Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.3.2.10 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.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant enzyme in complex with N-cyclohexyl-N'-(iodophenyl)urea, 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 precipitation solution, 4Ā°C, 10 days, soaking of crystals in inhibitor solution and n-hexadecyl-beta-D-maltoside, X-ray diffraction structure determination and analysis at 2.35 A resolution, modeling Homo sapiens
sitting drop vapour diffusion method, X-ray crystal structure determined at 2.6 A resolution, structure of the complex with the inhibitor N-cyclohexyl-NĀ‘-(iodophenyl)urea determine at 2.35 A resolution Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
N-cyclohexyl-N'-(iodophenyl)urea binding structure at the C-terminus Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P34913
-
-

Reaction

Reaction Comment Organism Reaction ID
an epoxide + H2O = a glycol the C-terminal part harbors the epoxide hydrolase activity, the phosphatase activity of the enzyme is located at the N-terminal part of EC 3.1.3.76, both catalytic sites act independently, the epoxide hydrolase reaction proceeds though an alkyl-enzyme intermediate involving the catalytic Asp333, and hydrogen bonds with Tyr381 and Tyr465, reaction mechanism, structure-mechanism relationship Homo sapiens

Subunits

Subunits Comment Organism
More the 25 kDa C-terminal part, with a hydrolase alpha/beta-fold, harbors the epoxide hydrolase activity, the enzyme's phosphatase activity of EC3.1.3.76 is located at the 35 kDa N-terminal part which has a different alpha/beta-fold, quarternary structure analysis, structure-mechanism relationship Homo sapiens

Synonyms

Synonyms Comment Organism
More see also EC 3.1.3.76 Homo sapiens