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Literature summary for 2.3.1.304 extracted from

  • Cho, M.; Brigham, C.J.; Sinskey, A.J.; Stubbe, J.
    Purification of polyhydroxybutyrate synthase from its native organism, Ralstonia eutropha: implications for the initiation and elongation of polymer formation in vivo (2012), Biochemistry, 51, 2276-2288.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.3.1.304

Cloned(Commentary)

Cloned (Comment) Organism
construction of an N-terminally Strep2-tagged PhaC, Strep2-PhaCRe, and integration into the Ralstonia eutropha genome in place of wild-type phaC and functional expression without a lag phase of CoA release in the enzyme reaction, functional expression of Strep2-PhaCRe in Escherichia coli strain BL21(DE3) showing a lag phase in CoA release Cupriavidus necator

Protein Variants

Protein Variants Comment Organism
C319A site-directed mutagenesis Cupriavidus necator

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
64000
-
 1 * 64000, PhaC, SDS-PAGE Cupriavidus necator
64000
-
 2 * 64000, PhaC, SDS-PAGE Cupriavidus necator

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n Cupriavidus necator
-
 [(R)-3-hydroxybutanoate]n+1 + CoA
-
 ?
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
 [(R)-3-hydroxybutanoate]n+1 + CoA
-
 ?

Organism

Organism UniProt Comment Textmining
Cupriavidus necator
-
-
-
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant N-terminally Strep2-tagged PhaC from Ralstonia eutropha by affinity chromatography. Strep2-PhaCRe co-purifies with the phasin protein, PhaP1, and with soluble polyhydroxybutyrate of 350 kDa MW in a high-molecular weight complex and in monomeric/dimeric forms with no associated PhaP1 or polyhydroxybutyrate Cupriavidus necator

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3 8 pooled monomeric and dimeric fractions of Strep2-PhaCRe, 30°C, pH not specified in the publication Cupriavidus necator
36
-
 purified recombinant Strep2-PhaCRe, 30°C, pH not specified in the publication Cupriavidus necator

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
-
 Cupriavidus necator [(R)-3-hydroxybutanoate]n+1 + CoA
-
 ?
3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
-
 Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1 [(R)-3-hydroxybutanoate]n+1 + CoA
-
 ?

Subunits

Subunits Comment Organism
dimer 2 * 64000, PhaC, SDS-PAGE Cupriavidus necator
monomer 1 * 64000, PhaC, SDS-PAGE Cupriavidus necator

Synonyms

Synonyms Comment Organism
class I PHB synthase
-
 Cupriavidus necator
class I polyhydroxybutyrate synthase
-
 Cupriavidus necator
PhaC
-
 Cupriavidus necator

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Cupriavidus necator

General Information

General Information Comment Organism
physiological function class I PHB synthase, PhaC, from Ralstonia eutropha catalyzes the formation of PHB from (R)-3-hydroxybutyryl-CoA, ultimately resulting in the formation of insoluble granules, the polymer elongation rate is much faster than the initiation rate Cupriavidus necator