Literature summary extracted from

Zhang, S.; Kolvek, S.; Lenz, R.W.; Goodwin, S.
Mechanism of the polymerization reaction initiated and catalyzed by the polyhydroxybutyrate synthase of Ralstonia eutropha (2003), Biomacromolecules, 4, 504-509.

Protein Variants

EC Number	Protein Variants	Comment	Organism
2.3.1.304	C319A	heterodimer containing the mutated subunit has no activity	Cupriavidus necator

Organism

EC Number	Organism	UniProt	Comment	Textmining
2.3.1.304	Cupriavidus necator	-	-	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2.3.1.304	3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n	-	Cupriavidus necator	[(R)-3-hydroxybutanoate](n+1) + CoA	-	?

Subunits

EC Number	Subunits	Comment	Organism
2.3.1.304	dimer	homodimer is the active form of the enzyme. Two identical thiol groups from C319 residues on each subunit of the homodimer are required to form the catalytic site for the initiation and propagation reactions. A dimer synthase that has initiated the polymerization reaction (primed synthase) is significantly more stable against dissociation than the unprimed (unreacted) dimer synthase	Cupriavidus necator

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Release 2023.1 (January 2023)