• 15 September 1989
    • journal article
    • research article
    • Vol. 264  (26) , 15298-15303
Abstract
The phbC gene encoding the third enzyme of the poly-.beta.-hydroxybutyrate biosynthetic pathway, poly-.beta.-hydroxybutyrate polymerase, in Alcaligenes eutrophus H16 has bene 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.