Hammer A, Stolz A, Knackmuss H
Institut für Mikrobiologie, Universität Stuttgart, Allmandring 31, D-70569 Stuttgart, Germany.
Arch Microbiol. 1996 Aug;166(2):92-100. doi: 10.1007/s002030050361.
4-Aminobenzenesulfonate is degraded via 4-sulfocatechol by a mixed bacterial culture that consists of Hydrogenophaga palleronii strain S1 and Agrobacterium radiobacter strain S2. From the 4-sulfocatechol-degrading organism A. radiobacter strain S2, a dioxygenase that converted 4-sulfocatechol to 3-sulfomuconate was purified to homogeneity. The purified enzyme also converted protocatechuate with a similar catalytic activity to 3-carboxy-cis, cis-muconate. Furthermore, the purified enzyme oxidized 3, 4-dihydroxyphenylacetate, 3,4-dihydroxycinnamate, catechol, and 3- and 4-methylcatechol. The enzyme had a mol. wt. of about 97,400 as determined by gel filtration and consisted of two different types of subunits with mol. wt. of about 23,000 and 28,500. The NH2-terminal amino acid sequences of the two subunits were determined. An isofunctional dioxygenase was partially purified from H. palleronii strain S1. A. radiobacter strain S2 also induced, after growth with 4-sulfocatechol, an rising dbl quote, "ordinary" protocatechuate 3,4-dioxygenase that did not oxidize 4-sulfocatechol. This enzyme was also purified to homogeneity, and its catalytic and structural characteristics were compared to the "4-sulfocatechol-dioxygenase" from the same strain.
4-氨基苯磺酸盐通过4-磺酸儿茶酚被一种混合细菌培养物降解，该培养物由苍白嗜氢菌菌株S1和放射形土壤杆菌菌株S2组成。从4-磺酸儿茶酚降解菌放射形土壤杆菌菌株S2中，纯化得到一种将4-磺酸儿茶酚转化为3-磺酸粘康酸的双加氧酶，使其达到同质。纯化后的酶还以类似的催化活性将原儿茶酸转化为3-羧基-顺，顺-粘康酸。此外，纯化后的酶能氧化3,4-二羟基苯乙酸、3,4-二羟基肉桂酸、儿茶酚以及3-和4-甲基儿茶酚。通过凝胶过滤测定，该酶的分子量约为97,400，由两种不同类型的亚基组成，分子量分别约为23,000和28,500。测定了这两个亚基的氨基末端氨基酸序列。从苍白嗜氢菌菌株S1中部分纯化得到一种同功能双加氧酶。放射形土壤杆菌菌株S2在用4-磺酸儿茶酚生长后，还诱导产生了一种“普通”的原儿茶酸3,4-双加氧酶，该酶不能氧化4-磺酸儿茶酚。这种酶也被纯化至同质，并将其催化和结构特性与同一菌株的“4-磺酸儿茶酚双加氧酶”进行了比较。
