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PHA synthase activity controls the molecular weight and polydispersity of polyhydroxybutyrate in vivo

✍ Scribed by Sim, Sang Jun; Snell, Kristi D.; Hogan, Scott A.; Stubbe, JoAnne; Rha, Chokyun; Sinskey, Anthony J.

Book ID
109901347
Publisher
Nature Publishing Group
Year
1997
Tongue
English
Weight
562 KB
Volume
15
Category
Article
ISSN
1087-0156

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## Abstract 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