Characterization of the maleylacetate reductase MacA of Rhodococcus opacus 1CP and evidence for the presence of an isofunctional enzyme.

@article{Seibert1998CharacterizationOT,
  title={Characterization of the maleylacetate reductase MacA of Rhodococcus opacus 1CP and evidence for the presence of an isofunctional enzyme.},
  author={Volker Seibert and E M Kourbatova and Ludmila Alexeevna Golovleva and Michael Schl{\"o}mann},
  journal={Journal of bacteriology},
  year={1998},
  volume={180 14},
  pages={3503-8}
}
Maleylacetate reductases (EC 1.3.1.32) have been shown to contribute not only to the bacterial catabolism of some usual aromatic compounds like quinol or resorcinol but also to the degradation of aromatic compounds carrying unusual substituents, such as halogen atoms or nitro groups. Genes coding for maleylacetate reductases so far have been analyzed mainly in chloroaromatic compound-utilizing proteobacteria, in which they were found to belong to specialized gene clusters for the turnover of… CONTINUE READING

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