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Literature summary for 2.3.1.304 extracted from

  • Zhang, S.; Kolvek, S.; Goodwin, S.; Lenz, R.W.
    Poly(hydroxyalkanoic acid) biosynthesis in Ectothiorhodospira shaposhnikovii: characterization and reactivity of a type III PHA synthase (2004), Biomacromolecules, 5, 40-48.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
PHA synthase genes (phaC and phaE) are cloned by screening a genomic library for PHA accumulation in Escherichia coli cells Ectothiorhodospira shaposhnikovii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.03
-
(R)-3-hydroxyvaleryl-CoA
-
Ectothiorhodospira shaposhnikovii
0.065
-
(R)-3-hydroxybutyryl-CoA
-
Ectothiorhodospira shaposhnikovii
0.085
-
4-hydroxybutyryl-CoA
-
Ectothiorhodospira shaposhnikovii

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
40600
-
3 * 41700 (PhaE) + 3 * 40600 (PhaC), two major complexes are identified in preparations of purified PHA synthase. The large complex appears to be composed of 12 PhaC subunits and 12 PhaE subunits (dodecamer). The small complex appears to be composed of 6 PhaC and 6 PhaE subunits (hexamer). In dilute aqueous solution, the synthase is predominantly composed of hexamer and has low activity accompanied with a significant lag period at the initial stage of reaction. The percentage of dodecameric complex increases with increasing salt concentration. The dodecameric complex has a greatly increased specific activity for the polymerization of (R)-3-hydroxybutyryl-CoA and a negligible lag period. The PHA synthase from Ectothiorhodospira shaposhnikoVii may catalyze a living polymerization and two PhaC and two PhaE subunits may comprise a single catalytic site in the synthase complex, SDS-PAGE Ectothiorhodospira shaposhnikovii
40600
-
6 * 41700 (PhaE) + 6 * 40600 (PhaC), two major complexes are identified in preparations of purified PHA synthase. The large complex appears to be composed of 12 PhaC subunits and 12 PhaE subunits (dodecamer). The small complex appears to be composed of 6 PhaC and 6 PhaE subunits (hexamer). In dilute aqueous solution, the synthase is predominantly composed of hexamer and has low activity accompanied with a significant lag period at the initial stage of reaction. The percentage of dodecameric complex increases with increasing salt concentration. The dodecameric complex has a greatly increased specific activity for the polymerization of (R)-3-hydroxybutyryl-CoA and a negligible lag period. The PHA synthase from Ectothiorhodospira shaposhnikoVii may catalyze a living polymerization and two PhaC and two PhaE subunits may comprise a single catalytic site in the synthase complex, SDS-PAGE Ectothiorhodospira shaposhnikovii
41700
-
3 * 41700 (PhaE) + 3 * 40600 (PhaC), two major complexes are identified in preparations of purified PHA synthase. The large complex appears to be composed of 12 PhaC subunits and 12 PhaE subunits (dodecamer). The small complex appears to be composed of 6 PhaC and 6 PhaE subunits (hexamer). In dilute aqueous solution, the synthase is predominantly composed of hexamer and has low activity accompanied with a significant lag period at the initial stage of reaction. The percentage of dodecameric complex increases with increasing salt concentration. The dodecameric complex has a greatly increased specific activity for the polymerization of (R)-3-hydroxybutyryl-CoA and a negligible lag period. The PHA synthase from Ectothiorhodospira shaposhnikoVii may catalyze a living polymerization and two PhaC and two PhaE subunits may comprise a single catalytic site in the synthase complex, SDS-PAGE Ectothiorhodospira shaposhnikovii
41700
-
6 * 41700 (PhaE) + 6 * 40600 (PhaC), two major complexes are identified in preparations of purified PHA synthase. The large complex appears to be composed of 12 PhaC subunits and 12 PhaE subunits (dodecamer). The small complex appears to be composed of 6 PhaC and 6 PhaE subunits (hexamer). In dilute aqueous solution, the synthase is predominantly composed of hexamer and has low activity accompanied with a significant lag period at the initial stage of reaction. The percentage of dodecameric complex increases with increasing salt concentration. The dodecameric complex has a greatly increased specific activity for the polymerization of (R)-3-hydroxybutyryl-CoA and a negligible lag period. The PHA synthase from Ectothiorhodospira shaposhnikoVii may catalyze a living polymerization and two PhaC and two PhaE subunits may comprise a single catalytic site in the synthase complex, SDS-PAGE Ectothiorhodospira shaposhnikovii

