Welford Richard W D, Kirkpatrick Joanna M, McNeill Luke A, Puri Munish, Oldham Neil J, Schofield Christopher J
UC Berkeley, Department of Chemistry, Berkeley, CA 94720, USA.
FEBS Lett. 2005 Sep 26;579(23):5170-4. doi: 10.1016/j.febslet.2005.08.033.
The ferrous iron and 2-oxoglutarate (2OG) dependent oxygenases catalyse two electron oxidation reactions by coupling the oxidation of substrate to the oxidative decarboxylation of 2OG, giving succinate and carbon dioxide coproducts. The evidence available on the level of incorporation of one atom from dioxygen into succinate is inconclusive. Here, we demonstrate that five members of the 2OG oxygenase family, AlkB from Escherichia coli, anthocyanidin synthase and flavonol synthase from Arabidopsis thaliana, and prolyl hydroxylase domain enzyme 2 and factor inhibiting hypoxia-inducible factor-1 from Homo sapiens all incorporate a single oxygen atom, almost exclusively derived from dioxygen, into the succinate co-product.
亚铁离子和2-氧代戊二酸（2OG）依赖性加氧酶通过将底物的氧化与2OG的氧化脱羧偶联来催化双电子氧化反应，生成琥珀酸和二氧化碳副产物。关于一个氧原子从双氧掺入琥珀酸的程度的现有证据尚无定论。在这里，我们证明了2OG加氧酶家族的五个成员，来自大肠杆菌的AlkB、来自拟南芥的花青素合酶和黄酮醇合酶，以及来自智人的脯氨酰羟化酶结构域酶2和缺氧诱导因子-1抑制因子，都将几乎完全源自双氧的单个氧原子掺入到琥珀酸副产物中。
