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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

Cloned

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

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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
28 strains belonging to 15 genera in the family Halobacteriaceae, sequence comparisons, phylogenetic analysis, overview
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a central region of the phaC gene of Cyanothece sp. strain PCC 8303 is cloned, sequenced and heterologously expressed in Escherichia coli
a synthetic operon for polyhydroxyalkanoate biosynthesis designed to yield high levels of PHA synthase activity in vivo is constructed by positioning a genetic fragment encoding beta-ketothiolase and acetoacetyl-CoA reductase behind a modified synthase gene containing an Escherichia coli promoter and ribosome binding site. Plasmids containing the synthetic operon and the native Alcaligenes eutrophus PHA operon are transformed into Escherichia DH5 alpha and analyzed for polyhydroxybutyrate production. The molecular weight of polymer isolated from recombinant Escherichia coli containing the modified synthase construct is lower than that of the polymer from Escherichia coli containing the native Alcaligenes eutrophus operon. A further decrease in polyester molecular weight is observed with increased induction of the PHA biosynthetic genes in the synthetic operon. Comparison of the enzyme activity levels of PHA biosynthetic enzymes in a strain encoding the native operon with a strain possessing the synthetic operon indicates that the amount of polyhydroxyalkanoate synthase in a host organism plays a key role in controlling the molecular weight and the polydispersity of polymer
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BP-M-CPF4, DNA and amino acid sequence determination and analysis, functional assessment by in vivo PHA biosynthesis in a PHA-negative mutant, recombinant expression in the PHA-negative mutant of Cupriavidus necator under control of phaC1 promoter from Cupriavidus necator, subcloning in Escherichia coli
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cloning from the PHAC cluster, DNA and amino acid sequence determination and analysis, phylogenetic analysis, genotyping
cloning from the PHAC cluster, DNA and amino acid sequence determination and analysis, phylogenetic analysis, genotyping, functional recombinant heterologous expression in the PHA-negative mutant of Cupriavidus necator PHB-4
cloning from the PHAC cluster, DNA and amino acid sequence determination and analysis, phylogenetic analysis, genotyping, recombinant expression in the PHA-negative mutant of Cupriavidus necator PHB-4 shows that the enzyme is not functional
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cloning from the PHAC cluster, DNA and amino acid sequence determination and analysis, phylogenetic analysis, genotyping, recombinant heterologous expression in the PHA-negative mutant of Cupriavidus necator PHB-4. PHB-4/pBBR1-ProCnJ60 accumulates 18.7% of wild-type polyhydroxybutyrate
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cloning of the gene cluster (phaECHme) encoding a polyhydroxyalkanoate (PHA) synthase in Haloferax mediterranei CGMCC 1.2087 via thermal asymmetric interlaced PCR
I3R9Z3; I3R9Z4
co-expressed with the NADPH-dependent acetoacetyl-CoA reductase gene from Ralstonia eutropha in Arabidopsis thaliana
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co-expression of PhaC with acetoacetyl-CoA synthetase, AACS, from Streptomyces sp. CL190 in Escherichia coli and Corynebacterium glutamicum leading to enhanced production of polyhydroxybutanoates, by cloning the AACS gene into the phaABC operon of Ralstonia eutropha
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construction of (His)6-tagged Ralstonia eutropha PHA synthase gene, expression in Escherichia coli
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construction of a recombinant Ralstonia eutropha PHB-4 harboring Aeromonas caviae biosynthesis genes under the control of a promoter for Ralstonia eutropha phb operon (phbRe promoter), and examination of the polyhydroxyalkanoate producing ability of the recombinants from various alkanoic acids as carbon sources. The polymerization step is not the rate-determining one in PHA biosynthesis by Ralstonia eutropha. The molecular weights of poly(3-hydroxybutyrate) produced by the recombinant strains are also independent of the levels of PHA synthase activity
