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Literature summary for 3.3.2.10 extracted from

  • Butov, G.; Burmistrov, V.; D'yachenko, V.
    Synthesis and properties of symmetrical N,N-bis(R-adamantan-1-yl)ureas as target-oriented soluble epoxide hydrolase (sEH) inhibitors (2017), Russ. J. Org. Chem., 53, 977-980 .
No PubMed abstract available

Inhibitors

Inhibitors Comment Organism Structure
additional information synthesis and properties of symmetrical N,N-bis(R-adamantan-1-yl)ureas as target-oriented soluble epoxide hydrolase (sEH) inhibitors, structure is confirmed by 1H NMR and mass spectra and elemental analyses Homo sapiens
N,N'-bis(3,5,7-trimethyladamantan-1-yl)urea
-
Homo sapiens
N,N'-bis(3,5-dimethyladamantan-1-yl)urea
-
Homo sapiens
N,N'-bis(3-chloroadamantan-1-yl)urea
-
Homo sapiens
N,N'-bis(3-ethyladamantan-1-yl)urea
-
Homo sapiens
N,N'-bis(3-methyladamantan-1-yl)urea
-
Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P34913
-
-

Subunits

Subunits Comment Organism
dimer the monomer of the antiparallel sEH homodimer consists of two globular proteins connected through a bridge containing excess proline, and each protein possesses its own domain (C-terminal epoxide hydrolase and N-terminal phosphatase) for binding to various substrates Homo sapiens

Synonyms

Synonyms Comment Organism
SEH
-
Homo sapiens

General Information

General Information Comment Organism
additional information the enzyme is bifunctional possessing C-terminal epoxide hydrolase and N-terminal phosphatase activities Homo sapiens
physiological function the role of the C-terminal (epoxide hydrolase) domain is confirmed by its participation in the metabolism of epoxy fatty acids to vicinal diols that are endogenous mediators of various undesirable physiological processes. Inhibition of sEH is efficient in inflammatory and neuropathic pains Homo sapiens