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Literature summary for 1.14.18.3 extracted from

  • Yu, S.S.; Ji, C.Z.; Wu, Y.P.; Lee, T.L.; Lai, C.H.; Lin, S.C.; Yang, Z.L.; Wang, V.C.; Chen, K.H.; Chan, S.I.
    The C-terminal aqueous-exposed domain of the 45 kDa subunit of the particulate methane monooxygenase in Methylococcus capsulatus (Bath) is a Cu(I) sponge (2007), Biochemistry, 46, 13762-13774.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
two aqueous-exposed subdomains toward the N- and C-termini of the large subunit are expressed in Escherichia coli BL21 (DE3) cells Methylococcus capsulatus

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
Methylococcus capsulatus 16020
-

Metals/Ions

Metals/Ions Comment Organism Structure
Cu+ the C-terminal domain of PmoB in pMMO is a reservoir for Cu(I) with properties similar to those of the E-cluster copper ions in the intact holoenzyme Methylococcus capsulatus

Organism

Organism UniProt Comment Textmining
Methylococcus capsulatus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni2+-Sepharose Fast Flow column chromatography Methylococcus capsulatus

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
particulate methane monooxygenase
-
Methylococcus capsulatus
pMMO
-
Methylococcus capsulatus
PmoB large subunit of pMMO Methylococcus capsulatus