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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
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constructs of phaCDm alone (pBBRMCS-2::phaCDm) and of phaEDmCDm (pBBRMCS-2::phaEDmCDm) in various vectors are obtained and transferred to several strains of Escherichia coli, as well as to the PHA-negative mutants PHB-4 and GPp104 of Ralstonia eutropha and Pseudomonas putida, respectively. In cells of the recombinant strains harboring phaEDmCDm small but significant amounts (up to 1.7% of cell dry matter) of poly(3-hydroxybutyrate) and of PHA synthase activity (up to 1.5 U/mg protein) are detected. Hybrid synthases consisting of PhaCDm and PhaE of Thiococcus pfennigii or Synechocystis sp. strain PCC 6308 are also constructed and are shown to be functionally active
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each subunit was cloned, expressed, and purified as a (His)6-tagged construct
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entire PHA synthase structural gene of Chlorogloeopsis fritschii PCC 6912 is cloned, sequenced and heterologously expressed in Escherichia coli
entire PHA synthase structural gene of Synechococcus sp. strain MA19 is cloned, sequenced and heterologously expressed in Escherichia coli
enzyme PhaCCc, recombinant expression
enzyme PhaECAv, recombinant expression
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expressed in a PHA-negative mutant of Pseudomonas putida
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expressed in Burkholderia sp. USM (JCM15050)
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expressed in Cupriavidus necator PHB-4
Burkholderia sp. USM (JCM 15050)
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expressed in Cupriavidus necator strain PHB-4
expressed in Cupriavidus necator strains PHB-4, Re2058 and Re2160 and Escherichia coli Rosetta2 (DE3) cells
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expressed in Escherichia coli
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expressed in Escherichia coli JM109 and BL21(DE3) cells
expressed in Escherichia coli JM109 cells
expressed in Escherichia coli Rosetta 2 (DE3) cells
expressed in Escherichia coli S17-1 cells
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expressed in polyhydroxyalkanoate synthase negative Aeromonas hydrophila mutant CQ4
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expressed in Ralstonia eutropha PHB-4
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expression in Escherichia coli
expression in Pseudomonas putida GPp104 PHA mutant
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expression of PhaRCBm, and as hybrid enzyme PhaRYB4CBm with Bacillus cereus YB-4, PhaRCYB4 in Escherichia coli JM109
expression of PhaRCYB4, and as hybrid enzyme PhaRYB4CBm with Bacillus megaterium NBRC15308, PhaRCBm in Escherichia coli JM109
expression of wild-type and mutant enzymes in Escherichai coli altering its content of polyhydroxyalkanoates
-
expression of wild-type and mutant enzymes in Escherichia coli altering its content of polyhydroxyalkanoates
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exypression in Escherichia coli
gene phaC
gene phaC (H16_A1437)
gene phaC, recombinant expression in Escherichia coli strain BW25113 and in its mutant variant BW25113 DELTAadhE, a alcohol dehydrogenase-deficient mutant strain. The heterologous expression of Aeromonas caviae Pha synthase leads to a high secretory production of 3-hydroxybutyrate and a large amount of 3-hydroxybutyrate oligomers in relation to 3-hydroxybutyrate monomers in the wild-type and mutant BW25113 strains. 3HBOs are secreted by the recombinant BW25113 and BW25113 DELTAadhE strains
gene phaC, recombinant expression in Escherichia coli strain BW25113 and in its mutant variant BW25113 DELTAadhE, a alcohol dehydrogenase-deficient mutant strain. The heterologous expression of Allochromatium vinosum Pha synthase leads to a veryl low secretory production of 3-hydroxybutyrate and a moderate amount of 3-hydroxybutyrate oligomers in relation to 3-hydroxybutyrate monomers in the wild-type BW25113 strain. In the mutant BW25113 strain, the relative amount of oligomers is reduced compared to wild-type. 3HBOs are secreted by the recombinant BW25113 and BW25113 DELTAadhE strains
