Literature summary for 2.3.1.304 extracted from

Sim, S.J.; Snell, K.D.; Hogan, S.A.; Stubbe, J.; Rha, C.; Sinskey, A.J.
PHA synthase activity controls the molecular weight and polydispersity of polyhydroxybutyrate in vivo (1997), Nat. Biotechnol., 15, 63-67.

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Cloned(Commentary)

Cloned (Comment)	Organism
a synthetic operon for polyhydroxyalkanoate biosynthesis designed to yield high levels of PHA synthase activity in vivo is constructed by positioning a genetic fragment encoding beta-ketothiolase and acetoacetyl-CoA reductase behind a modified synthase gene containing an Escherichia coli promoter and ribosome binding site. Plasmids containing the synthetic operon and the native Alcaligenes eutrophus PHA operon are transformed into Escherichia DH5 alpha and analyzed for polyhydroxybutyrate production. The molecular weight of polymer isolated from recombinant Escherichia coli containing the modified synthase construct is lower than that of the polymer from Escherichia coli containing the native Alcaligenes eutrophus operon. A further decrease in polyester molecular weight is observed with increased induction of the PHA biosynthetic genes in the synthetic operon. Comparison of the enzyme activity levels of PHA biosynthetic enzymes in a strain encoding the native operon with a strain possessing the synthetic operon indicates that the amount of polyhydroxyalkanoate synthase in a host organism plays a key role in controlling the molecular weight and the polydispersity of polymer	Cupriavidus necator

Cloned (Comment)

Organism

a synthetic operon for polyhydroxyalkanoate biosynthesis designed to yield high levels of PHA synthase activity in vivo is constructed by positioning a genetic fragment encoding beta-ketothiolase and acetoacetyl-CoA reductase behind a modified synthase gene containing an Escherichia coli promoter and ribosome binding site. Plasmids containing the synthetic operon and the native Alcaligenes eutrophus PHA operon are transformed into Escherichia DH5 alpha and analyzed for polyhydroxybutyrate production. The molecular weight of polymer isolated from recombinant Escherichia coli containing the modified synthase construct is lower than that of the polymer from Escherichia coli containing the native Alcaligenes eutrophus operon. A further decrease in polyester molecular weight is observed with increased induction of the PHA biosynthetic genes in the synthetic operon. Comparison of the enzyme activity levels of PHA biosynthetic enzymes in a strain encoding the native operon with a strain possessing the synthetic operon indicates that the amount of polyhydroxyalkanoate synthase in a host organism plays a key role in controlling the molecular weight and the polydispersity of polymer

Cupriavidus necator

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining

Organism

Organism	UniProt	Comment	Textmining
Cupriavidus necator	-	-	-

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Release 2023.1 (January 2023)