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Literature summary extracted from

  • Sudo, M.; Hori, C.; Ooi, T.; Mizuno, S.; Tsuge, T.; Matsumoto, K.
    Synergy of valine and threonine supplementation on poly(2-hydroxybutyrate-block-3-hydroxybutyrate) synthesis in engineered Escherichia coli expressing chimeric polyhydroxyalkanoate synthase (2020), J. Biosci. Bioeng., 129, 302-306 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.304 gene phaC, recombinant expression of the chimeric mutant enzyme PhaCAR in Escherichia coli Cupriavidus necator
2.3.1.304 gene phaC, recombinant expression of the chimeric mutant enzyme PhaCAR in Escherichia coli Aeromonas caviae

Protein Variants

EC Number Protein Variants Comment Organism
2.3.1.304 additional information engineering of a chimeric polyhydroxyalkanoate (PHA) synthase PhaCAR is composed of N-terminal portion of Aeromonas caviae PHA synthase and C-terminal portion of Ralstonia eutropha (Cupriavidus necator) PHA synthase. PhaCAR has a unique and useful capacity to synthesize the block PHA copolymer poly(2-hydroxybutyrate-block-3-hydroxybutyrate) [P(2HB-beta-3HB)] in engineered Escherichia coli from exogenous 2HB and 3HB. Synergy of valine and threonine supplementation on poly(2-hydroxybutyrate-block-3-hydroxybutyrate) synthesis in engineered Escherichia coli expressing chimeric polyhydroxyalkanoate synthase, overview. Incorporate the amino acid-derived 2-hydroxyalkanoate (2HA) units using PhaCAR and the 2HA-CoA-supplying enzymes lactate dehydrogenase (LdhA) and CoA transferase (HadA). Cells harboring the genes for PhaCAR, LdhA, and HadA, as well as for the 3HB-CoA-supplying enzymes beta-ketothiolase and acetoacetyl-CoA reductase, are cultivated with supplementation of four hydrophobic amino acids, i.e. leucine, valine, isoleucine, and phenylalanine, in the medium. No hydrophobic amino acid-derived monomers are incorporated into the polymer, which is most likely because of the strict substrate specificity of PhaCAR, except for P(2HB-co-3HB) which is produced with Val supplementation. The copolymer is likely P(2HB-beta-3HB) based on proton nuclear magnetic resonance analysis. Dual supplementation with Thr and Val shows synergy on the 2HB fraction of the polymer. Val supplementation promotes the 2HB synthesis likely by inhibiting the metabolism of 2-oxobutyrate into Ile and/or activating Thr dehydratase. PhaCAR spontaneously synthesizes poly(2HB-block-3-hydroxybutyrate) [P(2HB-beta-3HB)] from the mixture of 2HB and 3HB supplemented in the medium. Poly(2-hydroxybutyrate-block-3-hydroxybutyrate) [P(2HA-beta-3HB)] biosynthesis pathways from threonine in engineered Escherichia coli and proposed role of valine, overview Cupriavidus necator
2.3.1.304 additional information engineering of a chimeric polyhydroxyalkanoate (PHA) synthase PhaCAR is composed of N-terminal portion of Aeromonas caviae PHA synthase and C-terminal portion of Ralstonia eutropha (Cupriavidus necator) PHA synthase. PhaCAR has a unique and useful capacity to synthesize the block PHA copolymer poly(2-hydroxybutyrate-block-3-hydroxybutyrate) [P(2HB-beta-3HB)] in engineered Escherichia coli from exogenous 2HB and 3HB. Synergy of valine and threonine supplementation on poly(2-hydroxybutyrate-block-3-hydroxybutyrate) synthesis in engineered Escherichia coli expressing chimeric polyhydroxyalkanoate synthase, overview. Incorporate the amino acid-derived 2-hydroxyalkanoate (2HA) units using PhaCAR and the 2HA-CoA-supplying enzymes lactate dehydrogenase (LdhA) and CoA transferase (HadA). Cells harboring the genes for PhaCAR, LdhA, and HadA, as well as for the 3HB-CoA-supplying enzymes beta-ketothiolase and acetoacetyl-CoA reductase, are cultivated with supplementation of four hydrophobic amino acids, i.e. leucine, valine, isoleucine, and phenylalanine, in the medium. No hydrophobic amino acid-derived monomers are incorporated into the polymer, which is most likely because of the strict substrate specificity of PhaCAR, except for P(2HB-co-3HB) which is produced with Val supplementation. The copolymer is likely P(2HB-beta-3HB) based on proton nuclear magnetic resonance analysis. Dual supplementation with Thr and Val shows synergy on the 2HB fraction of the polymer. Valine supplementation promotes the 2HB synthesis likely by inhibiting the metabolism of 2-oxobutyrate into Ile and/or activating Thr dehydratase. PhaCAR spontaneously synthesizes poly(2HB-block-3-hydroxybutyrate) [P(2HB-beta-3HB)] from the mixture of 2HB and 3HB supplemented in the medium. Poly(2-hydroxybutyrate-block-3-hydroxybutyrate) [P(2HA-beta-3HB)] biosynthesis pathways from threonine in engineered Escherichia coli and proposed role of valine, overview Aeromonas caviae

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.304 Aeromonas caviae O32471
-
-
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
-

Synonyms

EC Number Synonyms Comment Organism
2.3.1.304 PHA synthase
-
 Cupriavidus necator
2.3.1.304 PHA synthase
-
 Aeromonas caviae
2.3.1.304 PhaC
-
 Cupriavidus necator
2.3.1.304 PhaC
-
 Aeromonas caviae
2.3.1.304 PhaCAc
-
 Aeromonas caviae
2.3.1.304 PhaCRe
-
 Cupriavidus necator
2.3.1.304 polyhydroxyalkanoate synthase
-
 Cupriavidus necator
2.3.1.304 polyhydroxyalkanoate synthase
-
 Aeromonas caviae