Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Tsuge, T.; Sato, S.; Hiroe, A.; Ishizuka, K.; Kanazawa, H.; Shiro, Y.; Hisano, T.
    Contribution of the distal pocket residue to the acyl-chain-length specificity of (R)-specific enoyl-coenzyme A hydratases from Pseudomonas spp. (2015), Appl. Environ. Microbiol., 81, 8076-8083 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.2.1.119 gene phaJ1, sequence comparison, recombinant expression of wild-type and mutant enzymes in Escherichia coli strains DH5alpha or JM109, and LS5218, overexpression of the enzyme in Escherichia coli strain BL21(DE3) Pseudomonas aeruginosa
4.2.1.119 gene phaJ1, sequence comparison, recombinant expression of wild-type and mutant enzymes in Escherichia coli strains DH5alpha or JM109, and LS5218, overexpression of the enzyme in Escherichia coli strain BL21(DE3) Pseudomonas putida

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.2.1.119 homology modeling of strcuture. In the acyl-chain binding pocket, the amino acid at position 72 is the only difference between the two structures of Pseudomonas aeruginosa and Pseudomonas putida isoforms Pseudomonas aeruginosa
4.2.1.119 homology modeling of strcuture. In the acyl-chain binding pocket, the amino acid at position 72 is the only difference between the two structures of Pseudomonas aeruginosa and Pseudomonas putida isoforms Pseudomonas putida
4.2.1.119 purified recombinant enzyme PhaJ1Pa, sitting drop vapor diffusion, mixing of 10 mg/ml protein in 20 mM Tris-HCl, pH 7.5, with mother liquor containing 15 to 20% w/v PEG 3350, 20% v/v glycerol, and 0.1 M bis-Tris, pH 6.0-6.5, X-ray diffraction structure determination and analysis at 1.7 A resolution Pseudomonas aeruginosa

Protein Variants

EC Number Protein Variants Comment Organism
4.2.1.119 I72V site-directed mutagenesis, the mutant has an increased preference for enoyl-CoAs with longer chain lengths compared to wild-type broadening the substrate specificity range, PHA accumulation in recombinant Escherichia coli LS5218 harboring parental or Val72/Ile72 mutant genes of phaJ1, overview Pseudomonas aeruginosa
4.2.1.119 additional information construction of three chimeric PhaJ1 enzymes, composed from Pseudomonas aeruginosa and Pseudomonas putida isoforms. All chimera show significant hydratase activity, and their substrate preferences is within the range exhibited by the parental PhaJ1 enzymes Pseudomonas aeruginosa
4.2.1.119 additional information construction of three chimeric PhaJ1 enzymes, composed from Pseudomonas aeruginosa and Pseudomonas putida isoforms. All chimera show significant hydratase activity, and their substrate preferences is within the range exhibited by the parental PhaJ1 enzymes Pseudomonas putida
4.2.1.119 additional information construction of three chimeric PhaJ1 enzymes, composed from the enzymes from Pseudomonas putida and Pseudomonas aeruginosa, PhaJ1Pp and PhaJ1Pa. All mutants show significant hydratase activity, and their substrate preferences are within the range exhibited by the parental PhaJ1 enzymes Pseudomonas aeruginosa
4.2.1.119 additional information construction of three chimeric PhaJ1 enzymes, composed from the enzymes from Pseudomonas putida and Pseudomonas aeruginosa, PhaJ1Pp and PhaJ1Pa. All mutants show significant hydratase activity, and their substrate preferences are within the range exhibited by the parental PhaJ1 enzymes Pseudomonas putida
4.2.1.119 V72I site-directed mutagenesis, the mutant has an increased preference for enoyl-coenzyme A (CoA) elements with shorter chain lengths compared to wild-type narrowing the substrate specificity range, PHA accumulation in recombinant Escherichia coli LS5218 harboring parental or Val72/Ile72 mutant genes of phaJ1, overview Pseudomonas putida

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.2.1.119 (2E)-2-enoyl-CoA + H2O Pseudomonas aeruginosa
-
 (3R)-3-hydroxyacyl-CoA
-
 r
4.2.1.119 (2E)-2-enoyl-CoA + H2O Pseudomonas putida
-
 (3R)-3-hydroxyacyl-CoA
-
 r

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.119 Pseudomonas aeruginosa Q9LBK2
-
-
4.2.1.119 Pseudomonas putida A0A177YY42
-
-
4.2.1.119 Pseudomonas putida E9P3X9
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.2.1.119 recombinant wild-type and mutant enzymes from Escherichia coli strain Bl21(DE3) Pseudomonas aeruginosa
4.2.1.119 recombinant wild-type and mutant enzymes from Escherichia coli strain Bl21(DE3) Pseudomonas putida

