Literature summary 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

General Stability

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

Localization

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

Metals/Ions

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

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.14.18.3	Methylosinus trichosporium	-	-	-

Storage Stability

EC Number	Storage Stability	Organism
1.14.18.3	4°C, membrane-bound enzyme, activity is lost after 24 h, can be stabilized by succinate	Methylosinus trichosporium

Substrates and Products (Substrate)

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

Synonyms

EC Number	Synonyms	Comment	Organism
1.14.18.3	MMO	-	Methylosinus trichosporium

Cofactor

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

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Release 2023.1 (January 2023)