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Revision as of 18:16, 16 October 2018
Parts
Background
“Liggreen” is composed of monolignols, and we have produced three enzymes to catalyze the polymerization. Laccase 1 from Pinus taeda can catalyze monolignols dehydrogenation, which leads to free radical addition of dehydrogenated monolignols. However, after the monolignols become dimers or oligomers, it will be hard for those dimers or oligomers to bind to the active site of laccase 1 and stop the dehydrogenation reaction of monolignols.
In this case, we choose the others enzymes, peroxidase 16 and peroxidase 18. Those are isoenzymes from Picea abies, which are able to bind to oligomers and directly polymerize.
All the enzymes above can function in the same pH value and buffer, which is critical to our design for co-reaction in production line.
Basic Parts
| Part Name | Part type | Description | Lenght |
|---|---|---|---|
| BBa_K2809001 | Ribosome binding site | Kozak sequence (Pichia pastoris) | 7 |
| BBa_K2809002 | Tag | Prepro-alpha-factor (codon modified for Pichia pastoris) | 267 |
| BBa_K2809010 | Protein_Domain | Mature Lac 1(laccase) | 1719 |
| BBa_K2809020 | Protein_Domain | Mature Px18(peroxidase) | 954 |
| BBa_K2809030 | Protein_Domain | Mature Px16(peroxidase) | 972 |
Composite Parts
| Part Name | Part type | Description | Lenght |
|---|---|---|---|
| BBa_K2809011 | Composite | Laccase 1 | 1993 |
| BBa_K2809021 | Peroxidase 18 | 1228 | |
| BBa_K2809031 | Peroxidase 16 | 1246 |