Phenol degradation by an enterobacterium: a Klebsiella strain carries a TOL-like plasmid and a gene encoding a novel phenol hydroxylase.
Phenol degradation by an enterobacterium: a Klebsiella strain carries a TOL-like plasmid and a gene encoding a novel phenol hydroxylase.
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肠杆菌降解苯酚：克雷伯氏菌菌株携带 TOL 样质粒和编码新型苯酚羟化酶的基因。
DOI：
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发表时间：
1999
期刊：
影响因子：
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通讯作者：
M. Kaufmann
中科院分区：
文献类型：
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作者：
K. Heesche;T. Schwarz;M. Kaufmann
尽管描述了许多不同微生物的苯酚催化剂，但在肠细菌菌株中没有这种途径的实例。在这里，我们描述了一种产酸克雷伯氏菌菌株，它生长在苯酚作为唯一的碳和能量来源上。苯酚羟化酶作为苯酚降解的关键酶，已被纯化至表观均一。与其他苯酚羟化酶相比，克雷伯氏菌属的酶在几个性质上不同：（i）纯化蛋白的SDS-PAGE和凝胶过滤分析显示，该酶是分子量为156 kDa的单体;（ii）稳态动力学测量结果显示，苯酚的K（m）值为0.22 mM;（iii）该酶既依赖于NADPH/FAD，又对EDTA敏感。邻苯二酚（苯酚羟化酶的反应产物）的进一步降解可通过通常位于TOL或TOL样质粒上的有效易位途径发生。从克雷伯氏菌菌株制备这种质粒并进一步表征。给出的数据表明，分离的菌株表现出高效苯酚降解微生物的所有特征。
Although phenol catabolism is described for many different microorganisms, there is no example for such a pathway in an enterobacterial strain. Here we characterize a Klebsiella oxytoca strain that grows on phenol as the only source of carbon and energy. As the key enzyme of phenol degradation, phenol hydroxylase was purified to apparent homogeneity. Compared with other phenol hydroxylases, the Klebsiella enzyme differs with respect to several properties: (i) SDS-PAGE and gel-filtration analysis of the purified protein revealed that the enzyme is a monomer with a molecular mass of 156 kDa; (ii) steady-state kinetic measurements resulted in a K(m) value of 0.22 mM for phenol; and (iii) the enzyme is both dependent on NADPH/FAD and sensitive to EDTA. Further degradation of catechol, the reaction product of phenol hydroxylase, may occur via the effective meta-fission pathway often located on TOL or TOL-like plasmids. Such a plasmid was prepared from the Klebsiella strain and further characterized. The given data demonstrate that the isolated strain exhibits all characteristics of an efficient phenol-degrading microorganism.
DOI：
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发表时间：
1989-01
期刊：
The Journal of biological chemistry
影响因子：
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作者：
G. Beardsley;B. Moroson;E. C. Taylor;R. Moran
通讯作者：
G. Beardsley;B. Moroson;E. C. Taylor;R. Moran