Abstract
Human tissues contain two enzymes that catalyze the oxidation of the 15-hydroxy group of prostaglandins: NAD-dependent 15-hydroxyprostaglandin dehydrogenase which is fairly specific for prostaglandins and NADP-dependent 15-hydroxyprostaglandin dehydrogenase with low specificity for prostaglandins. The recent determination of the amino acid sequence of the NAD-dependent enzyme has revealed similarities with a number of oxidoreductases with distinct specificities that constitute the short-chain alcohol dehydrogenase family. Comparison of the amino acid sequence of NADP-dependent 15-hydroxyprostaglandin dehydrogenase with the sequences of the NAD-dependent enzyme and other short-chain alcohol dehydrogenases revealed the same similarities, identifying the NADP-dependent enzyme as a short-chain alcohol dehydrogenase. The degree of homology between the two 15-hydroxyprostaglandin dehydrogenases is similar to the one between each of the two enzymes and other members of the family indicating an early evolutionary divergence of the two proteins.
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