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Literature summary for 1.14.14.24 extracted from

  • Hosseinpour, F.; Hidestrand, M.; Ingelman-Sundberg, M.; Wikvall, K.
    The importance of residues in substrate recognition site 3 for the catalytic function of CYP2D25 (vitamin D 25-hydroxylase) (2001), Biochem. Biophys. Res. Commun., 288, 1059-1063.
    View publication on PubMed
Search for more literature for 1.14.14.24

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Sus scrofa

Protein Variants

Protein Variants Comment Organism
A241G/L243V/F244L/P245R/R246F mutation in substrate recognition site 3, to the equivalent residues in CYP2D6, an enzyme not active in 25-hydroxylation. The 25-hydroxylase activity of the mutant is completely lost whereas the activity toward tolterodine remains virtually unaffected Sus scrofa

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.001
-
 bufuralol pH 7.4, 37°C, mutant A241G/L243V/F244L/P245R/R246F Sus scrofa
0.0014
-
 bufuralol pH 7.4, 37°C, wild-type Sus scrofa

Localization

Localization Comment Organism GeneOntology No. Textmining
microsome
-
 Sus scrofa
-
-

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1alpha-hydroxyvitamin D3 + O2 + NADPH + H+
-
 Sus scrofa 1alpha,25-dihydroxy-vitamin D3 + NADP+ + H2O
-
 ?
bufuralol + O2 + NADPH + H+
-
 Sus scrofa 1'-hydroxybufuralol + NADP+ + H2O
-
 ?
tolterodine + O2 + NADPH + H+
-
 Sus scrofa ? + NADP+ + H2O
-
 ?
vitamin D3 + O2 + NADPH + H+
-
 Sus scrofa 25-hydroxyvitamin D3 + NADP+ + H2O
-
 ?

Synonyms

Synonyms Comment Organism
CYP2D25
-
 Sus scrofa