15-hydroxyprostaglandin dehydrogenase (NADP+)
15-hydroxyprostaglandin dehydrogenase (NADP+) | |||||||||
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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 | ||||||||
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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
[edit]As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2PFG.
References
[edit]- Lee SC, Levine L (1975). "Prostaglandin metabolism. II. Identification of two 15-hydroxyprostaglandin dehydrogenase types". J. Biol. Chem. 250 (2): 548–52. doi:10.1016/S0021-9258(19)41931-5. 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.