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Gene Review

phaC  -  poly(3-hydroxyalkanoate) polymerase 2

Pseudomonas putida KT2440

 
 
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Disease relevance of phaC

  • Cloning, molecular analysis, and expression of the polyhydroxyalkanoic acid synthase (phaC) gene from Chromobacterium violaceum [1].
  • The final step in PHA biosynthesis is catalyzed by two PHA polymerases (phaC) in Pseudomonas putida [2].
  • It was found that the two phaC genes are not expressed in E. coli without an external promoter [2].
  • A process for the large-scale production of 4-hydroxyvalerate (4HV)-containing biopolyesters with a new monomer composition was developed by means of high-cell-density cultivation applying recombinant strains of Pseudomonas putida and Ralstonia eutropha, harboring the PHA-biosynthesis genes phaC and phaE of Thiocapsa pfennigii [3].
 

High impact information on phaC

  • The nucleotide sequence of this region showed a 1,782-bp poly (3-hydroxyalkanoate) (PHA) synthase gene (phaC(Ac) [i.e., the phaC gene from A. caviae]) together with four open reading frames (ORF1, -3, -4, and -5) and one putative promoter region [4].
  • In addition, the PHA monomer composition differed when different gene expression systems or different phaC genes were applied [2].
  • During heterologous expression of phaC from Plac on a high copy number plasmid, a rapid reduction of the number of colony forming units was observed, especially for phaC2 [2].
  • Recombinant strains of R. eutropha PHB-4 harboring either P. mendocina phaC gene even accumulated a homopolyester of 3HB during cultivation with gluconate, with poly(3HB) amounting to more than 80% of the cell dry matter if phaC2 was expressed [5].
  • Also, with respect to the molecular organization of phaE and phaC, this region of the T. pfennigii genome resembled very much the corresponding regions of C. vinosum and of Thiocystis violacea [6].
 

Chemical compound and disease context of phaC

  • A recombinant strain of Pseudomonas putida, which overexpressed phaE and phaC from T. pfennigii, was used to isolate the PHA synthase by a two-step procedure including chromatography on Procion Blue H-ERD and hydroxyapatite [6].

References

 
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