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Literature summary for 3.1.3.76 extracted from

  • Newman, J.W.; Morisseau, C.; Hammock, B.D.
    Epoxide hydrolases: their roles and interactions with lipid metabolism (2005), Prog. Lipid Res., 44, 1-51.
    View publication on PubMed
Search for more literature for 3.1.3.76

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure analysis Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.021
-
 threo-9-hydroxy-10-(phosphonooxy)octadecanoate pH 7.8, 37°C, recombinant enzyme Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ dependent on Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Reaction

Reaction Comment Organism Reaction ID
(9S,10S)-10-hydroxy-9-(phosphooxy)octadecanoate + H2O = (9S,10S)-9,10-dihydroxyoctadecanoate + phosphate the phosphatase activity of the enzyme is located at the N-terminal part, the C-terminal part harbors the epoxide hydrolase activity of EC 3.3.2.10, both catalytic sites act independently Homo sapiens
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
erythro-9-hydroxy-10-(phosphonooxy)octadecanoate + H2O
-
 Homo sapiens erythro-9,10-dihydroxyoctadecanoic acid + phosphate i.e. dihydroxy elaidic acid ?
additional information the enzyme acts regioselectively, substrate specificity Homo sapiens ?
-
 ?
threo-9-hydroxy-10-(phosphonooxy)octadecanoate + H2O preferred substrate Homo sapiens threo-9,10-dihydroxyoctadecanoic acid + phosphate i.e. dihydroxy stearic acid ?

Subunits

Subunits Comment Organism
More the phosphatase activity of the enzyme is located at the N-terminal part, the C-terminal part harbors the epoxide hydrolase activity of EC 3.3.2.10 Homo sapiens

Synonyms

Synonyms Comment Organism
lipid phosphatase
-
 Homo sapiens
More c.f. EC 3.3.2.10 Homo sapiens