Bioconversion of methane to cadaverine and lysine using an engineered type II methanotroph, Methylosinus trichosporium OB3b

2020 ◽  
Vol 22 (22) ◽  
pp. 7803-7811
Author(s):  
Thu Thi Nguyen ◽  
Ok Kyung Lee ◽  
Sanzhar Naizabekov ◽  
Eun Yeol Lee
Keyword(s):  
Metabolic Model ◽  
Type Ii ◽  
Methylosinus Trichosporium Ob3b ◽  
Methylosinus Trichosporium ◽  
Genome Scale

Cadaverine is an important monomer used for the production of bio-polyamides. Based on the genome-scale metabolic model of type II methanotroph, iMsOB3b1_cadaverine, we engineered Methylosinus trichosporium OB3b to produce cadaverine from methane.

scholarly journals Genome-Scale Metabolic Model Reconstruction and in Silico Investigations of Methane Metabolism in Methylosinus trichosporium OB3b

2020 ◽  
Vol 8 (3) ◽  
pp. 437 ◽  
Author(s):  
Sanzhar Naizabekov ◽  
Eun Yeol Lee
Keyword(s):  
Methane Oxidation ◽  
In Silico ◽  
Model Organism ◽  
Metabolic Model ◽  
Central Carbon Metabolism ◽  
Methylosinus Trichosporium Ob3b ◽  
Methylosinus Trichosporium ◽  
Specific Growth Rates ◽  
Methane Metabolism ◽  
Genome Scale

Methylosinus trichosporium OB3b is an obligate aerobic methane-utilizing alpha-proteobacterium. Since its isolation, M. trichosporium OB3b has been established as a model organism to study methane metabolism in type II methanotrophs. M. trichosporium OB3b utilizes soluble and particulate methane monooxygenase (sMMO and pMMO respectively) for methane oxidation. While the source of electrons is known for sMMO, there is less consensus regarding electron donor to pMMO. To investigate this and other questions regarding methane metabolism, the genome-scale metabolic model for M. trichosporium OB3b (model ID: iMsOB3b) was reconstructed. The model accurately predicted oxygen: methane molar uptake ratios and specific growth rates on nitrate-supplemented medium with methane as carbon and energy source. The redox-arm mechanism which links methane oxidation with complex I of electron transport chain has been found to be the most optimal mode of electron transfer. The model was also qualitatively validated on ammonium-supplemented medium indicating its potential to accurately predict methane metabolism in different environmental conditions. Finally, in silico investigations regarding flux distribution in central carbon metabolism of M. trichosporium OB3b were performed. Overall, iMsOB3b can be used as an organism-specific knowledgebase and a platform for hypothesis-driven theoretical investigations of methane metabolism.

scholarly journals Biocatalytic Oxidations of Substrates through Soluble Methane Monooxygenase from Methylosinus sporium 5

Catalysts ◽  
2018 ◽  
Vol 8 (12) ◽  
pp. 582 ◽  
Author(s):  
Yeo Park ◽  
Hee Yoo ◽  
Min Song ◽  
Dong-Heon Lee ◽  
Seung Lee
Keyword(s):  
Methane Monooxygenase ◽  
Cross Reactivity ◽  
Type Ii ◽  
Methylococcus Capsulatus ◽  
Specific Enzyme ◽  
Methylosinus Trichosporium Ob3b ◽  
Methylosinus Trichosporium ◽  
Catalytic Activities ◽  
Soluble Methane Monooxygenase ◽  
Fundamental Information

Methane, an important greenhouse gas, has a 20-fold higher heat capacity than carbon dioxide. Earlier, through advanced spectroscopy and structural studies, the mechanisms underlying the extremely stable C–H activation of soluble methane monooxygenase (sMMO) have been elucidated in Methylosinus trichosporium OB3b and Methylococcus capsulatus Bath. Here, sMMO components—including hydroxylase (MMOH), regulatory (MMOB), and reductase (MMOR)—were expressed and purified from a type II methanotroph, Methylosinus sporium strain 5 (M. sporium 5), to characterize its hydroxylation mechanism. Two molar equivalents of MMOB are necessary to achieve catalytic activities and oxidized a broad range of substrates including alkanes, alkenes, halogens, and aromatics. Optimal activities were observed at pH 7.5 for most substrates possibly because of the electron transfer environment in MMOR. Substitution of MMOB or MMOR from another type II methanotroph, Methylocystis species M, retained specific enzyme activities, demonstrating the successful cross-reactivity of M. sporium 5. These results will provide fundamental information for further enzymatic studies to elucidate sMMO mechanisms.

