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Literature summary for 5.3.99.3 extracted from

  • Yamamoto, K.; Suzuki, M.; Higashiura, A.; Aritake, K.; Urade, Y.; Uodome, N.; Hossain, T.; Nakagawa, A.
    New insights into the catalytic mechanism of Bombyx mori prostaglandin E synthase gained from structure-function analysis (2013), Biochem. Biophys. Res. Commun., 440, 762-767.
    View publication on PubMed
Search for more literature for 5.3.99.3

Activating Compound

Activating Compound Comment Organism Structure
glutathione the N-terminal domain contains the GSH-binding site (G-site) Bombyx mori

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression Bombyx mori

Crystallization (Commentary)

Crystallization (Comment) Organism
purified enzyme in complex with glutathione sulfonic acid, sitting drop vapor diffusion method, mixing of 10 mg/ml protein in 20 mM Tris-HCl , pH 8.5, and 0.2 M NaCl with 0.1 M HEPES, pH 7.5, 30% PEG 400 w/v, and 20% 1,2-propanediol v/v, in a 1:1 or 1:2 ratio, X-ray diffraction structure determination and analysis at 1.37 A resolution, molecular replacement Bombyx mori

Protein Variants

Protein Variants Comment Organism
D97A site-directed mutagenesis, isomerase inactive mutant Bombyx mori
N96A site-directed mutagenesis, the mutant shows reduced isomerase activity compared to the wild-type enzyme Bombyx mori
R99A site-directed mutagenesis, isomerase inactive mutant Bombyx mori

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(5Z,13E,15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate Bombyx mori
-
 (5Z,13E,15S)-11alpha,15-dihydroxy-9-oxoprosta-5,13-dienoate
-
 ?

Organism

Organism UniProt Comment Textmining
Bombyx mori
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme by ammonium sulfate fractionation, ion exchange chromatography, and gel filtration Bombyx mori

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(5Z,13E,15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate
-
 Bombyx mori (5Z,13E,15S)-11alpha,15-dihydroxy-9-oxoprosta-5,13-dienoate
-
 ?
additional information the enzyme also shows glutathione transferase activity with 1-chloro-2,4-dinitrobenzene Bombyx mori ?
-
 ?

Subunits

Subunits Comment Organism
More the N-terminal domain contains the GSH-binding site (G-site), and the C-terminal domain contains the binding site for hydrophobic substrate and PGH2 Bombyx mori

Synonyms

Synonyms Comment Organism
PGES
-
 Bombyx mori
Prostaglandin E synthase
-
 Bombyx mori

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Bombyx mori

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Bombyx mori

General Information

General Information Comment Organism
evolution the enzyme belongs to Sigma class glutathione transferase Bombyx mori
additional information the electron-sharing network of the Bombyx mori enzyme includes Asn95, Asp96, and Arg98, the residues contribute to catalytic activity. The C-terminal domain contains the binding site for hydrophobic substrate and PGH2, active site and substrate binding site structures, overview Bombyx mori