
Recently, we have cloned and analyzed two polyhydroxyalkanoate (PHA) synthase genes (phaC1 and phaC2 in the pha cluster) from Pseudomonas aureofaciens. In this report, the deduced amino acid (AA) sequences of PHA synthase 1 and PHA synthase 2 from P. aureofaciens are compared with those from three other bacterial strains (Pseudomonas sp. 61-3, P. oleovorans and P. aeruginosa) containing the homologous pha cluster. The level of homology of either PHA synthase 1 or PHA synthase 2 was high with each enzyme from these three bacterial strains. Furthermore, multialignment of PHA synthase AA sequences implied that both enzymes of PHA synthase 1 and PHA synthase 2 were highly conserved in the four strains including P. aureofaciens.
Isoenzymes, Bacterial Proteins, Pseudomonas, Molecular Sequence Data, Sequence Homology, Amino Acid Sequence, Sequence Alignment, Acyltransferases
Isoenzymes, Bacterial Proteins, Pseudomonas, Molecular Sequence Data, Sequence Homology, Amino Acid Sequence, Sequence Alignment, Acyltransferases
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