Genome-Scale Metabolic Model as a Virtual Platform to Reveal the Environmental Contribution of Methanogens

2017 ◽  
Vol 6 (2) ◽  
pp. 149-160 ◽  
Author(s):  
P. Chellapandi ◽  
M. Bharathi ◽  
R. Prathiviraj ◽  
R. Sasikala ◽  
M. Vikraman
Keyword(s):  
Metabolic Model ◽  
Environmental Contribution ◽  
Virtual Platform ◽  
Genome Scale

scholarly journals Predicting changes in renal metabolism after compound exposure with a genome-scale metabolic model

2021 ◽  
Vol 412 ◽  
pp. 115390
Author(s):  
Kristopher D. Rawls ◽  
Bonnie V. Dougherty ◽  
Kalyan C. Vinnakota ◽  
Venkat R. Pannala ◽  
Anders Wallqvist ◽  
...  
Keyword(s):  
Metabolic Model ◽  
Renal Metabolism ◽  
A Genome ◽  
Compound Exposure ◽  
Genome Scale

scholarly journals Methanobactin from Methylocystis sp. Strain SB2 Affects Gene Expression and Methane Monooxygenase Activity in Methylosinus trichosporium OB3b

2015 ◽  
Vol 81 (7) ◽  
pp. 2466-2473 ◽  
Author(s):  
Muhammad Farhan Ul-Haque ◽  
Bhagyalakshmi Kalidass ◽  
Alexey Vorobev ◽  
Bipin S. Baral ◽  
Alan A. DiSpirito ◽  
...  
Keyword(s):  
Gene Expression ◽  
Methane Monooxygenase ◽  
Particulate Methane Monooxygenase ◽  
Methylosinus Trichosporium Ob3b ◽  
Methylosinus Trichosporium ◽  
Monooxygenase Activity ◽  
Content Type ◽  
Soluble Methane Monooxygenase ◽  
A Subunit ◽  
Membrane Bound

ABSTRACTMethanotrophs can express a cytoplasmic (soluble) methane monooxygenase (sMMO) or membrane-bound (particulate) methane monooxygenase (pMMO). Expression of these MMOs is strongly regulated by the availability of copper. Many methanotrophs have been found to synthesize a novel compound, methanobactin (Mb), that is responsible for the uptake of copper, and methanobactin produced byMethylosinus trichosporiumOB3b plays a key role in controlling expression of MMO genes in this strain. As all known forms of methanobactin are structurally similar, it was hypothesized that methanobactin from one methanotroph may alter gene expression in another. WhenMethylosinus trichosporiumOB3b was grown in the presence of 1 μM CuCl2, expression ofmmoX, encoding a subunit of the hydroxylase component of sMMO, was very low.mmoXexpression increased, however, when methanobactin fromMethylocystissp. strain SB2 (SB2-Mb) was added, as did whole-cell sMMO activity, but there was no significant change in the amount of copper associated withM. trichosporiumOB3b. IfM. trichosporiumOB3b was grown in the absence of CuCl2, themmoXexpression level was high but decreased by several orders of magnitude if copper prebound to SB2-Mb (Cu-SB2-Mb) was added, and biomass-associated copper was increased. Exposure ofMethylosinus trichosporiumOB3b to SB2-Mb had no effect on expression ofmbnA, encoding the polypeptide precursor of methanobactin in either the presence or absence of CuCl2.mbnAexpression, however, was reduced when Cu-SB2-Mb was added in both the absence and presence of CuCl2. These data suggest that methanobactin acts as a general signaling molecule in methanotrophs and that methanobactin “piracy” may be commonplace.

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