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

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 th...

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Bibliographic Details
Published in:The Journal of biological chemistry 1989-09, Vol.264 (26), p.15298-15303
Main Authors: PEOPLES, O. P, SINSKEY, A. J
Format: Article
Language:English
Subjects:
Alcaligenes - enzymology
Alcaligenes - genetics
Amino Acid Sequence
Bacteriology
Base Sequence
Biological and medical sciences
Chromosome Deletion
Cloning, Molecular
Escherichia coli - genetics
Fundamental and applied biological sciences. Psychology
Gene Amplification
Genes
Genes, Bacterial
Hydroxybutyrates - metabolism
Metabolism. Enzymes
Microbiology
Molecular Sequence Data
Mutation
Plasmids
Polyesters - metabolism
Restriction Mapping
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Summary: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.
ISSN:0021-9258
1083-351X