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

Biosci Biotechnol Biochem. 2010;74(8):1710-2. doi: 10.1271/bbb.100224. Epub 2010 Aug 7.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 3-Hydroxybutyric Acid / chemistry*
  • Acyltransferases / chemistry
  • Acyltransferases / genetics*
  • Acyltransferases / metabolism*
  • Amino Acid Sequence
  • Molecular Sequence Data
  • Mutation*
  • Polyhydroxyalkanoates / chemistry
  • Polyhydroxyalkanoates / metabolism*
  • Pseudomonas / cytology
  • Pseudomonas / enzymology*
  • Pseudomonas / genetics
  • Pseudomonas / metabolism
  • Sequence Alignment
  • Sequence Homology, Amino Acid*

Substances

  • Polyhydroxyalkanoates
  • Acyltransferases
  • poly(3-hydroxyalkanoic acid) synthase
  • 3-Hydroxybutyric Acid