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Literature summary for 1.3.1.48 extracted from

  • Hori, T.; Yokomizo, T.; Ago, H.; Sugahara, M.; Ueno, G.; Yamamoto, M.; Kumasaka, T.; Shimizu, T.; Miyano, M.
    Structural basis of leukotriene B4 12-hydroxydehydrogenase/15-oxo-prostaglandin 13-reductase catalytic mechanism and a possible Src homology 3 domain binding loop (2004), J. Biol. Chem., 279, 22615-22623.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure of the bifunctional leukotriene B4 12-hydroxydehydrogenase/15-oxo-prostaglandin 13-reductase, the binary complex structure with NADP+, and the ternary complex structure with NADP+ and 15-oxo-prostaglandin E2, batch method using the automated crystallization system TERA by mixing equal volumes of protein solution (20 mM Tris-HCL, pH 8.0, 150 mM NaCl, 1 mM dithiothreitol) and precipitating solution (100 mM 4-morpholineethanesulfonic acid, pH 5.5-6.8), 17.5-27.5% polyethylene glycol 4000, 50 mM MgCl2 at 18°C Cavia porcellus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Cavia porcellus essential enzyme for eicosanoid inactivation ?
-
?

Organism

Organism UniProt Comment Textmining
Cavia porcellus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Cavia porcellus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information essential enzyme for eicosanoid inactivation Cavia porcellus ?
-
?

Synonyms

Synonyms Comment Organism
bifunctional leukotriene B4 12-hydroxydehydrogenase/15-oxo-prostaglandin 13-reductase
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Cavia porcellus
LTB4 12-HD/PGR
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Cavia porcellus