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… Expand
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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. Expand
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This chapter focuses on the enzymes involved in the bacterial oxidation of methane and methanol to formaldehyde and the energy transduction systems involved in coupling these oxidations to ATP synthesis by way of electron transport chains, proton translocation, and the proton motive force. Expand
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  • C. Anthony
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  • Sub-cellular biochemistry
  • 2000
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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. Expand
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TLDR
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. Expand
Quinoprotein ethanol dehydrogenase fromPseudomonas
TLDR
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. Expand
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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 inExpand
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Methanol dehydrogenase (MEDH, EC 1.1.99.8) is a soluble quinoprotein located in the periplasmic space of many methylotrophic bacteria (Anthony, 1986). The enzyme catalyzes the oxidation of methanolExpand
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TLDR
The prosthetic group of glucose dehydrogenase is, like that of methanol dehydrogen enzyme [3-S], a ‘pyrroloquinoline quinone’ (PQQ) and the name ‘quinoproteins’ is proposed for this distinct class of dehydrogenases. Expand
PQQ and Quinoproteins
Dye-linked ethanol dehydrogenases from Pseudomonas aeruginosa ATCC 17 933 and P. putida ATCC 17 421 were purified to homogeneity and crystallized. The amino acid composition of the two enzymes isExpand
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