Literature summary for 3.1.3.76 extracted from

Gomez, G.A.; Morisseau, C.; Hammock, B.D.; Christianson, D.W.
Structure of human epoxide hydrolase reveals mechanistic inferences on bifunctional catalysis in epoxide and phosphate ester hydrolysis (2004), Biochemistry, 43, 4716-4723.

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant enzyme, sitting drop vapour diffusion method, 0.005 ml of 12-16 mg/ml protein in 3 mM DTT, 0.1 M sodium phosphate, pH 7.4, is mixed with 0.005 ml precipitation solution containing 0.1 M Tris, pH 9.0, 30% w/v PEG 4000, and 0.2 M Li2SO4, versus 1 ml reservoir of precipitatin solution, 4°C, 10 days, X-ray diffraction structure determination and analysis at 2.6 A resolution, modeling	Homo sapiens

Crystallization (Comment)

Organism

purified recombinant enzyme, sitting drop vapour diffusion method, 0.005 ml of 12-16 mg/ml protein in 3 mM DTT, 0.1 M sodium phosphate, pH 7.4, is mixed with 0.005 ml precipitation solution containing 0.1 M Tris, pH 9.0, 30% w/v PEG 4000, and 0.2 M Li2SO4, versus 1 ml reservoir of precipitatin solution, 4°C, 10 days, X-ray diffraction structure determination and analysis at 2.6 A resolution, modeling

Homo sapiens

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	dependent on, binding structure at the N-terminus	Homo sapiens
phosphate	binding structure at the N-terminus	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, reaction mechanism, structure-mechanism relationship	Homo sapiens	a

Subunits

Subunits	Comment	Organism
More	the phosphatase activity of the enzyme is located at the 35 kDa N-terminal part which has a alpha/beta-fold, the 25 kDa C-terminal part, with a different hydrolase alpha/beta-fold, harbors the epoxide hydrolase activity of EC 3.3.2.10, quarternary structure analysis, structure-mechanism relationship	Homo sapiens

Synonyms

Synonyms	Comment	Organism
More	c.f. EC 3.3.2.10	Homo sapiens