Prostaglandin (PG) F(2α) is widely distributed in various organs and exhibits various biological functions, such as luteolysis, parturition, aqueous humor homeostasis, vasoconstriction, rennin secretion, pulmonary fibrosis and so on. The first enzyme reported to synthesize PGF(2) was referred to as PGF synthase belonging to the aldo-keto reductase (AKR) 1C family, and later PGF(2α) synthases were isolated from protozoans and designated as members of the AKR5A family. In 2003, AKR1B5, which is highly expressed in bovine endometrium, was reported to have PGF(2α) synthase activity, and recently, the paper entitled 'Prostaglandin F(2α) synthase activities of AKR 1B1, 1B3 and 1B7' was reported by Kabututu et al. (J. Biochem.145, 161-168, 2009). Clones that had already been registered in a database as aldose reductases (AKR1B1, 1B3, and 1B7) were expressed in Escherichia coli, and these enzymes were found to have PGF(2α) synthase activity. Moreover, in the above-cited article, the effects of inhibitors specific for aldose reductase on the PGF(2α) synthase activity of AKR1B were discussed. Here, I present an overview of various PGF/PGF(2α) synthases including those of AKR1B subfamily that have been reported until now.
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http://dx.doi.org/10.1093/jb/mvr116 | DOI Listing |
Biomol NMR Assign
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Department of Chemistry and Chemical Biology, TU Dortmund University, Dortmund, Germany.
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View Article and Find Full Text PDFSci Rep
January 2025
Department of Pharmacology and Toxicology, Faculty of Pharmacy, Ahram Canadian University, Giza, Egypt.
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Sci Rep
January 2025
Department of Biotechnology Engineering, NITTE (Deemed to be University), NMAM Institute of Technology, 574110, Karnataka, India.
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