POLY-BETA-HYDROXYBUTYRATE (PHB) BIOSYNTHESIS IN ALCALIGENES-EUTROPHUS H16 - IDENTIFICATION AND CHARACTERIZATION OF THE PHB POLYMERASE GENE (PHBC)
- 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.This publication has 16 references indexed in Scilit:
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