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Results 1 - 4 of 4
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comparison of P(3HB) biosynthesis by recombinant Cupriavidus necator PHB-4 harboring the synthase gene of Cupriavidus sp. USMAA2-4 from various plant oils
physiological function
heterologous expression of foreign PHA synthases in the single mutant lacking isoform PhaC2 and in a double mutant lacking both isoforms PhaC1 and PhaC2 results in a significant accumulation of polyhydroxybutanoate in all generated strains. Six of the thirteen generated phaC hybrid vectors lead to an increased polyhydroxybutanoate accumulation in the single mutant in comparison to the wild type strain. All recombinant strains of Rthe double mutant harboring heterologous phaC genes accumulate significantly less polyhydroxybutanoate than the recombinant single mutants and the wild type strain. Recombinant strains with higher content of accumulated polyhydroxybutanoate are linked to higher growth rates and higher maximum ODs, due to the light scattering effect of polyhydroxybutanoate granules. All recombinant strains of the double mutant show significantly decreased growth rates and maximum ODs
physiological function
P(3HB) synthase catalyzes polymerization of the 3-hydroxybutyryl-CoA monomers, Pseudomonas sp. USM 4-55 is a soil isolated bacterium that possesses the ability to produce polyhydroxyalkanoates consisting of both poly(3-hydroxybutyrate) homopolymer and medium-chain length monomers (6 to 14 carbon atoms) when sugars or fatty acids are utilized as the sole carbon source
physiological function
recombinant Escherichia coli expressing PHA synthase from Bacillus cereus shows a reduction of the molecular weight of PHA produced during the stationary phase of growth. Its carboxy end structure is capped by ethanol, as the result of alcoholytic cleavage of PHA chains by PhaRC induced by endogenous ethanol. This scission reaction is also induced by exogenous ethanol in both in vivo and in vitro assays. In addition, PhaRC has alcoholysis activity for PHA chains synthesized by other synthases
Results 1 - 4 of 4