Abstract
NAD+-dependent 15-hydroxyprostaglandin dehydrogenase (15-PGDH, EC 1.1.1.141) catalyzes the reversible oxidation of the C-15 hydroxyl group of a number of the prostaglandins, especially of the E and F series (1–3). The resulting 15-keto metabolites usually show greatly reduced biological activities. In addition to prostaglandins, 15-PGDH has recently been shown to catalyze the oxidation of omega-6-hydroxylated fatty acids including 12-HHT (4), 15-HETE, 5,15-diHETE and 8,15-diHETE (5). 15-PGDH is a cytosolic enzyme composed of two identical subunits each with a molecular weight of 29,000 daltons. 15-PGDH has widespread distribution in the body with most tissues possessing some activity although usually at low levels (6,7). Tissues with the highest activities include the lung, liver, kidney and human placenta and these are the organs most commonly used for purification of the enzyme. The highest degrees of purification have recently been reported by Bergholte and Okita (8) from pregnant rabbit lung, Krook et al (9) from human placenta, and Mak et al (10) from porcine kidney.
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Ensor, C.M., Tai, HH. (1991). Cloning, Expression and Site-Directed Mutagenesis of the cDNA for Human Placental NAD+-Dependent 15-Hydroxyprostaglandin Dehydrogenase. In: Bailey, J.M. (eds) Prostaglandins, Leukotrienes, Lipoxins, and PAF. GWUMC Department of Biochemistry Annual Spring Symposia. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-0727-1_5
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DOI: https://doi.org/10.1007/978-1-4899-0727-1_5
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