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2.3.1.304: poly[(R)-3-hydroxyalkanoate] polymerase

This is an abbreviated version!
For detailed information about poly[(R)-3-hydroxyalkanoate] polymerase, go to the full flat file.

Word Map on EC 2.3.1.304

Reaction

(3R)-3-hydroxyacyl-CoA
+
poly[(R)-3-hydroxyalkanoate]n
=
CoA
 +
poly[(R)-3-hydroxyalkanoate]n+1

Synonyms

BP-M-CPF4, broad-range class I PhaCAc, CLAOCE_21140, CLAOCE_21150, CLAOCE_21150/21140, class I PHA synthase, Class I PhaC, class I PhaCRe, class I PHB synthase, Class I poly(R)-hydroxyalkanoic acid synthase, class I polyhydroxyalkanoate synthase, class I polyhydroxybutyrate synthase, Class I synthase, Class II PHA polymerizing enzyme, class II PHA synthase, Class II PhaC, class II PhaC1, class III PHA synthase, class III PHB synthase, class III polyhydroxyalkanoate synthase, class III polyhydroxybutyrate synthase, class III synthase, class IV PHA synthase, H16_A1437, HPTL0263, HPTL0635, HPTL1376, intracellular polyhydroxyalkanoate synthase, P(3HB) synthase, PHA polymerase, PHA synthase, PHA synthase 1, PHA synthase I, PHA synthase II, PHA synthase III, PhaC, PhaC type II, PhaC-II, PhaC1, PhaC1P-5, PhaC1Pp, PhaC1Ps, PhaC1SG, PhaC2, PhaC2P-5, PhaC2Ps, PhaC2SG, PhaCAc, PhaCAv, phaCBP-M-CPF4, PhaCCc, PhaCCn-CAT, PhaCCs, PhaCCs-CAT, phaCCv, PhaCPhaEAv, PhaCRe, PhaE, PhaEC, PhaECAv, PhaRCBm, PhaRCYB4, PHB synthase, PhbC, PhbCRe, phbC_2, phbE, poly(3-hydroxybutyrate) synthase, poly(hydroxyalkanoic acid) synthase, poly-3-hydroxybutyrate synthase, poly-beta-hydroxybutyrate synthase, polyhydroxyalkanoate (PHA) synthase, polyhydroxyalkanoate synthase, polyhydroxyalkanoate synthase 1, polyhydroxyalkanoate synthase synthase, polyhydroxyalkanoic acids synthase, polyhydroxyalkanoic synthase I, polyhydroxyalkanoic synthase II, polyhydroxyalkanoic synthase III, polyhydroxybutyrate synthase, Q667_12980, TH-1_PHB synthase_HPTL_0263, TH-1_PHB synthase_HPTL_0635, TH-1_PHB synthase_HPTL_1376, type I PHA synthase, type I polyhydroxyalkanoate synthase, type II PHA synthase, type II PhaC1, type II polyhydroxyalkanoate synthase, type II Pseudomonas PHA synthase 1, type III PHA synthase, type-III PHA synthase, YdcS

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.1 Transferring groups other than aminoacyl groups
                2.3.1.304 poly[(R)-3-hydroxyalkanoate] polymerase

Subunits

Subunits on EC 2.3.1.304 - poly[(R)-3-hydroxyalkanoate] polymerase

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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dodecamer
Q9F5P8; Q9F5P9, Q9F5P9
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
hexamer
Q9F5P8; Q9F5P9, Q9F5P9
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
monomer
additional information