Source: recombinant N-terminal GST-tagged protein purified from E. coli · M_r: 47.5 kDa · Prostaglandin D synthase (PGDS) catalyzes the isomerization of PGH₂ to produce PGD₂. PGD₂ induces sleep, regulates nociception, inhibits platelet aggregation and acts as an allergic mediator. Two distinct types of PGDS have been identified, namely the lipocalin-type enzyme (β-trace) and the hematopoietic enzyme.^1,2,3 Lipocalin-type PGDS is localized in the central nervous system and male genital organs of various mammals and the human heart. This enzyme has been identified as β-trace, which is a major protein in human cerebrospinal fluid.¹ The recombinant human L-PGDS was expressed and purified from E.Coli as a 47.5 kDa glutathione S-transferase (GST)-fusion protein. To avoid incorrectly folded protein due to wrong disulfide (S-S) linking, cysteines 89 and 186 have been mutated to alanines in this enzyme. Alanine mutations or GST fusion does not alter the activity of the enzyme compared to wild-type.^4,5

1 Urade, Y., Watanabe, K., and Hayaishi, O. Prostaglandin D, E, and F synthases. J Lipid Mediat Cell Signal 12 257-273 (1995).

2 Urade, Y., and Hayaishi, O. Prostaglandin D synthase: Structure and function. Vitam Horm 58 89-120 (2000).

3 Urade, Y., and Eguchi, N. Lipocalin-type and hematopoietic prostaglandin D synthases as a novel example of functional convergence. Prostaglandins Other Lipid Mediat 68-69 375-382 (2002).

4 Irikura, D., Kumasaka, T., Yamamoto, M., et al. Cloning, expression, crystallization, and preliminary X-ray analysis of recombinant mouse lipocalin-type prostaglandin D synthase, a somnogen-producing enzyme. J Biochem 133 29-32 (2003).

5 Urade, Y., Tanaka, T., Eguchi, N., et al. Structural and functional significance of cysteine residues of glutathione-independent prostaglandin D synthase. J Biol Chem 270 1422-1428 (1995).

Urade, Y., Watanabe, K., and Hayaishi, O. Prostaglandin D, E, and F synthases. J Lipid Mediat Cell Signal 12 257-273 (1995).

Irikura, D., Kumasaka, T., Yamamoto, M., et al. Cloning, expression, crystallization, and preliminary X-ray analysis of recombinant mouse lipocalin-type prostaglandin D synthase, a somnogen-producing enzyme. J Biochem 133 29-32 (2003).

Urade, Y., Tanaka, T., Eguchi, N., et al. Structural and functional significance of cysteine residues of glutathione-independent prostaglandin D synthase. J Biol Chem 270 1422-1428 (1995).

Urade, Y., and Eguchi, N. Lipocalin-type and hematopoietic prostaglandin D synthases as a novel example of functional convergence. Prostaglandins Other Lipid Mediat 68-69 375-382 (2002).

Urade, Y., and Hayaishi, O. Prostaglandin D synthase: Structure and function. Vitam Horm 58 89-120 (2000).

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