Variation in copolymer composition and molecular weight of polyhydroxyalkanoate generated by saturation mutagenesis of Aeromonas caviae PHA synthase.
Amino acid substitutions at two residues downstream from the active-site histidine of polyhydroxyalkanoate (PHA) synthases are effective for changing the composition and the molecular weight of PHA. In this study, saturation mutagenesis at the position Ala505 was applied to PHA synthase (PhaCAc) from Aeromonas caviae to investigate the effects on the composition and the molecular weight of PHA synthesized in Ralstonia eutropha. The copolymer composition and molecular weight of PHA were varied by association with amino acid substitutions. There was a strong relationship between copolymer composition and PHA synthase activity of the cells. This finding will serve as a rationale for producing tailor-made PHAs.
Tsuge
Takeharu
T
Department of Innovative and Engineered Materials, Tokyo Institute of Technology, 4259 Nagatsuta, Yokohama 226-8502, Japan. tsuge.t.aa@m.titech.ac.jp
Watanabe
Shinko
S
Sato
Shun
S
Hiraishi
Tomohiro
T
Abe
Hideki
H
Doi
Yoshiharu
Y
Taguchi
Seiichi
S
D000217:Acyltransferases / Q000235:genetics* / Q000378:metabolism; D000333:Aeromonas / Q000737:chemistry* / Q000235:genetics; D000595:Amino Acid Sequence; D020118:Cupriavidus necator; D017931:DNA Primers / Q000235:genetics; D008969:Molecular Sequence Data; D016296:Mutagenesis; D054813:Polyhydroxyalkanoates / Q000737:chemistry*; D011108:Polymers / Q000737:chemistry; D017433:Protein Structure, Secondary
D017931:DNA Primers; D054813:Polyhydroxyalkanoates; D011108:Polymers; D000217:Acyltransferases; C077225:poly(3-hydroxyalkanoic acid) synthase