A new beneficial mutation in pseudomonas sp. 61-3 polyhydroxyalkanoate (PHA) synthase for enhanced cellular content of 3-hydroxybutyrate-based PHA explored using its enzyme homolog as a mutation template.
A newly isolated mutation (Gln508Leu) and a combination of it with previously discovered beneficial mutations in polyhydroxyalkanoate synthase 1 from Pseudomonas sp. 61-3 were found to enhance the production of poly(3-hydroxybutyrate) [P(3HB)] and poly(3HB-co-3-hydroxyalkanoate)s in recombinant Escherichia coli.
Shozui
Fumi
F
Division of Biotechnology and Macromolecular Chemistry, Graduate School of Engineering, Hokkaido University, Kita-ku, Sapporo, Japan. staguchi@eng.hokudai.ac.jp
Sun
Jian
J
Song
Yuyang
Y
Yamada
Miwa
M
Sakai
Kohei
K
Matsumoto
Ken'ichiro
K
Takase
Kazuma
K
Taguchi
Seiichi
S
D020155:3-Hydroxybutyric Acid / Q000737:chemistry*; D000217:Acyltransferases / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D000595:Amino Acid Sequence; D008969:Molecular Sequence Data; D009154:Mutation; D054813:Polyhydroxyalkanoates / Q000737:chemistry / Q000378:metabolism*; D011549:Pseudomonas / Q000166:cytology / Q000201:enzymology* / Q000235:genetics / Q000378:metabolism; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
D054813:Polyhydroxyalkanoates; D000217:Acyltransferases; C077225:poly(3-hydroxyalkanoic acid) synthase; D020155:3-Hydroxybutyric Acid