Subramanian V, Vaidyanathan C S
J Bacteriol. 1984 Nov;160(2):651-5. doi: 10.1128/jb.160.2.651-655.1984.
Anthranilate hydroxylase from Aspergillus niger catalyzes the oxidative deamination and dihydroxylation of anthranilic acid to 2,3-dihydroxybenzoic acid. This enzyme has been purified to homogeneity and has a molecular weight of 89,000. The enzyme is composed of two subunits of 42,000 with 2 gram-atoms of nonheme iron per mol. Fe2+-chelators like alpha,alpha'-dipyridyl and o-phenanthroline are potent inhibitors of the enzyme activity. Absorption and fluorescence spectra of the enzyme offer no evidence for the presence of other cofactors like flavin. Flavins and flavin-specific inhibitors like atebrin have no effect on the activity of the enzyme. The enzyme incorporates one atom of oxygen each from 18O2 and H218O into the product 2,3-dihydroxybenzoic acid. Based on these studies, it is concluded that anthranilate hydroxylase from A. niger is a new type of NADPH-linked nonheme iron monooxygenase.
黑曲霉邻氨基苯甲酸羟化酶催化邻氨基苯甲酸氧化脱氨并二羟基化生成2,3 -二羟基苯甲酸。该酶已被纯化至同质，分子量为89,000。该酶由两个42,000的亚基组成，每摩尔含有2克原子的非血红素铁。Fe2 +螯合剂如α,α'-联吡啶和邻菲罗啉是该酶活性的有效抑制剂。该酶的吸收光谱和荧光光谱没有提供存在其他辅因子如黄素的证据。黄素和黄素特异性抑制剂如阿的平对该酶的活性没有影响。该酶将来自18O2和H218O的一个氧原子分别掺入产物2,3 -二羟基苯甲酸中。基于这些研究，得出结论，黑曲霉邻氨基苯甲酸羟化酶是一种新型的NADPH连接的非血红素铁单加氧酶。
