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Literature summary extracted from

  • Kim, J.H.; Cho, I.S.; Ryu, J.; Lee, J.S.; Kang, J.S.; Kang, S.Y.; Kim, Y.H.
    In vitro and in silico investigation of anthocyanin derivatives as soluble epoxide hydrolase inhibitors (2018), Int. J. Biol. Macromol., 112, 961-967 .
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.3.2.10 12-[[(tricyclo[3.3.1.13,7]dec-1-ylamino)carbonyl]amino]-dodecanoic acid i.e. AUDA Homo sapiens
3.3.2.10 2-(3,4-dihydroxy-5-methoxyphenyl)-5,7-dihydroxy-1-benzopyran-1-ium-3-yl beta-D-glucopyranoside mixed-type inhibition Homo sapiens
3.3.2.10 2-(3,4-dihydroxyphenyl)-5,7-dihydroxy-1-benzopyran-1-ium noncompetitive inhibition Homo sapiens
3.3.2.10 2-(3,4-dihydroxyphenyl)-5,7-dihydroxy-1-benzopyran-1-ium-3-yl beta-D-glucopyranoside noncompetitive inhibition Homo sapiens
3.3.2.10 5,7-dihydroxy-2-(3,4,5-trihydroxyphenyl)-1-benzopyran-1-ium-3-yl beta-D-galactopyranoside mixed-type inhibition Homo sapiens
3.3.2.10 5,7-dihydroxy-2-(3,4,5-trihydroxyphenyl)-1-benzopyran-1-ium-3-yl beta-D-glucopyranoside noncompetitive inhibition Homo sapiens
3.3.2.10 additional information interaction of the enzyme with anthocyanin derivatives, molecular docking study, molecular dynamics study, overview. The molecular docking study shows a small pocket next to the active site, which is thought to be a common allosteric site, which probably is the binding site of noncompetitive and mixed inhibitors. Moreover, the anthocyanin core is located at the hydrophobic position of the inner allosteric site. The sugar moiety interacts with amino acid residues on the outside of the allosteric site. In particular, the hydroxyl group in the sugar of the compounds is bonded with the nitrogen of Trp525. The amino acid residue may play a key role in forming hydrogen bonds with the anthocyanin glycoside. Additionally, the molecular dynamics study confirms that anthocyanin 4 can form hydrogen bonds with this residue for 10 ns Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.3.2.10 additional information
-
 additional information steady-state enzyme kinetics study, overview Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
3.3.2.10 Homo sapiens P34913
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.3.2.10 3-phenyl-cyano(6-methoxy-2-naphthalenyl)methyl ester-2-oxiraneacetic acid + H2O fluorometric activity assay substrate Homo sapiens 6-methoxy-2-naphthaldehyde + ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.3.2.10 SEH
-
 Homo sapiens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.3.2.10 37
-
 assay at Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.3.2.10 7
-
 assay at Homo sapiens

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
3.3.2.10 0.000002
-
 pH 7.0, 37°C Homo sapiens 12-[[(tricyclo[3.3.1.13,7]dec-1-ylamino)carbonyl]amino]-dodecanoic acid
3.3.2.10 0.0043
-
 pH 7.0, 37°C Homo sapiens 2-(3,4-dihydroxy-5-methoxyphenyl)-5,7-dihydroxy-1-benzopyran-1-ium-3-yl beta-D-glucopyranoside
3.3.2.10 0.0102
-
 pH 7.0, 37°C Homo sapiens 2-(3,4-dihydroxyphenyl)-5,7-dihydroxy-1-benzopyran-1-ium
3.3.2.10 0.0112
-
 pH 7.0, 37°C Homo sapiens 5,7-dihydroxy-2-(3,4,5-trihydroxyphenyl)-1-benzopyran-1-ium-3-yl beta-D-galactopyranoside
3.3.2.10 0.0146
-
 pH 7.0, 37°C Homo sapiens 2-(3,4-dihydroxyphenyl)-5,7-dihydroxy-1-benzopyran-1-ium-3-yl beta-D-glucopyranoside
3.3.2.10 0.0253
-
 pH 7.0, 37°C Homo sapiens 5,7-dihydroxy-2-(3,4,5-trihydroxyphenyl)-1-benzopyran-1-ium-3-yl beta-D-glucopyranoside