EC Number |
Application |
Reference |
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3.1.1.76 | degradation |
enzyme is able to degrade functionalized polyhydroxyalkanoate polymers containing thioester groups in the side chain, releasing functional thioester-based monomers and oligomers |
-, 749730 |
3.1.1.76 | synthesis |
construcution of a biosynthetic pathway for the production of (R)-3-hydroxyalkanoates through in vivo depolymerization of poly(3-hydroxyalkanoates) in an Escherichia coli fadA mutant WA101 by introducing the Pseudomonas sp. 61-3 polyhydroxyalkanoate synthase gene (phaC2) and the Pseudomonas aeruginosa intracellular polyhydroxyalkanoate depolymerase gene (phaZ). Upon culture in Luria-Bertani (LB) medium containing 2 g/l of sodium decanoate, 3-hydroxyalkanoats can be produced to the concentration of 0.49 g/l. The mole fractions are 7.5 mol% of 3-hydroxybutanoate, 31.6 mol% of 3-hydroxyhexanoate, 30 mol% of 3-hydroxyoctanoate, 29.4 mol% of 3-hydroxydecanoate, and 1.5 mol% of 3-hydroxydodecanoate |
751434 |
3.1.1.76 | synthesis |
engineering of Rhodospirillum rubrum to synthesize a heteropolymer of mainly 3-hydroxydecanoic acid and 3-hydroxyoctanoic acid from CO- and CO2-containing artificial synthesis gas (syngas) using Pseudomonas putida 3-hydroxyacyl acyl carrier protein thioesterase, a medium-chain-length fatty acid coenzyme A ligase, and an medium-chain-length polyhydroxyalkanoate synthase. A heteropolymer of 3-hydroxydecanoic acid and 3-hydroxyoctanoic acid accumulates to up to 7.1% (wt/wt) of the cell dry weight. The recombinant strains are able to partially degrade the polymer, and the deletion of isoform PhaZ2 does not reduce mobilization of the accumulated polymer significantly. Mutation C176A in the active site of PhaZ2 leads to a slight increase in poly-3-hydroxyalkanoate accumulation |
-, 749659 |
3.1.1.76 | synthesis |
the enzyme migt be used as biocatalyst for the production of enantiopure hydroxyalkanoic acids and oligomers as building blocks for the synthesis of biobased polymers |
-, 729030 |