Literature summary for 2.3.1.304 extracted from

Buckley, R.M.; Stubbe, J.
Chemistry with an artificial primer of polyhydroxybutyrate synthase suggests a mechanism for chain termination (2015), Biochemistry, 54, 2117-2125.

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Organism

Organism	UniProt	Comment	Textmining
Caulobacter vibrioides	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
(R)-3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n	-	Caulobacter vibrioides	[(R)-3-hydroxybutanoate](n+1) + CoA	rate of elongation is much faster than the rate of initiation. The protein is uniformly loaded by a a single CoA/PhaC. Priming with the artificial primer sTCoA, i.e. a trimer of (R)-3-hydroxybutyryl-CoA in which the terminal OH group is replaced with a 3H, increases the uniformity of elongation, allowing distinct polymerization species to be observed. In the absence of (R)-3-hydroxybutyryl-CoA, a dimer of (R)-3-hydroxybutyryl-CoA is formed with a rate constant of 0.017 per s. The dimer forms via attack of CoA on the oxoester of the trimer of (R)-3-hydroxybutyryl-CoA-enzyme chain, leaving the synthase attached to a single (R)-3-hydroxybutyryl unit	?

Synonyms

Synonyms	Comment	Organism
PhaC	-	Caulobacter vibrioides

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Release 2023.1 (January 2023)