Difference between revisions of "Part:BBa K3729000"
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<b>Construct design:</b>We optimized the DNA sequence for expression in E. coli and flanked the open reading frame with an upstream strong promoter, a strong ribosome binding site (RBS), and a double terminator. This design of construct would lead to overexpression of the DNA sequence, further upregulating the production of butyryl- CoA dehydrogenase. Our composite part is synthesized by IDT.
 
<b>Construct design:</b>We optimized the DNA sequence for expression in E. coli and flanked the open reading frame with an upstream strong promoter, a strong ribosome binding site (RBS), and a double terminator. This design of construct would lead to overexpression of the DNA sequence, further upregulating the production of butyryl- CoA dehydrogenase. Our composite part is synthesized by IDT.
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<span class='h3bb'>Sequence and Features</span>
 
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We optimized the DNA sequence for expression in E. coli and flanked the open reading frame with an upstream strong promoter, a strong ribosome binding site (RBS), and a double terminator. This design of construct would lead to overexpression of the DNA sequence, further upregulating the production of butyryl- CoA dehydrogenase. Our composite part is synthesized by IDT.
 
  
 
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Revision as of 17:46, 21 October 2021


BCD 1: (Acyl-coa Dehydrogenase)

Butyryl- CoA dehydrogenase catalyzes the rate-limiting step (Crotonyl-CoA to butyryl-CoA) of the acetyl-CoA butyrate synthesis pathway, further increasing the efficiency of bacteria’s butyrate production. We obtained the DNA sequence (BCD) encoded for butyryl-CoA-dehydrogenase from the genome of Faecalibacterium prausnitzii.

Construct design:We optimized the DNA sequence for expression in E. coli and flanked the open reading frame with an upstream strong promoter, a strong ribosome binding site (RBS), and a double terminator. This design of construct would lead to overexpression of the DNA sequence, further upregulating the production of butyryl- CoA dehydrogenase. Our composite part is synthesized by IDT.