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In enzymology, carbon monoxide dehydrogenase () is an enzyme that catalyzes the chemical reaction :CO + H2O + A CO2 + AH2 The 3 substrates of this enzyme are CO, H2O, and A, whereas its two products are CO2 and AH2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with other acceptors. The systematic name of this enzyme class is carbon-monoxide:acceptor oxidoreductase. Other names in common use include anaerobic carbon monoxide dehydrogenase, carbon monoxide oxygenase, carbon-monoxide dehydrogenase, and carbon-monoxide:(acceptor) oxidoreductase. == Classes == Two major classes of the carbon monoxide dehydrogenase (CODH) enzymes have been identified. CODH containing a Mo-()-FAD active site have been found in aerobic bacteria, while a distinct class of Ni-() CODH enzymes have been purified from anaerobic bacteria.〔 〕〔 Both classes of CODH catalyze the reversible conversion between carbon dioxide (CO2) and carbonmonoxide (CO). CODH exists in both monofuctional and bifunctional forms. In the latter case, CODH forms a bifunctional cluster with acetyl-CoA synthase, as has been well characterized in the anaerobic bacteria ''Moorella thermoacetica''. 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「Carbon monoxide dehydrogenase」の詳細全文を読む スポンサード リンク
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