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Literature summary extracted from

  • Kawashima, Y.; Cheng, W.; Mifune, J.; Orita, I.; Nakamura, S.; Fukui, T.
    Characterization and functional analyses of R-specific enoyl coenzyme A hydratases in polyhydroxyalkanoate-producing Ralstonia eutropha (2012), Appl. Environ. Microbiol., 78, 493-502.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.2.1.119 overexpression of the three His6-tagged PhaJ4 homologues individually in Escherichia coli strain BL21(DE3) Cupriavidus necator

Protein Variants

EC Number Protein Variants Comment Organism
4.2.1.119 additional information engineered Ralstonia eutropha strains as host strains for PhaJ4aRe to PhaJ4cRe are capable of synthesizing poly((R)-3-hydroxybutyrate-co-(R)-3-hydroxyhexanoate) from soybean oil due to modifications enabling the biosynthesis of P(3HB-co-3HHx) composed of a larger 3HHx fraction without a negative impact on cell growth and PHA production on soybean oil, especially when phaJ4aRe or phaJ4bRe is tandemly introduced with phaJAc from Aeromonas caviae. Introduction of phaJ4aRe or phaJ4bRe into the Ralstonia eutropha strains using a broad-host-range vector enhances the 3HHx composition of the copolyesters, but the introduction of phaJ4cRe does not Cupriavidus necator

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.2.1.119 additional information
-
 additional information kinetic parameters of recombinant PhaJ4aRe to PhaJ4cRe or hydration toward trans-2-enoyl-CoAs of C4 to C8 and comparison to those of PhaJ4Pa and PhaJAc, overview Cupriavidus necator
4.2.1.119 additional information
-
 additional information kinetic parameters of recombinant PhaJ4aRe to PhaJ4cRe or hydration toward trans-2-enoyl-CoAs of C4 to C8 and comparison to those of PhaJ4Pa and PhaJAc, overview Pseudomonas aeruginosa

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.2.1.119 16500
-
 x * 17500, recombinant isozyme His-tagged PhaJ4aRe, SDS-PAGE, x * 17000, recombinant His-tagged PhaJ4bRe, SDS-PAGE, x * 16500, recombinant His-tagged PhaJ4cRe, SDS-PAGE Cupriavidus necator
4.2.1.119 17000
-
 x * 17500, recombinant isozyme His-tagged PhaJ4aRe, SDS-PAGE, x * 17000, recombinant His-tagged PhaJ4bRe, SDS-PAGE, x * 16500, recombinant His-tagged PhaJ4cRe, SDS-PAGE Cupriavidus necator
4.2.1.119 17500
-
 x * 17500, recombinant isozyme His-tagged PhaJ4aRe, SDS-PAGE, x * 17000, recombinant His-tagged PhaJ4bRe, SDS-PAGE, x * 16500, recombinant His-tagged PhaJ4cRe, SDS-PAGE Cupriavidus necator

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.2.1.119 (3R)-3-hydroxyacyl-CoA Cupriavidus necator
-
 (2E)-2-enoyl-CoA + H2O
-
 ?
4.2.1.119 (3R)-3-hydroxyacyl-CoA Pseudomonas aeruginosa
-
 (2E)-2-enoyl-CoA + H2O
-
 ?
4.2.1.119 (3R)-3-hydroxyacyl-CoA Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
 (2E)-2-enoyl-CoA + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.119 Cupriavidus necator
-
 presence of 16 orthologues of R-specific enoyl-CoA hydratase, among which three proteins shares high homologies with the enzyme specific to enoyl-CoAs of medium chain length encoded by phaJ4 from Pseudomonas aeruginosa
-
4.2.1.119 Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
 presence of 16 orthologues of R-specific enoyl-CoA hydratase, among which three proteins shares high homologies with the enzyme specific to enoyl-CoAs of medium chain length encoded by phaJ4 from Pseudomonas aeruginosa
-
4.2.1.119 Pseudomonas aeruginosa Q9HX12 gene phaJ4
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.2.1.119 recombinant His6-tagged PhaJ4 homologues from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Cupriavidus necator

