Alcohol dehydrogenase class 3 / S-(hydroxymethyl)glutathione dehydrogenase; Oxidizes long-chain aliphatic alcohols, long-chain hydroxylated fatty acids and S-hydroxymethylglutathione (hmGSH) in increasing order of preference. Shows little or no activity with short-chain aliphatic alcohols; Contains two zinc atoms. One is essential for catalytic activity while the other is not; Possibly involved in the metabolism of xenobiotics by cytochrome P450; Belongs to the zinc-containing alcohol dehydrogenase family, class- III subfamily; Localized in the cytoplasm; High confidence in function an [...]

Ferredoxin reductase; The oxidation of substrat by a cytochrome P450 requires the participation of a flavoprotein such as ferredoxin reductase, and an iron-sulfur protein such as ferredoxin, to mediate the transfer of electrons from NADH to P450 for oxygen activation; Uses the FAD as cofactor; Belongs to the FAD-dependent oxidoreductase family, ferredoxin-NADP reductase sub-family; Localized in the cytoplasm; Specificity unclear.

Ferredoxins are electron carrier proteins with an iron-sulfur as cofactor and that transfer electrons in a wide variety of metabolic reactions. Belongs to the putidaredoxin, terpredoxin and adrenodoxin sub-family and uses 2Fe-2S cluster as cofactor ligated at four conserved cysteine residues. The general core structure consists of beta(2)-alpha-beta(2). Localized in the cytoplasm; High confidence in function and specificity.

Cytochromes P450 are a group of heme-thiolate monooxygenases. They oxidize a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics; P450 enzymes usually act as terminal oxidases in multicomponent electron transfer chains, called P450-containing monooxygenase systems; Acts with the ferredoxin and the ferredoxin reductase; Localized in the cytoplasm; Specificity unclear.