1.1.1.141: 15-hydroxyprostaglandin dehydrogenase (NAD+)

This is an abbreviated version, for detailed information about 15-hydroxyprostaglandin dehydrogenase (NAD+), go to the full flat file.

Reaction

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

Synonyms

11alpha,15-dihydroxy-9-oxoprost-13-enoate:NAD+ 15-oxidoreductase, 15-hydroxy prostaglandin dehydrogenase, 15-hydroxyprostaglandin dehydrogenase, 15-hydroxyprostaglandin-dehydrogenase, 15-hydroxyprostanoic dehydrogenase, 15-OH-PGDH, 15-PGDH, 15-prostaglandin dehydrogenase, dehydrogenase, 15-hydroxyprostaglandin, HPGD, NAD+ dependent 15-hydroxyprostaglandin dehydrogenase, NAD+ dependent PGDH, NAD+-15-hydroxy prostanoate oxidoreductase, NAD+-dependent 15-hydroxyprostaglandin dehydrogenase, NAD+-dependent 15-hydroxyprostaglandin dehydrogenase (type I), NAD+-dependent 15-PGDH, NAD+-linked 15-hydroxyprostaglandin dehydrogenase, NAD-dependent 15-hydroxyprostaglandin dehydrogenase, NAD-specific 15-hydroxyprostaglandin dehydrogenase, PGDH, prostaglandin dehydrogenase

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.141 15-hydroxyprostaglandin dehydrogenase (NAD+)

Crystallization

Crystallization on EC 1.1.1.141 - 15-hydroxyprostaglandin dehydrogenase (NAD+)

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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
modeling of structure for mutant A140P. Mutation disrupts binding of the substrate prostaglandin E2 both because the pyrrolidine ring of Pro140 fills a space that in the wildtype complex is occupied by the prostaglandin E2 target side-chain 15-OH and because there is a resulting loss of catalytically important hydrogen bonding of the 15-OH to the nearby serine at residue 138
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