Literature summary for 2.3.1.304 extracted from

Jia, Y.; Yuan, W.; Wodzinska, J.; Park, C.; Sinskey, A.J.; Stubbe, J.
Mechanistic studies on class I polyhydroxybutyrate (PHB) synthase from Ralstonia eutropha: class I and III synthases share a similar catalytic mechanism (2001), Biochemistry, 40, 1011-1019.

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Protein Variants

Protein Variants	Comment	Organism
C319A	less than 0.0005% of the wild-type activity	Cupriavidus necator
D480N	0.004% of the wild-type activity	Cupriavidus necator
H481Q	20% of the wild-type activity	Cupriavidus necator
H508Q	less than 0.0005% of the wild-type activity	Cupriavidus necator

Organism

Organism	UniProt	Comment	Textmining
Cupriavidus necator	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n	Ralstonia eutropha synthase possesses an essential catalytic dyad (C319-H508) in which the C319 is involved in covalent catalysis. A conserved Asp, D480, is not required for acylation of C319 by sT-CoA and is proposed to function as a general base catalyst to activate the hydroxyl of HBCoA for ester formation	Cupriavidus necator	[(R)-3-hydroxybutanoate](n+1) + CoA	-	?

Subunits

Subunits	Comment	Organism
dimer	it is suggested that a dimeric form of the enzyme is involved in elongation	Cupriavidus necator

Synonyms

Synonyms	Comment	Organism
class I polyhydroxybutyrate synthase	-	Cupriavidus necator

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Release 2023.1 (January 2023)