Literature summary for 1.14.18.3 extracted from

Xin, J.Y.; Cui, J.R.; Hu, X.X.; Li, S.B.; Xia, C.G.; Zhu, L.M.; Wang, Y.Q.
Particulate methane monooxygenase from Methylosinus trichosporium is a copper-containing enzyme (2002), Biochem. Biophys. Res. Commun., 295, 182-186.

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General Stability

General Stability	Organism
copper ions increase the stability of exfoliated pMMO	Methylosinus trichosporium

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
membrane	membrane-bound particulate enzyme form termed pMMO	Methylosinus trichosporium	16020	-

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Cu2+	pMMO contains tightly bound copper, EDTA has no effect	Methylosinus trichosporium

Organism

Organism	UniProt	Comment	Textmining
Methylosinus trichosporium	-	-	-
Methylosinus trichosporium IMV 3011	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
pMMO	Methylosinus trichosporium

Renatured (Commentary)

Renatured (Comment)	Organism
copper ions increase the stability of exfoliated pMMO	Methylosinus trichosporium

Synonyms

Synonyms	Comment	Organism
MMO	-	Methylosinus trichosporium
pMMO	particulate, membrane-bound enzyme form	Methylosinus trichosporium

Cofactor

Cofactor	Comment	Organism	Structure
NADH	not: pMMO	Methylosinus trichosporium

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Release 2023.1 (January 2023)