Journal
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
Volume 394, Issue 1, Pages 87-98Publisher
ELSEVIER SCIENCE INC
DOI: 10.1006/abbi.2001.2522
Keywords
polyhydroxybutyrate; PHA synthase; Ralstonia eutropha; Allochromatium vinosun; phosphopantetheinylation
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Funding
- NIGMS NIH HHS [GM49171] Funding Source: Medline
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Class I and III polyhydroxyalkanoate (PHA) synthases catalyze the conversion of beta -hydroxybutyryl coenzyme A (HBCoA) to polyhydroxybutyrate. The Class I PHA synthase from Ralstonia eutropha has been purified by numerous labs with reported specific activities that vary between 1 and 160 U/mg. An N-terminal (His)(6)-PHA synthase was constructed and purified with specific activity of 40 U/mg. The variable activity is shown to be related to the protein's propensity to aggregate and not to incomplete post-translational modification by coenzyme A and a phosphopantetheinyl transferase. The substrate specificities of this enzyme and the Class III PRA synthase from Allochromatium vinosum have been determined with nine analogs of varied chain length and branching, OH group position within the chain, and thioesters. The results suggest that in vitro, both PRA synthases are very specific and provide further support for their active site structural similarities. In vitro results differ from studies in vivo. (C) 2001 Academic Press.
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