Molecular biology of bacterial methanol oxidation

Vries, G.E de

doi:10.1111/j.1574-6968.1986.tb01861.x

Cited by 20 publications

(10 citation statements)

References 134 publications

(202 reference statements)

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“…A similar cluster, mox-FJGI, has been found in Methylobacterium extorquens AM1 (for review see refs. 4,5). moxF is the structural gene for the a-subunit of methanol dehydrogenase [71] whereas the /3-subunit is encoded by moxI.…”

Section: Mox-operonmentioning

confidence: 99%

“…Tests to modify Paracoccus wild-type strains by transposon mutagenesis also showed comparably poor results [199] or even failed [4]. To overcome these obstacles de Vries et al [90] set out to create mutant strains with enhanced conjugational frequencies.…”

Section: Restriction/modification Sys-temsmentioning

confidence: 99%

“…by combining our present understanding of Paracoccus denitrificans with that of the closely related and more thoroughly investigated purple bacteria Rhodobacter capsulatus and Rhodobacter sphaeroides, and other related bacteria within the a-subdivision [1][2][3]. Paracoccus has also been discussed in recent reviews on the genetics of methylotrophic bacteria [4,5]. Analysis of available data allows proposal of a first model not only for a consensus promoter, but also for a common regulatory sequence motif which may be crucial for oxygen-dependent regulation of gene expression not only in bacteria.…”

Section: Introductionmentioning

confidence: 99%

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Genetics of Paracoccus denitrificans

Steinrücke

Ludwig

1993

FEMS Microbiology Letters

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Paracoccus has approx. 15 subunits [28]. The transcriptional organization of this NDH-l-cluster is presently unknown. NQ01 and NQ02 code for flavoproteins, NQ03 to NQ06 are genes for iron-sulfur proteins whereas NQ07 to NQ014 code for polypeptides of the hydrophobic protein fraction [28]. The gene order in this cluster is NQ07, NQ06, NQ05, NQ04, NO02, NQ01 NQ03, NQ08 NQ09, NQ010, NQ011, NQO12, NQ013, and NQ014.Upstream of NQ07 an open reading frame with homology to Escherichia coli uvrA is found. A reading frame with homology to E. coli biotin acetyl-CoA carboxylase ligase has been found downstream of the cluster [28].Sequences for two genes, NQ01 [29], encoding the NADH-binding subunit, and NQ02 [30], which codes for an iron-sulfur protein, have been published. Two URFs have been found; sequence similarities of URF2 to ctaG of the Paracoccus cta-operon suggest a possible role as an assembly protein, most probably in the attachment of iron [29,30,55]. Because of its simpler structure the Paracoccus complex is likely to play an important part in investigating inhibitory agents or the mode of complex formation during assembly. Mutant strains are presently not available.

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Section: Mox-operonmentioning

confidence: 99%

Section: Restriction/modification Sys-temsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Genetics of Paracoccus denitrificans

Steinrücke

Ludwig

1993

FEMS Microbiology Letters

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“…pyrroloquinoline quinone (PQQ) dependent methanol dehydrogenase (MDH; EC 1.1.99.8) for the initial oxidation of methanol (Anthony 1982(Anthony , 1986Duine et al 1978Duine et al , 1986de Vries 1986). The situation in Gram-positive methylotrophic bacteria is less clear as relatively few of these organisms have been isolated and studied in detail thus far (Dijkhuizen and Levering 1987).…”

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confidence: 99%

Methanol metabolism in thermotolerant methylotrophic Bacillus strains involving a novel catabolic NAD-dependent methanol dehydrogenase as a key enzyme

et al. 1989

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Abstract. The enzymology of methanol utilization in thermotolerant methytotrophic Bacillus strains was investigated. In all strains an immunological]y related NAD-dependent methanol dehydrogenase was involved in the initial oxidation of methanol. In cells of Bacillus sp. C1 grown under methanol-limiting conditions this enzyme constituted a high percentage of total soluble protein. The methanol dehydrogenase from this organism was purified to homogeneity and characterized. In cell-free extracts the enzyme displayed biphasic kinetics towards methanol, with apparent Km values of 3.8 and 166 mM. Carbon assimilation was by way of the fructose-1,6-bisphosphate aldolase cleavage and transketolase/transaldolase rearrangement variant of the RuMP cycle of formaldehyde fixation. The key enzymes of the RuMP cycle, hexulose-6-phosphate synthase (HPS) and hexulose-6-phosphate isomerase (HPI), were present at very high levels of activity. Failure of whole cells to oxidize formate, and the absence of formaldehyde-and formate dehydrogenases indicated the operation of a non-linear oxidation sequence for formaldehyde via HPS. A comparison of the levels of methanol dehydrogenase and HPS in cells of Bacillus sp. C1 grown on methanol and glucose suggested that the synthesis of these enzymes is not under coordinate control.

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“…Methanol is naturally produced in the anaerobic metabolism of many varieties of bacteria and is Chaiyasut et al 4357 ubiquitous in the environment (Vries, 1986;Schrader et al, 2009). It is also presented as a consequence of enzymatic degradation of pectins.…”

Section: Introductionmentioning

confidence: 99%

Factors affecting methanol content of fermented plant beverage containing Morinda citrifolia

Chaiyasut¹,

Jantavong²,

Kruatama³

et al. 2013

Afr. J. Biotechnol.

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Pectin extraction of fresh Morinda citrifolia Linn or Noni using HCl at various concentrations was studied. The highest pectin yield (9.89% w/w) was achieved by using 20 mM HCl. Pectinmethylesterase (PME) activity and specific activity of raw M. citrifolia were 0.276 (µmol/ml. min) and 1.48 (Units/mg), respectively whereas, in the ripen M. citrifolia, they were 1.006 (µmol/ml. min) and 2.96 (Units/mg), respectively. Four formulas (F1, F2, F3 and F4) of the fermented plant beverage (FPBs) were prepared by varying material size (blended and diced) and sterilization process [72°C and using potassium metabisulfite (KMS)] using factorial design. Soluble pectin in FPBs using blended material (F3 and F4) was higher than in FPBs using diced material (F1 and F2). Soluble pectin in FPBs using pasteurization (F1 and F3) was also higher than FPBs using KMS (F2 and F4). At 24 h fermented period, methanol concentration in FPBs using blended material (F3 and F4) was higher than FPBs using diced material (F1 and F2). Methanol concentration in FPBs using KMS (F2 and F4) was also higher than FPBs using pasteurization (F1 and F3). After 24 h fermentation time, methanol concentration in FPBs using blended material (F3 and F4) could not be detected until the end of the fermentation whereas, in FPBs using diced material, methanol was found throughout the fermentation (F1 and F2). The study indicates that the most influencial factor on methanol production in FPBs was raw material size. Other factors were sterilization, PME and pectin, respectively. Thus, the recommended procedure of the fermentation of plant beverage was the use of blended raw M. citrifolia and pasteurization at 72°C for 15 s. These conditions prevent methanol production in FPBs. Therefore, quality and safety of the FPBs will be accepted by consumers.

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Molecular biology of bacterial methanol oxidation

Cited by 20 publications

References 134 publications

Genetics of Paracoccus denitrificans

Genetics of Paracoccus denitrificans

Methanol metabolism in thermotolerant methylotrophic Bacillus strains involving a novel catabolic NAD-dependent methanol dehydrogenase as a key enzyme

Factors affecting methanol content of fermented plant beverage containing Morinda citrifolia

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