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.119 (3R)-3-hydroxyacyl-CoA
-
 Cupriavidus necator (2E)-2-enoyl-CoA + H2O
-
 ?
4.2.1.119 (3R)-3-hydroxyacyl-CoA
-
 Pseudomonas aeruginosa (2E)-2-enoyl-CoA + H2O
-
 ?
4.2.1.119 (3R)-3-hydroxyacyl-CoA recombinant forms of the three proteins, PhaJ4aRe to PhaJ4cRe, show enoyl-CoA hydratase activity with R specificity, and the catalytic efficiencies are elevated as the substrate chain length increases from C4 to C8. PhaJ4aRe and PhaJ4bRe show over 10fold higher catalytic efficiency than PhaJ4cRe Cupriavidus necator (2E)-2-enoyl-CoA + H2O
-
 ?
4.2.1.119 (3R)-3-hydroxyacyl-CoA
-
 Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1 (2E)-2-enoyl-CoA + H2O
-
 ?
4.2.1.119 (3R)-3-hydroxyacyl-CoA recombinant forms of the three proteins, PhaJ4aRe to PhaJ4cRe, show enoyl-CoA hydratase activity with R specificity, and the catalytic efficiencies are elevated as the substrate chain length increases from C4 to C8. PhaJ4aRe and PhaJ4bRe show over 10fold higher catalytic efficiency than PhaJ4cRe Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1 (2E)-2-enoyl-CoA + H2O
-
 ?
4.2.1.119 additional information engineered Ralstonia eutropha strains as host strains for PhaJ4aRe to PhaJ4cRe are capable of synthesizing poly((R)-3-hydroxybutyrate-co-(R)-3-hydroxyhexanoate) from soybean oil, but only PhaJ4aRe is one of the major enzymes supplying the (R)-3-hydroxyhexanoate-CoA monomer through beta-oxidation, pathway overview Cupriavidus necator ?
-
 ?
4.2.1.119 additional information the enzyme is specific for enoyl-CoAs of medium chain length Pseudomonas aeruginosa ?
-
 ?
4.2.1.119 additional information engineered Ralstonia eutropha strains as host strains for PhaJ4aRe to PhaJ4cRe are capable of synthesizing poly((R)-3-hydroxybutyrate-co-(R)-3-hydroxyhexanoate) from soybean oil, but only PhaJ4aRe is one of the major enzymes supplying the (R)-3-hydroxyhexanoate-CoA monomer through beta-oxidation, pathway overview Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
4.2.1.119 ? x * 17500, recombinant isozyme His-tagged PhaJ4aRe, SDS-PAGE, x * 17000, recombinant His-tagged PhaJ4bRe, SDS-PAGE, x * 16500, recombinant His-tagged PhaJ4cRe, SDS-PAGE Cupriavidus necator

Synonyms

EC Number Synonyms Comment Organism
4.2.1.119 PhaJ4
-
 Pseudomonas aeruginosa
4.2.1.119 PhaJ4aRe
-
 Cupriavidus necator
4.2.1.119 PhaJ4bRe
-
 Cupriavidus necator
4.2.1.119 PhaJ4cRe
-
 Cupriavidus necator
4.2.1.119 R-specific enoyl coenzyme A hydratase
-
 Cupriavidus necator
4.2.1.119 R-specific enoyl coenzyme A hydratase
-
 Pseudomonas aeruginosa
4.2.1.119 R-specific enoyl-CoA hydratase
-
 Cupriavidus necator
4.2.1.119 R-specific enoyl-CoA hydratase
-
 Pseudomonas aeruginosa

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.2.1.119 30
-
 assay at Cupriavidus necator
4.2.1.119 30
-
 assay at Pseudomonas aeruginosa

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.2.1.119 7.5
-
 assay at Cupriavidus necator
4.2.1.119 7.5
-
 assay at Pseudomonas aeruginosa

General Information

EC Number General Information Comment Organism
4.2.1.119 evolution phylogenetic tree of MaoC-like domains in PhaJ homologues encoded in Ralstonia eutropha H16 genome and domains in the known PhaJ proteins from Aeromonas caviae and Pseudomonas aeruginosa Cupriavidus necator
4.2.1.119 evolution phylogenetic tree of MaoC-like domains in PhaJ homologues encoded in Ralstonia eutropha H16 genome and domains in the known PhaJ proteins from Aeromonas caviae and Pseudomonas aeruginosa Pseudomonas aeruginosa
4.2.1.119 malfunction deletion of phaJ4aRe from the chromosome results in significant decrease of (R)-3-hydroxyhexanoate composition in the accumulated copolyester, whereas no change is observed with deletion of phaJ4bRe or phaJ4cRe Cupriavidus necator