15-hydroxyprostaglandin dehydrogenase (NADP+)
| 15-hydroxyprostaglandin dehydrogenase (NADP+) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.1.1.197 | ||||||||
| CAS no. | 54989-39-8 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a 15-hydroxyprostaglandin dehydrogenase (NADP+) (EC 1.1.1.197) is an enzyme that catalyzes the chemical reaction
- (13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate + NADP+ (13E)-11alpha-hydroxy-9,15-dioxoprost-13-enoate + NADPH + H+
Thus, the two substrates of this enzyme are (13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate and NADP+, whereas its 3 products are (13E)-11alpha-hydroxy-9,15-dioxoprost-13-enoate, NADPH, 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 (13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate:NADP+ 15-oxidoreductase. Other names in common use include NADP+-dependent 15-hydroxyprostaglandin dehydrogenase, NADP+-linked 15-hydroxyprostaglandin dehydrogenase, NADP+-specific 15-hydroxyprostaglandin dehydrogenase, type II 15-hydroxyprostaglandin dehydrogenase, and 15-hydroxyprostaglandin dehydrogenase (NADP+).
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2PFG.
References
- 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 E9-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.
