Formaldehyde dehydrogenase preparations from Methylococcus capsulatus (Bath) comprise methanol dehydrogenase and methylene tetrahydromethanopterin dehydrogenase

Microbiology ◽  
2004 ◽  
Vol 150 (3) ◽  
pp. 707-713 ◽  
Author(s):  
Ekundayo K. Adeosun ◽  
Thomas J. Smith ◽  
Anne-Mette Hoberg ◽  
Giles Velarde ◽  
Robert Ford ◽  
...  
Keyword(s):  
Methanol Dehydrogenase ◽  
Formaldehyde Dehydrogenase ◽  
Methylococcus Capsulatus

scholarly journals Membrane-Associated Quinoprotein Formaldehyde Dehydrogenase from Methylococcus capsulatus Bath

2001 ◽  
Vol 183 (23) ◽  
pp. 6832-6840 ◽  
Author(s):  
James A. Zahn ◽  
David J. Bergmann ◽  
Jeffery M. Boyd ◽  
Ryan C. Kunz ◽  
Alan A. DiSpirito
Keyword(s):  
Methane Monooxygenase ◽  
Cell Protein ◽  
Formaldehyde Dehydrogenase ◽  
Methylococcus Capsulatus ◽  
Visible Absorption ◽  
Paramagnetic Resonance ◽  
Obligate Methylotroph ◽  
Major Activity ◽  
Cells Cultured ◽  
In Cells

ABSTRACT A membrane-associated, dye-linked formaldehyde dehydrogenase (DL-FalDH) was isolated from the obligate methylotrophMethylococcus capsulatus Bath. The enzyme was the major formaldehyde-oxidizing enzyme in cells cultured in high (above 1 μmol of Cu per mg of cell protein) copper medium and expressing the membrane-associated methane monooxygenase. Soluble NAD(P)+-linked formaldehyde oxidation was the major activity in cells cultured in low-copper medium and expressing the soluble methane monooxygenase (Tate and Dalton, Microbiology 145:159–167, 1999; Vorholt et al., J. Bacteriol. 180:5351–5356, 1998). The membrane-associated enzyme is a homotetramer with a subunit molecular mass of 49,500 Da. UV-visible absorption, electron paramagnetic resonance, and electrospray mass spectrometry suggest the redox cofactor of the DL-FalDH is pyrroloquinoline quinone (PQQ), with a PQQ-to-subunit stochiometry of approximately 1:1. The enzyme was specific for formaldehyde, oxidizing formaldehyde to formate, and utilized the cytochrome b 559/569 complex as the physiological electron acceptor.

scholarly journals Lysates of Methylococcus capsulatus Bath induce a lean-like microbiota, intestinal FoxP3+RORγt+IL-17+ Tregs and improve metabolism

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Benjamin A. H. Jensen ◽  
Jacob B. Holm ◽  
Ida S. Larsen ◽  
Nicole von Burg ◽  
Stefanie Derer ◽  
...  
Keyword(s):  
Western Diet ◽  
Liver Fat ◽  
Methylococcus Capsulatus ◽  
High Fat ◽  
Low Fat Diet ◽  
Reduced Body ◽  
Westernized Diet ◽  
Induced Changes ◽  
Immunological Homeostasis ◽  
Small And Large Intestine

AbstractInteractions between host and gut microbial communities are modulated by diets and play pivotal roles in immunological homeostasis and health. We show that exchanging the protein source in a high fat, high sugar, westernized diet from casein to whole-cell lysates of the non-commensal bacterium Methylococcus capsulatus Bath is sufficient to reverse western diet-induced changes in the gut microbiota to a state resembling that of lean, low fat diet-fed mice, both under mild thermal stress (T22 °C) and at thermoneutrality (T30 °C). Concomitant with microbiota changes, mice fed the Methylococcus-based western diet exhibit improved glucose regulation, reduced body and liver fat, and diminished hepatic immune infiltration. Intake of the Methylococcu-based diet markedly boosts Parabacteroides abundances in a manner depending on adaptive immunity, and upregulates triple positive (Foxp3+RORγt+IL-17+) regulatory T cells in the small and large intestine. Collectively, these data point to the potential for leveraging the use of McB lysates to improve immunometabolic homeostasis.

Metabolic alteration of Methylococcus capsulatus str. Bath during a microbial gas-phase reaction

2021 ◽  
Vol 330 ◽  
pp. 125002
Author(s):  
Yan-Yu Chen ◽  
Yuki Soma ◽  
Masahito Ishikawa ◽  
Masatomo Takahashi ◽  
Yoshihiro Izumi ◽  
...  
Keyword(s):  
Gas Phase ◽  
Phase Reaction ◽  
Methylococcus Capsulatus ◽  
Gas Phase Reaction ◽  
Metabolic Alteration

scholarly journals The three-dimensional structures of methanol dehydrogenase from two methylotrophic bacteria at 2.6-A resolution.

1992 ◽  
Vol 267 (31) ◽  
pp. 22289-22297
Author(s):  
Z.X. Xia ◽  
W.W. Dai ◽  
J.P. Xiong ◽  
Z.P. Hao ◽  
V.L. Davidson ◽  
...  
Keyword(s):  
Three Dimensional ◽  
Methanol Dehydrogenase ◽  
Methylotrophic Bacteria
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