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Literature summary for 1.14.14.1 extracted from

  • Pachecka, J.; Tomaszewski, P.; Kubiak-Tomaszewska, G.
    Cytochrome P450 polymorphism--molecular, metabolic and pharmacogenetic aspects. I. Mechanisms of activity of cytochrome P450 monooxygenases (2008), Acta Pol. Pharm., 65, 303-306.
    View publication on PubMed

Localization

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum
-
Homo sapiens 5783
-
mitochondrial inner membrane CYP24A1 and CYP27A1 Homo sapiens 5743
-

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ an electron transferred to CYP(Fe3+), interacting with the proper substrate, reduces Fe3+ in the heme system to Fe2+, allowing a consequent interaction of the CYP(Fe2+)-substrate complex with O2. The second transferred electron allows for transformation of the O2-CYP(Fe2+)-substrate complex into a form with an anion potentialized reactive oxygen species -O2-CYP(Fe2+)-substrate, permitting destabilization of the bond between the atoms of the oxygen molecule to form a bond of one of the oxygen atoms with the substrate. The second oxygen atom is reduced to H2O by reductive equivalent transport systems (cytochrome P450 reductase, cytochrome b5 reductase/cytochrome b5, adrenodoxin reductase/adrenodoxin) Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
hepatocyte
-
Homo sapiens
-

Synonyms

Synonyms Comment Organism
CYP monooxygenase
-
Homo sapiens
CYP24A1
-
Homo sapiens
CYP27A1
-
Homo sapiens
CYP5A1
-
Homo sapiens
CYP8A1
-
Homo sapiens
cytochrome P450 monooxygenase
-
Homo sapiens

Cofactor

Cofactor Comment Organism Structure
cytochrome P450
-
Homo sapiens
FAD
-
Homo sapiens
FMN
-
Homo sapiens
NADPH
-
Homo sapiens