Poly-beta-hydroxybutyrate (PHB) biosynthesis in Alcaligenes eutrophus H16. Identification and characterization of the PHB polymerase gene (phbC).

TitlePoly-beta-hydroxybutyrate (PHB) biosynthesis in Alcaligenes eutrophus H16. Identification and characterization of the PHB polymerase gene (phbC).
Publication TypeJournal Article
Year of Publication1989
AuthorsPeoples, OP, Sinskey, AJ
JournalJ Biol Chem
Volume264
Issue26
Pagination15298-303
Date Published1989 Sep 15
ISSN0021-9258
KeywordsAlcaligenes, Amino Acid Sequence, Base Sequence, Chromosome Deletion, Cloning, Molecular, Escherichia coli, Gene Amplification, Genes, Genes, Bacterial, Hydroxybutyrates, Molecular Sequence Data, Mutation, Plasmids, Polyesters, Restriction Mapping
Abstract

The phbC gene encoding the third enzyme of the poly-beta-hydroxybutyrate biosynthetic pathway, poly-beta-hydroxybutyrate polymerase, in Alcaligenes eutrophus H16 has been identified by the complementation of poly-beta-hydroxybutyrate negative mutants of A. eutrophus H16. These results demonstrate that the three enzymes of the poly-beta-hydroxybutyrate biosynthetic pathway are organized phbC-phbA-phbB. Expression of all three genes in Escherichia coli results in a significant level (50% dry cell weight) of poly-beta-hydroxybutyrate production. phbC encodes a polypeptide of Mr = 63,900 which has a hydropathy profile distinct from typical membrane proteins indicating that poly-beta-hydroxybutyrate biosynthesis probably does not involve a membrane complex.

Alternate JournalJ Biol Chem
Citation Key191
PubMed ID2670936