE3)</i>. The activity of the enzyme expressed by MLacs1 was verified by <i>Escherichia coli</i> and the product catalyzed by MLacs1, DHA-CoA, was verified by Saccharomyces cerevisiae</i> to ensure the synthesis of DHA-PC and the possibility of subsequent synthesis of DHA-PC. | + | <p>Basic parts <b>MLacs1 (<a href="https://parts.igem.org/Part:BBa_K5255003">BBa_K5255003</a>)</b> is a mutant of wild-type Lacs1. Long-chain acyl-coenzyme A (CoA) synthetases (LACSs) activate free fatty acids to acyl-CoA thioesters and play critical roles in fatty acid metabolism. Lacs1 can use DHA, CoA and ATP as substrates to catalyze the synthesis of DHA-CoA, which is the precursor of DHA-PC. MLacs1 sequence was obtained by mutating the active site of its protein, and MLacs1 was introduced into <i>Saccharomyces cerevisiae INVSC1</i> and <i>E.coli BL21 (DE3)</i>. The activity of the enzyme expressed by MLacs1 was verified by <i>Escherichia coli</i> and the product catalyzed by MLacs1, DHA-CoA, was verified by Saccharomyces cerevisiae</i> to ensure the synthesis of DHA-PC and the possibility of subsequent synthesis of DHA-PC. |
Revision as of 05:39, 30 September 2024
MLACS1
Basic parts MLacs1 (BBa_K5255003) is a mutant of wild-type Lacs1. Long-chain acyl-coenzyme A (CoA) synthetases (LACSs) activate free fatty acids to acyl-CoA thioesters and play critical roles in fatty acid metabolism. Lacs1 can use DHA, CoA and ATP as substrates to catalyze the synthesis of DHA-CoA, which is the precursor of DHA-PC. MLacs1 sequence was obtained by mutating the active site of its protein, and MLacs1 was introduced into Saccharomyces cerevisiae INVSC1 and E.coli BL21 (DE3). The activity of the enzyme expressed by MLacs1 was verified by Escherichia coli and the product catalyzed by MLacs1, DHA-CoA, was verified by Saccharomyces cerevisiae to ensure the synthesis of DHA-PC and the possibility of subsequent synthesis of DHA-PC.