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Literature summary for 1.14.13.25 extracted from

  • Kalidass, B.; Ul-Haque, M.F.; Baral, B.S.; DiSpirito, A.A.; Semrau, J.D.
    Competition between metals for binding to methanobactin enables expression of soluble methane monooxygenase in the presence of copper (2015), Appl. Environ. Microbiol., 81, 1024-1031 .
    View publication on PubMedView publication on EuropePMC
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Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
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 Methylosinus trichosporium OB3b 5737
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Organism

Organism UniProt Comment Textmining
Methylosinus trichosporium OB3b P27353 and P27355 and P27354 and P27356 and Q53563 and Q53562 P27353 (alpha/MmoX), P27355 (gamma/MmoZ), P27354 (beta/MmoY), P27356 (MmoB), Q53563 (MmoC), Q53562 (MmoD). The soluble methane monooxygenase (sMMO) consists of four components A/MMOH (composed of alpha/MmoX, beta/MmoY and gamma/MmoZ), B/MMOB (MmoB), C/MMOR (MmoC) and D/MMOD (MmoD)
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Synonyms

Synonyms Comment Organism
sMMO
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 Methylosinus trichosporium OB3b
soluble methane monooxygenase
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 Methylosinus trichosporium OB3b

Expression

Organism Comment Expression
Methylosinus trichosporium OB3b soluble, methane monooxygenase (sMMO) is expressed and active in the presence of copper if gold is also simultaneously present. Such expression is due to gold binding to methanobactin produced by Methylosinus trichosporium OB3b, thereby limiting copper uptake. Such expression and activity is significantly reduced if methanobactin preloaded with copper is also added. Both soluble, methane monooxygenase (sMMO) and particulate methane monooxygenase (pMMO) can be expressed when copper and gold are present, as gold effectively competes with copper for binding to methanobactin. Under certain geochemical conditions, both forms of methane monooxygenase may be expressed and active in situ up