Literature summary for 2.3.1.304 extracted from

Tian, J.; Sinskey, A.J.; Stubbe, J.
Class III polyhydroxybutyrate synthase: involvement in chain termination and reinitiation (2005), Biochemistry, 44, 8369-8377.

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Organism

Organism	UniProt	Comment	Textmining
Allochromatium vinosum	-	recombinant	-

Purification (Commentary)

Purification (Comment)	Organism
-	Allochromatium vinosum

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
(R)-3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n	an inherent property of the synthase is chain termination and reinitiation. Class III PhaCPhaEAv synthase initiates polymerization through selfpriming. The primed synthase, species I, can serve as a substrate for further polyhydroxybutanoate elongation. Since hydroxybutyryl units can be added onto the existing polymers when HB-CoA is introduced into a reaction mixture containing preformed intermediate species, the reaction catalyzed by PhaCPhaEAv is nonprocessive. When enough (R)-3-hydroxybutyryl-CoA (S/E ratio is high) is available to load all of the enzyme present, the polymerization may be processive such that no intermediates can be detected and preformed oligomers cannot be extended	Allochromatium vinosum	[(R)-3-hydroxybutanoate](n+1) + CoA	-	?

Synonyms

Synonyms	Comment	Organism
class III polyhydroxybutyrate synthase	-	Allochromatium vinosum
PhaCPhaEAv	-	Allochromatium vinosum

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Release 2023.1 (January 2023)