15-hydroxyprostaglandin dehydrogenase (NAD+)
| hydroxyprostaglandin dehydrogenase 15-(NAD) | |||||||||
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15-hydroxyprostaglandin dehydrogenase dimer (NAD dependent), Human | |||||||||
| Identifiers | |||||||||
| EC number | 1.1.1.141 | ||||||||
| CAS number | 9030-87-9 | ||||||||
| 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 / EGO | ||||||||
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Hydroxyprostaglandin dehydrogenase 15-(NAD) (the HUGO-approved symbol = HPGD; HGNC ID, HGNC:5154), also called 15-hydroxyprostaglandin dehydrogenase (NAD+), (EC 1.1.1.141), is an enzyme that catalyzes the following 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, 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.