Purification and some properties of the tungsten-containing carboxylic acid reductase from Clostridium formicoaceticum.

@article{White1991PurificationAS,
  title={Purification and some properties of the tungsten-containing carboxylic acid reductase from Clostridium formicoaceticum.},
  author={Hiltrud U. White and Richard Feicht and Christoph Huber and Friedrich Lottspeich and Helmut Simon},
  journal={Biological chemistry Hoppe-Seyler},
  year={1991},
  volume={372 11},
  pages={999-1005}
}
Judged by properties observed during the purification and based on the sequence of the first 25 amino acids, the enzyme from Clostridium formicoaceticum catalysing the reversible reduction of non-activated carboxylic acids to aldehydes at the expense of reduced viologens, is astonishingly different from that found by us in C. thermoaceticum. According to native and SDS gel electrophoresis the reductase is nearly homogeneous after only 26-fold purification. The specificity for various substrates… CONTINUE READING

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