Synthesis of Certain Assimilatory and Dissimilatory Enzymes during Bacterial Adaptation to Growth on Trimethylamine

Boulton, Chris A.; Large, Peter J.

doi:10.1099/00221287-101-1-151

Cited by 24 publications

(10 citation statements)

References 22 publications

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“…However, the failure to detect any increase in activity during growth on C, compounds was more indicative of the enzyme having no role in the metabolism of C, compounds. This observation, although consistently found in the survey of organisms in this study, was in contrast to the initial report of Johnson & Quayle (1964) and also that of Boulton & Large (1977). The latter authors showed that when Pseudomonas aminovorans was transferred from a medium containing succinate as the carbon source to one containing trimethylamine certain enzymes associated with the metabolism of C, compounds were induced during the phase of adaptation by the bacteria to growth on the second substrate, Some of these enzymes, including the glutathione-and NAD+-dependent formaldehyde dehydrogenase, showed a rapid increase in specific enzyme activity, whilst others, including the dye-lin ked formaldehyde dehydrogenase, increased in specific activity only slowly.…”

Section: Discussioncontrasting

confidence: 56%

“…Two of these enzymes are dye-linked, with the NH,+-independent enzyme having significantly low activity. A low activity for this enzyme has been reported by several workers (Johnson & Quayle, 1964;Boulton & Large, 1977;Bamforth & O'Connor, 1979). This could be a reflection of the true activity of the enzyme or a result of measuring the activity using non-physiological dyes as electron acceptors.…”

Section: Discussionmentioning

confidence: 98%

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Partial Purification and Characterization of a Dye-linked Formaldehyde Dehydrogenase from Hyphomierobium X

Marison¹,

Attwood²

1980

Microbiology

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All organisms surveyed among a range of methylotrophic bacteria growing on both C, and multi-carbon substrates contained a dye-linked formaldehyde dehydrogenase. The activity of this enzyme was very low in bacteria grown on C, compounds when compared to the activities of other C,-specific enzymes and was not induced during growth on C, compounds. The enzyme was partially purified (1 1-fold) from methanol-and ethanolgrown Hyphomicrobium X. Though not homogeneous, it did not contain methanol dehydrogenase, formate dehydrogenase or cytochrome c. Methylphenazonium methylsulphate (PMS), cytochrome c, Wurster's Blue, dichlorophenol-indophenol (DCPIP) and methylphenazonium ethosulphate (PES) could act as the primary electron acceptors in the assay system with apparent K, values for the first three substances of 0.69, 128 and 3.07 ,!AM, respectively. The activity of the partially purified enzyme could be maintained over 3 months at -20 "C in the presence of ethanol (lo%, v/v). The molecular weight of the enzyme was 83 500 k 2500. It was active from pH 6.5 to 9-0 with maximum activity at pH 7.2 using cytochrome c as the electron acceptor and at pH 7.6 when PMS and DCPIP were used. Several different aldehydes could act as substrates; the apparent Km values for formaldehyde, acetaldehyde, propionaldehyde and heptaldehyde were 2860, 270, 13 and 2.5 ,UM, respectively. Methanol and ethanol were not substrates. The dye-linked formaldehyde dehydrogenase is probably a general aldehyde dehydrogenase not directly involved in the dissimilation of C1 compounds.

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Section: Discussioncontrasting

confidence: 56%

Section: Discussionmentioning

confidence: 98%

Partial Purification and Characterization of a Dye-linked Formaldehyde Dehydrogenase from Hyphomierobium X

Marison¹,

Attwood²

1980

Microbiology

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“…Microbial degradation of trimethylamine by aerobic bacteria (Colby and Zatman 1973;Boulton and Large 1977;Steenkamp and Mallinson 1976;Large and Haywood 1981;Levering et al 1981;Urakami et al 1990;Ohara et al 1990) and in laboratory-scale bioreactors (Partidário and Carrondo 1993;Lobo et al 1997) have been intensively studied. Although aerobic degradation is effective for the microbial removal of trimethylamine, molecular oxygen may not always be available in contaminated sites, possibly because of its prompt depletion by aerobic metabolism itself and its low solubility in water.…”

