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In enzymology, an aldehyde ferredoxin oxidoreductase () is an enzyme that catalyzes the chemical reaction :an aldehyde + H2O + 2 oxidized ferredoxin an acid + 2 H+ + 2 reduced ferredoxin This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with an iron-sulfur protein as acceptor. The systematic name of this enzyme class is aldehyde:ferredoxin oxidoreductase. This enzyme is also called AOR. It is a relatively rare example of a tungsten-containing protein.〔 ==Occurrence== The active site of the AOR family feature an oxo-tungstern center bound to a pair of molybdopterin cofactors (which does not contain molybdenum) and an 4Fe4S cluster. This family includes AOR, formaldehyde ferredoxin oxidoreductase (FOR), glyceraldehyde-3-phosphate ferredoxin oxidoreductase (GAPOR), all isolated from hyperthermophilic archea;〔 carboxylic acid reductase found in clostridia; and hydroxycarboxylate viologen oxidoreductase from ''Proteus vulgaris'', the sole member of the AOR family containing molybdenum. GAPOR may be involved in glycolysis, but the functions of the other proteins are not yet clear. AOR has been proposed to be the primary enzyme responsible for oxidising the aldehydes that are produced by the 2-keto acid oxidoreductases. AOR is found in hyperthermophillic archaea, Pyrococcus furiosus. The archaeons ''Pyrococcus'' ES-4 strain and ''Thermococcus'' ES-1 strain differ by their substrate specificity: AFOs show a broader size range of its aldehyde subtrates. Its primary role is to oxidize aldehyde coming derived from the metabolsm of amino acids and glucoses. Aldehyde Ferredoxin Oxidoreductase is a member of an AOR family, which includes glyceraldehyde-3-phosphate ferredoxin oxidoreductase (GAPOR) and Formaldehyde Ferredoxin Oxidoreductase.〔 抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』 ■ウィキペディアで「Aldehyde ferredoxin oxidoreductase」の詳細全文を読む スポンサード リンク
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