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Literature summary extracted from

  • Miyahara, Y.; Hiroe, A.; Tsuge, T.; Taguchi, S.
    Microbial secretion platform for 3-hydroxybutyrate oligomer and its end-capped forms using chain transfer reaction-mediated polyhydroxyalkanoate synthases (2019), Biotechnol. J., 14, e1900201 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.304 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 Aeromonas caviae
2.3.1.304 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 Allochromatium vinosum
2.3.1.304 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 Bacillus cereus
2.3.1.304 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 Priestia megaterium
2.3.1.304 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 Bacillus sp. INT005
2.3.1.304 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 Cupriavidus necator
2.3.1.304 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 Delftia acidovorans

Protein Variants

EC Number Protein Variants Comment Organism
2.3.1.304 additional information establishment of Escherichia coli as a microbial secretion platform for 3-hydroxybutyrate oligomer and its end-capped forms using chain transfer reaction-mediated polyhydroxyalkanoate synthases, overview Bacillus cereus
2.3.1.304 additional information establishment of Escherichia coli as a microbial secretion platform for 3-hydroxybutyrate oligomer and its end-capped forms using chain transfer reaction-mediated polyhydroxyalkanoate synthases, overview Cupriavidus necator
2.3.1.304 additional information establishment of Escherichia coli as a microbial secretion platform for 3-hydroxybutyrate oligomer and its end-capped forms using chain transfer reaction-mediated polyhydroxyalkanoate synthases, overview Delftia acidovorans
2.3.1.304 additional information establishment of Escherichia coli as a microbial secretion platform for 3-hydroxybutyrate oligomer and its end-capped forms using chain transfer reaction-mediated polyhydroxyalkanoate synthases, overview Allochromatium vinosum
2.3.1.304 additional information establishment of Escherichia coli as a microbial secretion platform for 3-hydroxybutyrate oligomer and its end-capped forms using chain transfer reaction-mediated polyhydroxyalkanoate synthases, overview Bacillus sp. INT005
2.3.1.304 additional information establishment of Escherichia coli as a microbial secretion platform for 3-hydroxybutyrate oligomer and its end-capped forms using chain transfer reaction-mediated polyhydroxyalkanoate synthases, overview Priestia megaterium
2.3.1.304 additional information establishment of Escherichia coli as a microbial secretion platform for 3-hydroxybutyrate oligomer and its end-capped forms using chain transfer reaction-mediated polyhydroxyalkanoate synthases, overview Aeromonas caviae

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.304 Aeromonas caviae O32471
-
-
2.3.1.304 Allochromatium vinosum P45370
-
-
2.3.1.304 Bacillus cereus D2Z0B8
-
-
2.3.1.304 Bacillus sp. INT005 Q8GI81
-
-
2.3.1.304 Cupriavidus necator P23608 i.e. Ralstonia eutropha
-
2.3.1.304 Cupriavidus necator ATCC 17699 P23608 i.e. Ralstonia eutropha
-
2.3.1.304 Cupriavidus necator DSM 428 P23608 i.e. Ralstonia eutropha
-
2.3.1.304 Cupriavidus necator Stanier 337 P23608 i.e. Ralstonia eutropha
-
2.3.1.304 Delftia acidovorans O87110 i.e. Pseudomonas acidovorans
-
2.3.1.304 Priestia megaterium Q9ZF92
-
-

Synonyms

EC Number Synonyms Comment Organism
2.3.1.304 PHA synthase
-
 Bacillus cereus
2.3.1.304 PHA synthase
-
 Cupriavidus necator
2.3.1.304 PHA synthase
-
 Delftia acidovorans
2.3.1.304 PHA synthase
-
 Allochromatium vinosum
2.3.1.304 PHA synthase
-
 Bacillus sp. INT005
2.3.1.304 PHA synthase
-
 Priestia megaterium
2.3.1.304 PHA synthase
-
 Aeromonas caviae
2.3.1.304 polyhydroxyalkanoate synthase
-
 Bacillus cereus
2.3.1.304 polyhydroxyalkanoate synthase
-
 Cupriavidus necator
2.3.1.304 polyhydroxyalkanoate synthase
-
 Delftia acidovorans
2.3.1.304 polyhydroxyalkanoate synthase
-
 Allochromatium vinosum
2.3.1.304 polyhydroxyalkanoate synthase
-
 Bacillus sp. INT005
2.3.1.304 polyhydroxyalkanoate synthase
-
 Priestia megaterium
2.3.1.304 polyhydroxyalkanoate synthase
-
 Aeromonas caviae

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.1.304 30
-
 in vivo assay at Bacillus cereus
2.3.1.304 30
-
 in vivo assay at Cupriavidus necator
2.3.1.304 30
-
 in vivo assay at Delftia acidovorans
2.3.1.304 30
-
 in vivo assay at Allochromatium vinosum
2.3.1.304 30
-
 in vivo assay at Bacillus sp. INT005
2.3.1.304 30
-
 in vivo assay at Priestia megaterium
2.3.1.304 30
-
 in vivo assay at Aeromonas caviae