1. Class IV polyhydroxyalkanoate (PHA) synthases and PHA-producing Bacillus
- Author
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Manami Hyakutake, Kouhei Mizuno, and Takeharu Tsuge
- Subjects
biology ,Polyhydroxyalkanoates ,Protein subunit ,fungi ,Nucleic acid sequence ,Bacillus cereus ,Active site ,General Medicine ,biology.organism_classification ,medicine.disease_cause ,Applied Microbiology and Biotechnology ,Recombinant Proteins ,Protein Subunits ,Biochemistry ,Cereus ,Bacillus megaterium ,Escherichia coli ,biology.protein ,medicine ,Acyltransferases ,Biotechnology - Abstract
This review highlights the recent investigations of class IV polyhydroxyalkanoate (PHA) synthases, the newest classification of PHA synthases. Class IV synthases are prevalent in organisms of the Bacillus genus and are composed of a catalytic subunit PhaC (approximately 40 kDa), which has a PhaC box sequence ([GS]-X-C-X-[GA]-G) at the active site, and a second subunit PhaR (approximately 20 kDa). The representative PHA-producing Bacillus strains are Bacillus megaterium and Bacillus cereus; the nucleotide sequence of phaC and the genetic organization of the PHA biosynthesis gene locus are somewhat different between these two strains. It is generally considered that class IV synthases favor short-chain-length monomers such as 3-hydroxybutyrate (C4) and 3-hydroxyvalerate (C5) for polymerization, but can polymerize some unusual monomers as minor components. In Escherichia coli expressing PhaRC from B. cereus YB-4, the biosynthesized PHA undergoes synthase-catalyzed alcoholytic cleavage using endogenous and exogenous alcohols. This alcoholysis is thought to be shared among class IV synthases, and this reaction is useful not only for the regulation of PHA molecular weight but also for the modification of the PHA carboxy terminus. The novel properties of class IV synthases will open up the possibility for the design of new PHA materials.
- Published
- 2015
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