Organism

Organism UniProt Comment Textmining
Ectothiorhodospira shaposhnikovii Q9F5P8 and Q9F5P9 PHA synthase subunit PhaC and PhaC
-
Ectothiorhodospira shaposhnikovii Q9F5P9 PHA synthase subunit PhaE
-

Purification (Commentary)

Purification (Comment) Organism
recombinantly expressed in Escherichia coli Ectothiorhodospira shaposhnikovii

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
27.6
-
-
Ectothiorhodospira shaposhnikovii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(R)-3-hydroxybutyryl-CoA + [(R)-3-hydroxybutanoate]n
-
Ectothiorhodospira shaposhnikovii [(R)-3-hydroxybutanoate](n+1) + CoA
-
?
(R)-3-hydroxybutyryl-CoA + [3-hydroxybutanoate]n
-
Ectothiorhodospira shaposhnikovii [(R)-3-hydroxybutanoate](n+1) + CoA
-
?
(R)-3-hydroxypentanoyl-CoA + [(R)-3-hydroxypentanoate]n
-
Ectothiorhodospira shaposhnikovii [(R)-3-hydroxypentanoate](n+1)
-
?
3-hydroxybutyryl-CoA + [3-hydroxybutanoate]n
-
Ectothiorhodospira shaposhnikovii [3-hydroxybutanoate](n+1) + CoA
-
?
3-hydroxyvaleryl-CoA + [3-hydroxyvalerate]n
-
Ectothiorhodospira shaposhnikovii [3-hydroxyvalerate](n+1) + CoA
-
?
4-hydroxybutyryl-CoA + [3-hydroxybutanoate]n
-
Ectothiorhodospira shaposhnikovii [4-hydroxybutanoate](n+1) + CoA
-
?

Subunits

Subunits Comment Organism
dodecamer 6 * 41700 (PhaE) + 6 * 40600 (PhaC), two major complexes are identified in preparations of purified PHA synthase. The large complex appears to be composed of 12 PhaC subunits and 12 PhaE subunits (dodecamer). The small complex appears to be composed of 6 PhaC and 6 PhaE subunits (hexamer). In dilute aqueous solution, the synthase is predominantly composed of hexamer and has low activity accompanied with a significant lag period at the initial stage of reaction. The percentage of dodecameric complex increases with increasing salt concentration. The dodecameric complex has a greatly increased specific activity for the polymerization of (R)-3-hydroxybutyryl-CoA and a negligible lag period. The PHA synthase from Ectothiorhodospira shaposhnikoVii may catalyze a living polymerization and two PhaC and two PhaE subunits may comprise a single catalytic site in the synthase complex, SDS-PAGE Ectothiorhodospira shaposhnikovii
hexamer 3 * 41700 (PhaE) + 3 * 40600 (PhaC), two major complexes are identified in preparations of purified PHA synthase. The large complex appears to be composed of 12 PhaC subunits and 12 PhaE subunits (dodecamer). The small complex appears to be composed of 6 PhaC and 6 PhaE subunits (hexamer). In dilute aqueous solution, the synthase is predominantly composed of hexamer and has low activity accompanied with a significant lag period at the initial stage of reaction. The percentage of dodecameric complex increases with increasing salt concentration. The dodecameric complex has a greatly increased specific activity for the polymerization of (R)-3-hydroxybutyryl-CoA and a negligible lag period. The PHA synthase from Ectothiorhodospira shaposhnikoVii may catalyze a living polymerization and two PhaC and two PhaE subunits may comprise a single catalytic site in the synthase complex, SDS-PAGE Ectothiorhodospira shaposhnikovii

Synonyms

Synonyms Comment Organism
type III PHA synthase
-
Ectothiorhodospira shaposhnikovii

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
122
-
(R)-3-hydroxyvaleryl-CoA based on the assumption that 2 PhaC and 2 PhaE subunits comprise one catalytic site Ectothiorhodospira shaposhnikovii
297
-
4-hydroxybutyryl-CoA based on the assumption that 2 PhaC and 2 PhaE subunits comprise one catalytic site Ectothiorhodospira shaposhnikovii
320
-
(R)-3-hydroxybutyryl-CoA based on the assumption that 2 PhaC and 2 PhaE subunits comprise one catalytic site Ectothiorhodospira shaposhnikovii