A novel coenzyme from bacterial primary alcohol dehydrogenases

  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},
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.



Substrate Specificity of the Purified Primary Alcohol Dehydrogenases from Methanol-Oxidizing Bacteria

A possible explanation for this specificity, with regard to aldehydes, is presented in terms of degree of hydration of the aldehyde.

Hexose phosphate synthese and tricarboxylic acid-cycle enzymes in bacterium 4B6, an obligate methylotroph.

Of 49 compounds tested, only methylamine, dimethylamine or trimethylamines supports the growth of one isolate, bacterium 4B 6, indicating that this organism is a new type of obligate methylotroph.

Microbial Oxidation of Methane and Methanol: Crystallization of Methanol Dehydrogenase and Properties of Holo- and Apo-Methanol Dehydrogenase from Methylomonas methanica

The crystalline methanol dehydrogenase had an absorption peak at 350 nm in the visible region and weak fluorescence peaks at 440 and 470 nm due to the presence of a pteridine derivative as the prosthetic group and was catalytically inactive.

The microbial oxidation of methanol. The prosthetic group of the alcohol dehydrogenase of Pseudomonas sp. M27: a new oxidoreductase prosthetic group.

Data are given that support the suggestion that the prosthetic group of the enzyme is a pteridine derivative, and Kinetic studies show a correlation between enzyme inactivation by acid, alkali or heat and liberation of the fluorescent material.

Oxidation of C1 compounds by particulate fractions from Methylococcus capsulatus: properties of methanol oxidase and methanol dehydrogenase

It is suggested that the major site of methanol and formaldehyde oxidation in M. capsulatus occurs on the intracytoplasmic membranes in vivo and is coupled to oxygen reduction.

Effect of Monovalent Cations on the Malic Enzyme from the Extreme Halophile, Halobacterium cutirubrum

The malic enzyme from Halobacterium cutirubrum requires monovalent cations for both activation and stabilization, and results support the idea that the roles of salts in both processes are different.