1.1.1.141: 15-hydroxyprostaglandin dehydrogenase (NAD+)

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For detailed information about 15-hydroxyprostaglandin dehydrogenase (NAD+), go to the full flat file.

Reaction

Synonyms

11alpha,15-dihydroxy-9-oxoprost-13-enoate:NAD+ 15-oxidoreductase, 15-hydroxy prostaglandin dehydrogenase, 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, nicotinamide adenine dinucleotide-dependent 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+)

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Results	in table
30	Activating Compound
43	AA Sequence
9	Application
1	CAS Registry Number
23	Cloned(Commentary)
62	Cofactor
1	Crystallization (Commentary)
1263	Disease/ Diagnostics
11	Expression
9	General Information
7	General Stability
108	IC50 Value
268	Inhibitors
7	kcat/KM [mM/s]
38	Ki Value [mM]
100	KM Value [mM]
8	Localization
19	Molecular Weight [Da]
51	Natural Substrates/ Products (Substrates)
164	Organism
6	Pathway
1	PDB ID
19	pH Optimum
2	pH Range
70	Protein Variants
34	Purification (Commentary)
9	Reaction
3	Reaction Type
101	Reference
226	Source Tissue
24	Specific Activity [micromol/min/mg]
8	Storage Stability
175	Substrates and Products (Substrate)
14	Subunits
121	Synonyms
1	Systematic Name
13	Temperature Optimum [°C]
4	Temperature Stability [°C]
25	Turnover Number [1/s]

Crystallization

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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

Homo sapiens

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689129