Combination of N149S and D171G mutations in Aeromonas caviae polyhydroxyalkanoate synthase and impact on polyhydroxyalkanoate biosynthesis
β Scribed by Takeharu Tsuge; Shinko Watanabe; Daisuke Shimada; Hideki Abe; Yoshiharu Doi; Seiichi Taguchi
- Book ID
- 109329983
- Publisher
- John Wiley and Sons
- Year
- 2007
- Tongue
- English
- Weight
- 109 KB
- Volume
- 277
- Category
- Article
- ISSN
- 0378-1097
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## Abstract Amino acid substitutions at two residues downstream from the activeβsite 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
## Abstract Summary: Type I polyhydroxyalkanoate (PHA) synthases, as represented by __Ralstonia eutropha__ enzyme (PhaC~Re~), have narrow substrate specificity toward (__R__)β3βhydroxyacylβcoenzyme A with acyl chain length of C3βC5 to yield PHA polyesters. In this study, saturation point mutagenesi