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Literature summary for 1.14.18.3 extracted from

  • Cornish, A.; MacDonald, J.; Burrows, K.J.; King, T.S.; Scott, D.; Higgins, I.J.
    Succinate as an in vitro electron donor for the particulate methane mono-oxygenase of Methylosinus trichosporium (1985), Biotechnol. Lett., 7, 319-324.
No PubMed abstract available
Search for more literature for 1.14.18.3

General Stability

General Stability Organism
instability of enzyme in crude extract Methylosinus trichosporium
succinate stabilizes the membrane-bound enzyme Methylosinus trichosporium

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm enzyme from cells grown under conditions of low copper availability Methylosinus trichosporium 5737
-
membrane enzyme from cells grown under conditions of high copper availability is membrane-bound Methylosinus trichosporium 16020
-

Metals/Ions

Metals/Ions Comment Organism Structure
Cu2+ copper genetically regulates the enzyme activity of the soluble and membrane-bound form Methylosinus trichosporium

Organism

Organism UniProt Comment Textmining
Methylosinus trichosporium
-
-
-

Storage Stability

Storage Stability Organism
4°C, membrane-bound enzyme, activity is lost after 24 h, can be stabilized by succinate Methylosinus trichosporium

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
methane + reduced acceptor + H* + O2
-
 Methylosinus trichosporium methanol + acceptor + H2O
-
 ?

Synonyms

Synonyms Comment Organism
MMO
-
 Methylosinus trichosporium

Cofactor

Cofactor Comment Organism Structure
additional information succinate, particulate enzyme functions in vitro with either succinate or NADH as electron donor, soluble enzyme functions only with NADH Methylosinus trichosporium
NADH
-
 Methylosinus trichosporium
succinate electron donor, membrane-bound enzyme Methylosinus trichosporium