15-hydroxyprostaglandin dehydrogenase

In enzymology, a 15-hydroxyprostaglandin dehydrogenase (NAD+) (EC 1.1.1.141) is an enzyme that catalyzes the chemical reaction

(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate + NAD⁺ (5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-13-enoate + NADH + H⁺

Thus, the two substrates of this enzyme are (5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate and NAD⁺, whereas its 3 products are (5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-13-enoate, NADH, and H⁺.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate:NAD+ 15-oxidoreductase. Other names in common use include NAD+-dependent 15-hydroxyprostaglandin dehydrogenase (type I), PGDH, 11alpha,15-dihydroxy-9-oxoprost-13-enoate:NAD+ 15-oxidoreductase, 15-OH-PGDH, 15-hydroxyprostaglandin dehydrogenase, 15-hydroxyprostanoic dehydrogenase, NAD+-specific 15-hydroxyprostaglandin dehydrogenase, prostaglandin dehydrogenase, and 15-hydroxyprostaglandin dehydrogenase (NAD+).

Structural studies

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2GDZ.

References

• Anggaard E and Samuelsson B (1966). "Purification and properties of a 15-hydroxyprostaglandin dehydrogenase from swine lung". Prostaglandins 25: 293–300. 
• Braithwaite SS, Jarabak J (1975). "Studies on a 15-hydroxyprostaglandin dehydrogenase from human placenta. Purification and partial characterization". J. Biol. Chem. 250 (6): 2315–8. PMID 1117007. 
• Lee SC, Levine L (1975). "Prostaglandin metabolism. II. Identification of two 15-hydroxyprostaglandin dehydrogenase types". J. Biol. Chem. 250 (2): 548–52. PMID 234431. 
• Lee SC, Pong SS, Katzen D, Wu KY, Levine L (1975). "Distribution of prostaglandin E 9-KETOREDUCTASE AND TYPES I and II 15-hydroxyprostaglandin dehydrogenase in swine kidney medulla and cortex". Biochemistry. 14 (1): 142–5. doi:10.1021/bi00672a024. PMID 803247.