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.119 (2E)-2-enoyl-CoA + H2O
-
 Pseudomonas aeruginosa (3R)-3-hydroxyacyl-CoA
-
 r
4.2.1.119 (2E)-2-enoyl-CoA + H2O
-
 Pseudomonas putida (3R)-3-hydroxyacyl-CoA
-
 r
4.2.1.119 (2E)-crotonyl-CoA + H2O
-
 Pseudomonas aeruginosa (3R)-3-hydroxybutanoyl-CoA
-
 r
4.2.1.119 (2E)-crotonyl-CoA + H2O
-
 Pseudomonas putida (3R)-3-hydroxybutanoyl-CoA
-
 r
4.2.1.119 (2E)-oct-2-enoyl-CoA + H2O
-
 Pseudomonas aeruginosa (R)-3-hydroxyoctanoyl-CoA
-
 r
4.2.1.119 (2E)-oct-2-enoyl-CoA + H2O
-
 Pseudomonas putida (R)-3-hydroxyoctanoyl-CoA
-
 r
4.2.1.119 additional information chain-length specificity of PhaJ1 is determined mainly by the bulkiness of the amino acid residue at position 72, but other factors, such as structural fluctuations, also affect specificity Pseudomonas aeruginosa ?
-
 ?
4.2.1.119 additional information chain-length specificity of PhaJ1 is determined mainly by the bulkiness of the amino acid residue at position 72, but other factors, such as structural fluctuations, also affect specificity Pseudomonas putida ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.2.1.119 (R)-specific enoyl-coenzyme A hydratase
-
 Pseudomonas aeruginosa
4.2.1.119 (R)-specific enoyl-coenzyme A hydratase
-
 Pseudomonas putida
4.2.1.119 PhaJ1
-
 Pseudomonas aeruginosa
4.2.1.119 PhaJ1
-
 Pseudomonas putida
4.2.1.119 PhaJ1Pa
-
 Pseudomonas aeruginosa
4.2.1.119 PhaJ1Pp
-
 Pseudomonas putida

Temperature Optimum [°C]

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

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.2.1.119 8
-
 assay at Pseudomonas aeruginosa
4.2.1.119 8
-
 assay at Pseudomonas putida

General Information

EC Number General Information Comment Organism
4.2.1.119 additional information contribution of the distal pocket residue to the acyl-chain-length specificity of (R)-specific enoyl-coenzyme A hydratases from Pseudomonas spp., enzyme structure homology modeling, structure comparisons of the enzymes from Pseudomonas putida and Pseudomonas aeruginosa, PhaJ1Pp and PhaJ1Pa, overview Pseudomonas putida
4.2.1.119 additional information contribution of the distal pocket residue to the acyl-chain-length specificity of (R)-specific enoyl-coenzyme A hydratases from Pseudomonas spp., enzyme structure homology modeling, structure comparisons of the enzymes from Pseudomonas putida and Pseudomonas aeruginosa, PhaJ1Pp and PhaJ1Pa, overview. Active site and acyl-chain-binding pocket structure Pseudomonas aeruginosa
4.2.1.119 physiological function (R)-specific enoyl-coenzyme A (enoyl-CoA) hydratases (PhaJs) are capable of supplying monomers from fatty acid beta-oxidation to polyhydroxyalkanoate (PHA) biosynthesis. PhaJ1Pp from Pseudomonas putida shows a broader substrate specificity Pseudomonas aeruginosa
4.2.1.119 physiological function (R)-specific enoyl-coenzyme A (enoyl-CoA) hydratases (PhaJs) are capable of supplying monomers from fatty acid beta-oxidation to polyhydroxyalkanoate (PHA) biosynthesis. PhaJ1Pp from Pseudomonas putida shows a broader substrate specificity Pseudomonas putida
4.2.1.119 physiological function comparison of the enzymes from Pseudomonas putida with residue 72Val resulting in increased preference for enoyl-coenzyme A substrates with shorter chain lengths and Pseudomonas aeruginosa with residue 72Ile resulting in an increased preference for enoyl-CoAs with longer chain lengths Pseudomonas putida
4.2.1.119 physiological function comparison of the enzymes from Pseudomonas putida with residue Val72 resulting in increased preference for enoyl-coenzyme A substrates with shorter chain lengths and Pseudomonas aeruginosa with residue Ile72 resulting in an increased preference for enoyl-CoAs with longer chain lengths Pseudomonas aeruginosa