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Literature summary for 2.3.1.304 extracted from
- Substrate chain-length specificities of polyhydroxyalkanoate synthases PhaC1 and PhaC2 from Pseudomonas aeruginosa P-5 (2016), Korean J. Microbiol., 52, 455-462 .
No PubMed abstract available
Application
| Application | Comment | Organism |
|---|---|---|
| synthesis | the enzyme mutant S326T/Q482K might be useful for production of distinct polyhydroxyalkanoate copolymers with improved material properties | Pseudomonas aeruginosa |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| recombinant expression of PhaC1P-5 in Pseudomonas putida strain Gp104 | Pseudomonas aeruginosa |
| recombinant expression of PhaC2P-5 in Pseudomonas putida strain Gp104 or in Ralstonia eutropha strain PHB-4 | Pseudomonas aeruginosa |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| Q482K | site-directed mutagenesis, the mutant is very effective in synthesizing copolymers with a higher 3-hydroxyalkanoate fraction compared to wild-type | Pseudomonas aeruginosa |
| S326T | site-directed mutagenesis, the mutant is very effective in synthesizing copolymers with a higher 3-hydroxyalkanoate fraction compared to wild-type | Pseudomonas aeruginosa |
| S326T/Q482K | site-directed mutagenesis, the double mutant grown on nonanoic acid in Pseudomonas putida strain GPp104 or grown on valeric acid in Ralstonia eutropha strain PHB-4 shows a 2.5fold higher copolymer content with 3.8fold increased 3-hydroxyalkanoate fraction compared to wild-type | Pseudomonas aeruginosa |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Pseudomonas aeruginosa | H6VX88 | - |
- |
| Pseudomonas aeruginosa | H6VX89 | - |
- |
| Pseudomonas aeruginosa P-5 | H6VX88 | - |
- |
| Pseudomonas aeruginosa P-5 | H6VX89 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | analysis of enzyme substrate chain length specificity, overview. Enzyme PhaC2P-5 incorporates both 3-hydroxyalkanoate monomers and medium-chain-length 3-hydroxyalkanoates into polyhydoxyalkanoate (PHA) | Pseudomonas aeruginosa | ? | - |
- |
 |
| additional information | analysis of enzyme substrate chain length specificity, overview. PhaC1P-5 prefers only medium chain-length 3-hydroxyalkanoates for polymerization | Pseudomonas aeruginosa | ? | - |
- |
|
| additional information | analysis of enzyme substrate chain length specificity, overview. PhaC1P-5 prefers only medium chain-length 3-hydroxyalkanoates for polymerization | Pseudomonas aeruginosa P-5 | ? | - |
- |
|
| additional information | analysis of enzyme substrate chain length specificity, overview. Enzyme PhaC2P-5 incorporates both 3-hydroxyalkanoate monomers and medium-chain-length 3-hydroxyalkanoates into polyhydoxyalkanoate (PHA) | Pseudomonas aeruginosa P-5 | ? | - |
- |
|
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| PhaC1 | - |
Pseudomonas aeruginosa |
| PhaC1P-5 | - |
Pseudomonas aeruginosa |
| PhaC2 | - |
Pseudomonas aeruginosa |
| PhaC2P-5 | - |
Pseudomonas aeruginosa |
| polyhydroxyalkanoate synthase | - |
Pseudomonas aeruginosa |
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