Literature summary for 1.14.18.3 extracted from

Culpepper, M.A.; Cutsail, G.E.; Hoffman, B.M.; Rosenzweig, A.C.
Evidence for oxygen binding at the active site of particulate methane monooxygenase (2012), J. Am. Chem. Soc., 134, 7640-7643.

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Protein Variants

Protein Variants	Comment	Organism
H137A/H139A	the mutant of subunit domain spmoB disrupts the dicopper site and exhibits no activity	Methylococcus capsulatus
H48N	the mutant of subunit domain spmoB disrupts the monocopper site, but still exhibits enzyme activity	Methylococcus capsulatus
H48N/H137A/H139A	the mutant of subunit domain spmoB disrupts the dicopper site and exhibits no activity	Methylococcus capsulatus

Metals/Ions

Metals/Ions	Comment	Organism	Structure
copper	the enzyme contains a dicopper center	Methylococcus capsulatus

Organism

Organism	UniProt	Comment	Textmining
Methylococcus capsulatus	-	-	-

Subunits

Subunits	Comment	Organism
heterotrimer	2 * 000, calculated from amino acid sequence	Methylococcus capsulatus

Synonyms

Synonyms	Comment	Organism
particulate methane monooxygenase	-	Methylococcus capsulatus
pMMO	-	Methylococcus capsulatus
spmoB	recombinant soluble domains of the pmoB subunit of particulate methane monooxygenase	Methylococcus capsulatus

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Release 2023.1 (January 2023)