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Literature summary extracted from

  • Culpepper, M.A.; Rosenzweig, A.C.
    Structure and protein-protein interactions of methanol dehydrogenase from Methylococcus capsulatus (Bath) (2014), Biochemistry, 53, 6211-6219 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.18.3 recombinant expression of wild-type holoenzyme and truncated recombinant periplasmic domains of pMMO (spmoB) Methylococcus capsulatus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.14.18.3 membrane membrane-bound Methylococcus capsulatus 16020
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.14.18.3 300000
-
 alpha3beta3gamma3 trimer comprising three copies each of the pmoB (alpha), pmoA (beta), and pmoC (gamma) subunits Methylococcus capsulatus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.18.3 methane + quinol + O2 Methylococcus capsulatus
-
 methanol + quinone + H2O
-
 ?
1.14.18.3 methane + quinol + O2 Methylococcus capsulatus Bath
-
 methanol + quinone + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.18.3 Methylococcus capsulatus G1UBD1 AND Q607G3 alpha- and beta-subunits
-
1.14.18.3 Methylococcus capsulatus Bath G1UBD1 AND Q607G3 alpha- and beta-subunits
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.18.3 native holoenzyme from isolated membranes by solubilization with detergent n-dodecyl beta-D-maltoside, ultrafiltration, and gel filtration Methylococcus capsulatus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.18.3 methane + quinol + O2
-
 Methylococcus capsulatus methanol + quinone + H2O
-
 ?
1.14.18.3 methane + quinol + O2
-
 Methylococcus capsulatus Bath methanol + quinone + H2O
-
 ?

Subunits

EC Number Subunits Comment Organism
1.14.18.3 heterotrimer the pMMO is an about 300 kDa alpha3beta3gamma3 trimer comprising three copies each of the pmoB (alpha), pmoA (beta), and pmoC (gamma) subunits. The pmoA and pmoC subunits are composed primarily of transmembrane helices, and pmoB consists of two periplasmic cupredoxin-like domains linked by two transmembrane helices. The active site is proposed to be a dinuclear copper center located in the N-terminal pmoB periplasmic domain close to the membrane interface Methylococcus capsulatus

Synonyms

EC Number Synonyms Comment Organism
1.14.18.3 particulate MMO
-
 Methylococcus capsulatus
1.14.18.3 pMMO
-
 Methylococcus capsulatus

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.18.3 additional information the pMMO electron donor is generally thought to be ubiquinol generated by a type 2 NADH:quinone oxidoreductase. The addition of cytochrome could facilitate electron transfer without the requirement for NADH Methylococcus capsulatus
1.14.18.3 quinol the cofactor receives electrons from NADH Methylococcus capsulatus

General Information

EC Number General Information Comment Organism
1.14.18.3 metabolism in the initial steps of their metabolic pathway, methanotrophic bacteria oxidize methane to methanol with methane monooxygenases (MMOs) and methanol to formaldehyde with methanol dehydrogenases (MDHs). Membrane-bound particulate MMO (pMMO) and MDH interact to form a metabolic supercomplex, interaction analysis and biolayer interferometry studies demonstrate specific protein-protein interactions between methanol dehydrogenase (MDH) and Methyylococcus capsulatus (Bath) pMMO as well as between MDH and the truncated recombinant periplasmic domains of pMMO (spmoB), kinetics, overview Methylococcus capsulatus