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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Pyruvate ferredoxin oxidoreductase from the hyperthermophilic archaeon, Pyrococcus furiosus, functions as a CoA-dependent pyruvate decarboxylase
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Pyruvate ferredoxin oxidoreductase from the hyperthermophilic archaeon, Pyrococcus furiosus, functions as a CoA-dependent pyruvate decarboxylase

机译：来自嗜热古细菌Pyrococcus furiosus的丙酮酸铁氧还蛋白氧化还原酶起CoA依赖性丙酮酸脱羧酶的作用

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摘要

Pyruvate ferredoxin oxidoreductase (POR) has been previously purified from the hyperthermophilic archaeon, Pyrococcus furiosus, an organism that grows opti- mally at 100 deg C by fermenting carbohydrates and peptides. The enzyme contains thiamine pyrophosphate and catalyzes the oxidative decarboxylation of pyruvate to acetyl-CoA and CO_2 and reduces P. furiosus ferredoxin. Here we show that this enzyme also catalyzes the formation of acetaldehyde from pyruvate in a CoA-dependent reaction. Desulfocoenzyme A substituted for CoA showing that the cofactor plays a struc- tural rather than a catalytic role. Ferredoxin was not neces- sary for the pyruvate decarboxylase activity of POR, nor did it inhibit acetaldehyde production.
机译：丙酮酸铁氧还蛋白氧化还原酶（POR）先前已从嗜热古细菌激烈热球菌（Pyrococcus furiosus）中纯化，该生物通过发酵碳水化合物和多肽在100℃下最佳生长。该酶含有硫胺素焦磷酸，并催化丙酮酸氧化脱羧为乙酰辅酶A和CO_2，并还原恶性疟原虫铁氧还蛋白。在这里，我们显示了该酶还可以在CoA依赖性反应中催化丙酮酸中乙醛的形成。脱硫辅酶A代替了CoA，表明辅因子起结构作用而不是催化作用。铁氧还蛋白对于POR的丙酮酸脱羧酶活性不是必需的，也不抑制乙醛的产生。

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