Panb1-α factor-4CL-AOX1 Terminator
Sequence and Features
- 10COMPATIBLE WITH RFC
- 12COMPATIBLE WITH RFC
- 21Illegal XhoI site found at 124
Illegal XhoI site found at 649
- 23COMPATIBLE WITH RFC
- 25COMPATIBLE WITH RFC
- 1000Illegal BsaI site found at 1483
Illegal BsaI.rc site found at 1618
This is a composite part for extracellular expression of 4-Coumarate:CoA Ligase. 4CL is expressed and participates in the production from ferulic acid to p-Coumaroyl-CoA. Panb1 is a constitutive promoter in yeast, which is expressed under anaerobic conditions, while under aerobic conditions, Panb1, as a repression target of ROX1, is inhibited. When Panb1 initiates the expression, the signal peptide, α-factor, is used to express 4CL outside of the cell.
Usage and Biology
In the curcumin biosynthesis pathway, 4CL is located in the upstream of the metabolic pathway and plays a key role in the synthesis of phenylpropane derivatives. 4CL is the branching enzyme that connects the lignin synthesis pathway and flavonoid pathway, controls the metabolic synthesis direction of phenylpropane derivatives, and is the key enzyme in the phenylpropane synthesis pathway. 4CL acts on different substrates to produce acyl CoA thiolipids for subsequent reactions. Through the synthesis of these phenylpropane derivatives CoA lipids (e.g. p-gumaroyl CoA, feruloyl CoA, p-coumaryl CoA), downstream enzymes use them as substrates to form different phenylpropane metabolites. Therefore, 4CL enzyme plays a switching role in the biosynthesis of curcumin. In the curcumin biosynthesis pathway, the role of 4CL in dipeptide-CoA synthase DCS/ curcumin synthase CURS is to catalyze cinnamic acid to produce cinnamyl-CoA and make the reaction to the direction of curcumin production. In the curcumin synthase CUS pathway, ferulic acid is used to catalyze the formation of gumaroyl-CoA in order to facilitate the following reaction.