Pyruvic oxime dioxygenase from the heterotrophic nitrifier Alcaligenes faecalis:: Purification, and molecular and enzymatic properties
Pyruvic oxime dioxygenase from the heterotrophic nitrifier Alcaligenes faecalis:: Purification, and molecular and enzymatic properties
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DOI：
10.1093/oxfordjournals.pcp.a029473
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发表时间：
1999-01-01
影响因子：
4.9
通讯作者：
Yamanaka, T
中科院分区：
文献类型：
--
作者：
Ono, Y;Enokiya, A;Yamanaka, T
从异养硝化菌Alcaligenes faecalis IFO 13111中纯化了一种将亚硝酸盐肟氧化为亚硝酸盐的酶。该酶的分子量为115 kDa，其分子由3个分子量相同的亚基组成，分子量为40 kDa。该酶分子中含有3个非血红素铁原子，当铁原子处于亚铁态时具有活性。该酶消耗1 mol O-2，从1 mol丙酮酸肟形成1 mol亚硝酸盐和丙酮酸盐。因此，该酶被认为是一种双加氧酶。
From the heterotrophic nitrifier Alcaligenes faecalis IFO 13111, an enzyme was purified which oxidized pyruvic oxime to nitrite. The molecular mass of the enzyme was 115 kDa and its molecule was composed of three molecules of subunits with the same molecular mass of 40 kDa. The enzyme contained 3 atoms of nonheme iron in the molecule and was active when the iron atoms were in a ferrous state. The enzyme consumed one mol of O-2 to form one mol each of nitrite and pyruvate from one mol of pyruvic oxime. Therefore, the enzyme was thought to be a pyruvic oxime dioxygenase.