gene phaC, recombinant expression in Escherichia coli strain BW25113 and in its mutant variant BW25113 DELTAadhE, a alcohol dehydrogenase-deficient mutant strain. The heterologous expression of Bacillus cereus Pha synthase leads to a moderate secretory production of 3-hydroxybutyrate and a large amount of 3-hydroxybutyrate oligomers in relation to 3-hydroxybutyrate monomers in the wild-type and mutant BW25113 strains. 3HBOs are secreted by the recombinant BW25113 and BW25113 DELTAadhE strains
gene phaC, recombinant expression in Escherichia coli strain BW25113 and in its mutant variant BW25113 DELTAadhE, a alcohol dehydrogenase-deficient mutant strain. The heterologous expression of Bacillus megaterium Pha synthase leads to a moderate secretory production of 3-hydroxybutyrate and a very low amount of 3-hydroxybutyrate oligomers in relation to 3-hydroxybutyrate monomers in the wild-type BW25113 strain. In the mutant BW25113 strain, no oligomers are produced. 3HBOs are secreted by the recombinant BW25113 and BW25113 DELTAadhE strains
gene phaC, recombinant expression in Escherichia coli strain BW25113 and in its mutant variant BW25113 DELTAadhE, a alcohol dehydrogenase-deficient mutant strain. The heterologous expression of Bacillus sp. INT005 Pha synthase leads to a low secretory production of 3-hydroxybutyrate, but a large amount of 3-hydroxybutyrate oligomers in relation to 3-hydroxybutyrate monomers in the wild-type and mutant BW25113 strains. 3HBOs are secreted by the recombinant BW25113 and BW25113 DELTAadhE strains
gene phaC, recombinant expression in Escherichia coli strain BW25113 and in its mutant variant BW25113 DELTAadhE, a alcohol dehydrogenase-deficient mutant strain. The heterologous expression of Cupriavidus necator Pha synthase leads to very lo secretory production and a very low amount of 3-hydroxybutyrate oligomers in relation to 3-hydroxybutyrate monomers in the wild-type and mutant BW25113 strains. 3HBOs are secreted by the recombinant BW25113 and BW25113 DELTAadhE strains
gene phaC, recombinant expression in Escherichia coli strain BW25113 and in its mutant variant BW25113 DELTAadhE, a alcohol dehydrogenase-deficient mutant strain. The heterologous expression of Delftia acidovorans Pha synthase leads to a low secretory production of 3-hydroxybutyrate and a very large amount of 3-hydroxybutyrate oligomers in relation to 3-hydroxybutyrate monomers in the wild-type and mutant BW25113 strains. 3HBOs are secreted by the recombinant BW25113 and BW25113 DELTAadhE strains
gene phaC, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
gene phaC, recombinant expression of the chimeric mutant enzyme PhaCAR in Escherichia coli
gene phaC, sequence comparisons, phylogenetic analysis
gene phaC1Ps6-19 phylogenetic analysis, expression of phaC1Ps6-19 mutants in Escherichia coli strain XL-1 Blue
gene phaC1Ps6-19, DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression of mutant E130D/S325T/S477G/Q481K in Escherichia coli strain XL-1 Blue
gene phaCUSMAA2-4, DNA and amino acid sequence determination and analysis, expression in and complementation of mutant Cupriavidus necator PHB-4 deficient in PHA synthesis, expression in Escherichia coli strain S17-1
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gene PhaEC, sequence comparisons, construction of a plasmid with genes encoding thiolase A (thlA), 3-hydroxybutyryl-CoA dehydrogenase (hbd), and crotonase (crt) from Clostridium scatologenes strain ATCC 25775 and (R)-enoyl-CoA hydratase (phaJ) and PHA synthase (phaEC) from Clostridium acetireducens strain DSM 10703 under control of promoter Ppta-ack from Clostridium ljungdahlii strain DSM 13583 into pMTL83151 Clostridium-Escherichia coli shuttle plasmid. The clustered genes thlA, hbd, and crt are initially cloned into pMTL83151, together with Ppta-ack promoter, recombinant expression in Escherichia coli
A0A1E8EW93; A0A1E8EW64
gene phbCPs encoded in the phb operon, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, the genetic organization of phb operon shows a putative promoter region, followed by phbBPs-phbAPs-phbCPs, with phbRPs encoding a putative transcriptional activator that is located in the opposite orientation, upstream of phbBACPs. Heterologous expression of phbCPs from pGEM3ABex vector in Escherichia coli JM109 resulting in P(3HB) accumulation of up to 40% of dry cell weight
