来自恶臭假单胞菌的对甲酚-（受体）氧化还原酶（羟化）（一种黄素细胞色素）的纯化及性质
The purification and properties of p-cresol-(acceptor) oxidoreductase (hydroxylating), a flavocytochrome from Pseudomonas putida.
作者信息
Hopper D J, Taylor D G
出版信息
Biochem J. 1977 Oct 1;167(1):155-62. doi: 10.1042/bj1670155.
Abstract
The enzyme that catalyses the hydroxylation of the methyl group of p-cresol was purified from Pseudomonas putida. It has mol.wt. 115000 and appears to contain two subunits of equal molecular weight. One subunit is a c-type cytochrome and the other is a flavoprotein. Reduction of the cytochrome occurred on addition of substrate. The same enzyme catalyses both p-cresol hydroxylation and the further oxidation of the product, 4-hydroxybenzyl alcohol. The stoicheiometry of acceptor reduced per molecule of substrate oxidized is that for two dehydrogenation reactions. The Km for p-cresol is 7.3 x 10(-6) M and that for 4-hydroxybenzyl alcohol is 47.6 x 10(-6) M. The enzyme, which is assayed with phenazine methosulphate as electron acceptor, was stimulated by particulate material, which probably contains the acceptor in vivo.
摘要
催化对甲酚甲基羟基化反应的酶是从恶臭假单胞菌中纯化得到的。它的分子量为115000，似乎包含两个分子量相等的亚基。一个亚基是c型细胞色素，另一个是黄素蛋白。添加底物后细胞色素发生还原反应。同一种酶既催化对甲酚的羟基化反应，也催化产物4-羟基苄醇的进一步氧化反应。每氧化一分子底物时被还原的受体的化学计量关系符合两个脱氢反应。对甲酚的米氏常数为7.3×10⁻⁶M，4-羟基苄醇的米氏常数为47.6×10⁻⁶M。以吩嗪硫酸甲酯作为电子受体来测定该酶活性时，其活性受到颗粒物质的刺激，这种颗粒物质在体内可能含有受体。
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