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Literature summary extracted from

  • Lundell, K.; Wikvall, K.
    Species-specific and age-dependent bile acid composition: aspects on CYP8B and CYP4A subfamilies in bile acid biosynthesis (2008), Curr. Drug Metab., 9, 323-331.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.14.139 genetic structure and phylogenetic analysis Mus musculus
1.14.14.139 genetic structure and phylogenetic analysis Homo sapiens
1.14.14.139 genetic structure and phylogenetic analysis Rattus norvegicus
1.14.14.139 genetic structure and phylogenetic analysis Sus scrofa
1.14.14.139 genetic structure and phylogenetic analysis Oryctolagus cuniculus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.14.139 Fe2+ a cytochrome P450 enzyme Mus musculus
1.14.14.139 Fe2+ a cytochrome P450 enzyme Homo sapiens
1.14.14.139 Fe2+ a cytochrome P450 enzyme Rattus norvegicus
1.14.14.139 Fe2+ a cytochrome P450 enzyme Sus scrofa
1.14.14.139 Fe2+ a cytochrome P450 enzyme Oryctolagus cuniculus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.14.139 5beta-cholestan-3alpha,7alpha-diol + [reduced NADPH-hemoprotein reductase] + O2 Mus musculus
-
5beta-cholestan-3alpha,7alpha,12alpha-triol + [oxidized NADPH-hemoprotein reductase] + H2O
-
?
1.14.14.139 5beta-cholestan-3alpha,7alpha-diol + [reduced NADPH-hemoprotein reductase] + O2 Homo sapiens
-
5beta-cholestan-3alpha,7alpha,12alpha-triol + [oxidized NADPH-hemoprotein reductase] + H2O
-
?
1.14.14.139 5beta-cholestan-3alpha,7alpha-diol + [reduced NADPH-hemoprotein reductase] + O2 Rattus norvegicus
-
5beta-cholestan-3alpha,7alpha,12alpha-triol + [oxidized NADPH-hemoprotein reductase] + H2O
-
?
1.14.14.139 5beta-cholestan-3alpha,7alpha-diol + [reduced NADPH-hemoprotein reductase] + O2 Sus scrofa
-
5beta-cholestan-3alpha,7alpha,12alpha-triol + [oxidized NADPH-hemoprotein reductase] + H2O
-
?
1.14.14.139 5beta-cholestan-3alpha,7alpha-diol + [reduced NADPH-hemoprotein reductase] + O2 Oryctolagus cuniculus
-
5beta-cholestan-3alpha,7alpha,12alpha-triol + [oxidized NADPH-hemoprotein reductase] + H2O
-
?
1.14.14.139 additional information Mus musculus the enzyme is involved in trihydroxy bile acid metabolism and cholic acid synthesis from cholesterol, overview ?
-
?
1.14.14.139 additional information Homo sapiens the enzyme is involved in trihydroxy bile acid metabolism and cholic acid synthesis from cholesterol, overview ?
-
?
1.14.14.139 additional information Rattus norvegicus the enzyme is involved in trihydroxy bile acid metabolism and cholic acid synthesis from cholesterol, overview ?
-
?
1.14.14.139 additional information Sus scrofa the enzyme is involved in trihydroxy bile acid metabolism and cholic acid synthesis from cholesterol, overview ?
-
?
1.14.14.139 additional information Oryctolagus cuniculus the enzyme is involved in trihydroxy bile acid metabolism and cholic acid synthesis from cholesterol, overview ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.14.14.139 Homo sapiens
-
-
-
1.14.14.139 Mus musculus
-
-
-
1.14.14.139 Oryctolagus cuniculus
-
-
-
1.14.14.139 Rattus norvegicus
-
-
-
1.14.14.139 Sus scrofa
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.14.139 5beta-cholestan-3alpha,7alpha-diol + [reduced NADPH-hemoprotein reductase] + O2
-
Mus musculus 5beta-cholestan-3alpha,7alpha,12alpha-triol + [oxidized NADPH-hemoprotein reductase] + H2O
-
?
1.14.14.139 5beta-cholestan-3alpha,7alpha-diol + [reduced NADPH-hemoprotein reductase] + O2
-
Homo sapiens 5beta-cholestan-3alpha,7alpha,12alpha-triol + [oxidized NADPH-hemoprotein reductase] + H2O
-
?
1.14.14.139 5beta-cholestan-3alpha,7alpha-diol + [reduced NADPH-hemoprotein reductase] + O2
-
Rattus norvegicus 5beta-cholestan-3alpha,7alpha,12alpha-triol + [oxidized NADPH-hemoprotein reductase] + H2O
-
?
1.14.14.139 5beta-cholestan-3alpha,7alpha-diol + [reduced NADPH-hemoprotein reductase] + O2
-
Sus scrofa 5beta-cholestan-3alpha,7alpha,12alpha-triol + [oxidized NADPH-hemoprotein reductase] + H2O
-
?
1.14.14.139 5beta-cholestan-3alpha,7alpha-diol + [reduced NADPH-hemoprotein reductase] + O2
-
Oryctolagus cuniculus 5beta-cholestan-3alpha,7alpha,12alpha-triol + [oxidized NADPH-hemoprotein reductase] + H2O
-
?
1.14.14.139 additional information the enzyme is involved in trihydroxy bile acid metabolism and cholic acid synthesis from cholesterol, overview Mus musculus ?
-
?
1.14.14.139 additional information the enzyme is involved in trihydroxy bile acid metabolism and cholic acid synthesis from cholesterol, overview Homo sapiens ?
-
?
1.14.14.139 additional information the enzyme is involved in trihydroxy bile acid metabolism and cholic acid synthesis from cholesterol, overview Rattus norvegicus ?
-
?
1.14.14.139 additional information the enzyme is involved in trihydroxy bile acid metabolism and cholic acid synthesis from cholesterol, overview Sus scrofa ?
-
?
1.14.14.139 additional information the enzyme is involved in trihydroxy bile acid metabolism and cholic acid synthesis from cholesterol, overview Oryctolagus cuniculus ?
-
?

Synonyms

EC Number Synonyms Comment Organism
1.14.14.139 CYP8B1
-
Mus musculus
1.14.14.139 CYP8B1
-
Homo sapiens
1.14.14.139 CYP8B1
-
Rattus norvegicus
1.14.14.139 CYP8B1
-
Sus scrofa
1.14.14.139 CYP8B1
-
Oryctolagus cuniculus
1.14.14.139 More the enzyme belongs to the CYP8B subfamily Mus musculus
1.14.14.139 More the enzyme belongs to the CYP8B subfamily Homo sapiens
1.14.14.139 More the enzyme belongs to the CYP8B subfamily Rattus norvegicus
1.14.14.139 More the enzyme belongs to the CYP8B subfamily Sus scrofa
1.14.14.139 More the enzyme belongs to the CYP8B subfamily Oryctolagus cuniculus

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.14.139 cytochrome a cytochrome P450 enzyme Rattus norvegicus
1.14.14.139 cytochrome a cytochrome P450 enzyme Oryctolagus cuniculus
1.14.14.139 cytochrome P450 a cytochrome P450 enzyme Mus musculus
1.14.14.139 cytochrome P450 a cytochrome P450 enzyme Homo sapiens
1.14.14.139 cytochrome P450 a cytochrome P450 enzyme Sus scrofa