Application | Comment | Organism |
---|---|---|
synthesis | expansion of the substrate specificity and enhancment of biosynthesis of polyhydroxyalkanoate by site-specific mutagenesis. Mutated PhaC1s are coexpressed with beta-ketothiolase and acetoacetyl-CoA reductase to supply sufficient short-chain length (R)-3-hydroxyacyl-CoA as a substrate. Mutation L484V remarkably enhances the monomer ratio of (R)-3-hydroxybutyrate in a polyhydroxyalkanoate accumulation experiment. Val is the most favorable amino acid for incorporating (R)-3-hydroxybutyrate unit synthesis. A single mutation at Q481M, S482G and A547V obviously increases polyhydroxyalkanoate yields. Q481M and S482G enhance the (R)-3-hydroxyhexanoate monomer composition in the polyhydroxyalkanoate accumulation | Pseudomonas putida |
Cloned (Comment) | Organism |
---|---|
expression in Pseudomonas putida GPp104 PHA mutant | Pseudomonas putida |
Protein Variants | Comment | Organism |
---|---|---|
A547V | mutation increases polyhydroxyalkanoate yields | Pseudomonas putida |
L484V | mutation remarkably enhances the monomer ratio of (R)-3-hydroxybutyrate in a polyhydroxyalkanoate accumulation experiment. Val is the most favorable amino acid for incorporating (R)-3-hydroxybutyrate unit synthesis | Pseudomonas putida |
Q481M | mutation increases polyhydroxyalkanoate yields and enhances the (R)-3-hydroxyhexanoate monomer composition in the polyhydroxyalkanoate accumulation | Pseudomonas putida |
S482G | mutation increases polyhydroxyalkanoate yields and enhances the (R)-3-hydroxyhexanoate monomer composition in the polyhydroxyalkanoate accumulation | Pseudomonas putida |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pseudomonas putida | - |
- |
- |
Pseudomonas putida GPo1 / ATCC29347 | - |
- |
- |
Synonyms | Comment | Organism |
---|---|---|
PhaC1 | - |
Pseudomonas putida |