A novel coenzyme from bacterial primary alcohol dehydrogenases

@article{Salisbury1979ANC,
  title={A novel coenzyme from bacterial primary alcohol dehydrogenases},
  author={S. A. Salisbury and Hugh S. Forrest and William B. T. Cruse and Olga Kennard},
  journal={Nature},
  year={1979},
  volume={280},
  pages={843-844}
}
METHYLOTROPHIC bacteria are able to use methane derivatives as their sole source of carbon and metabolic energy and so can sustain growth on methane, methanol and other organic compounds which lack carbon–carbon bonds1. They are not autotrophic and, being unable to use carbon dioxide, rely ultimately on their ability to oxidise these substances. Although the primary alcohol dehydrogenases from a variety of methanol-grown bacteria have been purified and compared, and despite the increasing… 

Bacterial oxidation of methane and methanol.

  • C. Anthony
  • Chemistry
    Advances in microbial physiology
  • 1986

Quinoprotein alcohol dehydrogenase from a non-methylotroph, Acinetobacter calcoaceticus.

The A. calcoaceticus enzyme shows the broadest substrate specificity hitherto known for this type of enzyme in that it also oxidizes higher aldehydes, and arguments are presented for the idea that quinoprotein alcohol dehydrogenases exist in other alkane- or alcohol-grown bacteria.

Generation of products by methanotrophs.

The findings of Dalton and his colleagues that partially purified methane monooxygenase (MMO) preparations oxygenate a wide range of organic compounds, supported the hypothesis that these oxidations are a result of the lack of specificity of enzymes involved in the oxidation of methane to carbon dioxide.

Physiology and genetics of methylotrophic bacteria.

A comprehensive treatise on the regulation and molecular mechanism of methanol oxidation is presented, followed by the data that have become available through the use of genetic analysis.

Methanol dehydrogenase, a PQQ-containing quinoprotein dehydrogenase.

Methanol dehydrogenase (MDH) is a soluble quinoprotein which has pyrroloquinoline quinone (PQQ) as its prosthetic group and it uses a specific cytochrome, cy tochrome cL as electron acceptor.

Quinone-dependent alcohol dehydrogenases and fad-dependent alcohol oxidases

This review considers quinone-dependent alcohol dehydrogenases and FAD-dependent alcohol oxidases, enzymes that are present in numerous methylotrophic eu- and prokaryotes and significantly differ in

Quinoprotein ethanol dehydrogenase fromPseudomonas

Two dye-linked ethanol dehydrogenases from Pseudomonas aeruginosa and putida were purified to homogeneity and crystallized and found to have a low affinity for methanol and in addition to primary alcohols they also oxidize secondary alcohols.

Methanol dehydrogenase structure

Methanol dehydrogenase catalyzes the oxidation of methanol to formaldehyde, utilizing the single carbon compound as the sole source of carbon and energy.

PQQ and Quinoproteins

Dye-linked ethanol dehydrogenases from Pseudomonas aeruginosa ATCC and P. putida ATCC were purified to homogeneity and crystallized and are similar to the quinoprotein methanol dehydrogenase known from methylotrophic bacteria.
...

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