in vivo studies on a Wautersia eutropha strain in which the class I synthase gene has been replaced with the D302A-PhaCPhaE gene and the organism examined under PHB production conditions by transmission electron microscopy. Very small granules are observed in contrast to the 200-500 nm granules observed with the wild-type strain
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isoform PhaC2 is expressed in Escherichia coli LS1298 cells
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mutant enzymes expressed in Escherichia coli
PHA synthase genes (phaC and phaE) are cloned by screening a genomic library for PHA accumulation in Escherichia coli cells
Q9F5P8; Q9F5P9, Q9F5P9
recombinant Escherichia coli strain JM109 harboring the E130D mutant gene accumulates 10fold higher (1.0 wt%) poly(3-hydroxybutyrate) from glucose, compared to recombinant Escherichia coli harboring the wild-type PHA synthase gene (0.1 wt%). Recombinant Escherichia coli strain LS5218 harboring the E130D PHA synthase gene grown on dodecanoate produces more poly(3-hydroxybutanoate-co-3-hydroxyalkanoate) (20 wt%) copolymer than an LS5218 strain harboring the wild-type PHA synthase gene (13 wt%). The E130D mutation also results in the production of copolymer with a slight increase in 3-hydroxybutanoate composition, compared to copolymer produced by the wild-type PHA synthase
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recombinant expression of His-tagged PhaC1Pp in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha
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recombinant expression of His-tagged PhaECAv in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha
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recombinant expression of PhaC1P-5 in Pseudomonas putida strain Gp104
recombinant expression of PhaC2P-5 in Pseudomonas putida strain Gp104 or in Ralstonia eutropha strain PHB-4
recombinant expression of the enzyme used as a fusion protein with a self-cleaving intein linker for production of the fused proteins, e.g. Aequorea victoria green fluorescent protein (GFP), Mycobacterium tuberculosis vaccine candidate Rv1626, the immunoglobulin G (IgG) binding ZZ domain of protein A derived from Staphylococcus aureus, human tumor necrosis factor alpha (TNFalpha), human granulocyte colony-stimulating factor (G-CSF), and human interferon alpha 2beta (IFNalpha2beta) in the Escherichia coli system. A pH or thiol inducible intein is employed in combination with PHA beads for target protein production and purification, method evaluation, overview
the phaC coding region is subcloned into vector pBBR1-JO2 under lac promoter control. The resulting plasmid, pQQ4, mediates PHB accumulation in the mutant Ralstonia eutropha PHBN4 and recombinant Escherichia coli JM109(pBHR69)
the wild-type and mutated PHA synthase genes from Aeromonas caviae are introduced into Arabidopsis thaliana together with the NADPH-dependentacetoacetyl-CoA reductase gene from Ralstonia eutropha. Expression of the highly active mutated PHA synthase genes, N149S and D171G, leads to an 8-10fold increase in PHA content in the T1 transgenic Arabidopsis, compared to plants harboring the wild-type PHA synthase gene. In homozygous T2 progenies, PHA content is further increased up to 6.1 mg/g cell dry weight. GC/MS analysis of the purified PHA from the transformants revealed that these PHAs are poly(3-hydroxybutyrate-co-3-hydroxyvalerate) copolymers consisting of 0.2-0.8 mol% 3-hydroxyvalerate
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While Chromobacterium violaceum accumulates poly(3-hydroxybutyrate) or poly(3-hydroxybutyrate-co-3-hydroxyvalerate) when grown on a fatty acid carbon source, Klebsiella aerogenes and Ralstonia eutropha (formerly Alcaligenes eutrophus), harboring phaCCv, accumulate poly(3-hydroxybutyrate) or poly(3-hydroxybutyrate-co-3-hydroxyvalerate) and, additionally, poly(3-hydroxybutyrate-co-3-hydroxyhexanoate) when even-chain-length fatty acids are utilized as the carbon source. This finding suggests that the metabolic environments of these organisms are sufficiently different to alter the product range of the Chromobacterium violaceum PHA synthase. Neither recombinant Escherichia coli nor recombinant Pseudomonas putida harboring phaCCv accumulate significant levels of polyhydroxyalkanoic acids
wild-type and (His)6-tagged PhaCRe, expression in Escherichia coli. Wild-type enzyme expressed in Escherichia coli shows 35% of the enzyme from Ralstonia eutropha
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