Section: Introductionmentioning

confidence: 99%

A novel denitrifying bacterial isolate that degrades trimethylamine both aerobically and anaerobically via two different pathways

Kim

Bae

Lee

2001

Archives of Microbiology

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The aerobic and anaerobic degradation of trimethylamine by a newly isolated denitrifying bacterium from an enrichment culture with trimethylamine inoculated with activated sludge was studied. Based on 16S rDNA analysis, this strain was identified as a Paracoccus sp. The isolate, strain T231, aerobically degraded trimethylamine, dimethylamine and methylamine and released a stoichiometric amount of ammonium ion into the culture fluid as a metabolic product, indicating that these methylated amines were completely degraded to formaldehyde and ammonia. The strain degraded trimethylamine also under denitrifying conditions and consumed a stoichiometric amount of nitrate, demonstrating that complete degradation of trimethylamine was coupled with nitrate reduction. Cell-free extract prepared from cells grown aerobically on trimethylamine exhibited activities of trimethylamine mono-oxygenase, trimethylamine N-oxide demethylase, dimethylamine mono-oxygenase, and methylamine mono-oxygenase. Cell-free extract from cells grown anaerobically on trimethylamine and nitrate exhibited activities of trimethylamine dehydrogenase and dimethylamine dehydrogenase. These results indicate that strain T231 had two different pathways for aerobic and anaerobic degradation of trimethylamine. This is a new feature for trimethylamine metabolism in denitrifying bacteria.

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“…to their substrate specificity (Johnson & Quayle, 1964;Pate1 & Hoare, 1971;Boulton & Large, 1977). The FDH enzyme isolated from Methylococcus capsulatus (Bath) is particularly unusual in that it required a heat-stable (70 "C/12 min) dialysable protein for activity.…”

Section: S T a T E A N D H D A L T O Nmentioning

confidence: 99%

A low-molecular-mass protein from Methylococcus capsulatus (Bath) is responsible for the regulation of formaldehyde dehydrogenase activity in vitro

Tate¹,

Dalton²

1999

Microbiology

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An 8 6 kDa protein, which the authors call a modifin, has been purified from Methylococcus capsulatus (Bath) and has been shown to alter the substrate specificity and kinetics of NAD+-linked formaldehyde dehydrogenase (FDH) isolated from the same organism. Purification methods for both the modifin and FDH are presented which reliably produced pure protein for further analysis. Analysis of the molecular mass and N-terminal sequence of both FDH and the modifin indicate that they are unique proteins and show no similarity to alcohol or aldehyde dehydrogenase enzymes isolated from methylotrophic bacteria. Substrate specificity studies demonstrated that FDH oxidized formaldehyde exclusively in the presence of the modifin; a diverse range of aldehydes and alcohols were oxidized by FDH in the absence of the modifin. No formaldehyde oxidation was detected in the absence of the modifin. Attempts to replace the modifin with glutathione or high concentrations of methanol to stimulate formaldehyde oxidation failed. With acetaldehyde as substrate, FDH showed standard Michaelis-Menten kinetics; interaction of FDH with the modifin using formaldehyde as substrate altered the kinetics of the reaction to sigmoidal. Kinetic analysis during turnover experiments indicated that the FDH may be associated with bound formaldehyde following enzyme isolation and that NAD may also be associated with the enzyme but in a form that is less tightly bound than found with the methanol dehydrogenase from Bacillus methanolicus. Data are presented which indicate that the modifin may play an important role in regulating formaldehyde concentration in vivo.

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Synthesis of Certain Assimilatory and Dissimilatory Enzymes during Bacterial Adaptation to Growth on Trimethylamine

Cited by 24 publications

References 22 publications

Partial Purification and Characterization of a Dye-linked Formaldehyde Dehydrogenase from Hyphomierobium X

Partial Purification and Characterization of a Dye-linked Formaldehyde Dehydrogenase from Hyphomierobium X

A novel denitrifying bacterial isolate that degrades trimethylamine both aerobically and anaerobically via two different pathways

A low-molecular-mass protein from Methylococcus capsulatus (Bath) is responsible for the regulation of formaldehyde dehydrogenase activity in vitro

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