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Literature summary for 1.14.18.3 extracted from

  • Zhang, S.; Karthikeyan, R.; Fernando, S.
    Low-temperature biological activation of methane structure, function and molecular interactions of soluble and particulate methane monooxygenases (2017), Rev. Environ. Sci. Biotechnol., 16, 611-623 .
No PubMed abstract available

Application

Application Comment Organism
energy production teh enzyme can be used as biocatalysts for industrial activation of methane at relatively low temperatures required for breaking the highly stable C-H bond(s) Methylococcus capsulatus

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
Methylosinus trichosporium 16020
-
membrane
-
Methylocystis sp. 16020
-
membrane membrane-bound Methylococcus capsulatus 16020
-

Metals/Ions

Metals/Ions Comment Organism Structure
copper the metal center consists of multiple copper centers, a dicopper center and a mono-copper center. Methane activation occurs at the Cu centers of particulate methane monooxygenase Methylosinus trichosporium
copper the metal center consists of multiple copper centers, a dicopper center and a mono-copper center. Methane activation occurs at the Cu centers of particulate methane monooxygenase Methylocystis sp.
Cu2+ required for activity, each of pmoA, pmoB, and pmoC houses a dicopper center Methylococcus capsulatus
additional information the pMMO active site might possess a di-iron center located at the transmembrane zinc/copper site Methylococcus capsulatus
Zn2+ enzyme-bound Methylococcus capsulatus

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Methylococcus capsulatus G1UBD1 AND Q607G3 alpha- and beta-subunits
-
Methylococcus capsulatus Bath G1UBD1 AND Q607G3 alpha- and beta-subunits
-
Methylocystis sp.
-
-
-
Methylocystis sp. Rockwell
-
-
-
Methylosinus trichosporium
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
methane + quinol + O2
-
Methylococcus capsulatus methanol + quinone + H2O
-
?
methane + quinol + O2 methane activation occurs at the Cu centers of particulate methane monooxygenase Methylosinus trichosporium methanol + quinone + H2O
-
?
methane + quinol + O2 methane activation occurs at the Cu centers of particulate methane monooxygenase Methylocystis sp. methanol + quinone + H2O
-
?
methane + quinol + O2
-
Methylococcus capsulatus Bath methanol + quinone + H2O
-
?
methane + quinol + O2 methane activation occurs at the Cu centers of particulate methane monooxygenase Methylocystis sp. Rockwell methanol + quinone + H2O
-
?

Subunits

Subunits Comment Organism
heterotrimer enzyme pMMO possesses an alpha3beta3gamma3 trimeric structure composed of the pmoB, pmoA, and pmoC polypeptides and multiple metal binding sites Methylococcus capsulatus

Synonyms

Synonyms Comment Organism
particulate methane monooxygenase
-
Methylosinus trichosporium
particulate methane monooxygenase
-
Methylocystis sp.
particulate methane monooxygenase
-
Methylococcus capsulatus
pMMO
-
Methylosinus trichosporium
pMMO
-
Methylocystis sp.
pMMO
-
Methylococcus capsulatus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
-
Methylococcus capsulatus
40 45
-
Methylosinus trichosporium
40 45
-
Methylocystis sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2 7.3
-
Methylosinus trichosporium
7.2 7.3
-
Methylocystis sp.

Cofactor

Cofactor Comment Organism Structure
NAD+ methane activation by particulate methane monooxygenase is NAD-dependent Methylosinus trichosporium
NAD+ methane activation by particulate methane monooxygenase is NAD-dependent. Docking simulations of NAD+ on the enzyme clearly show preferential binding of the cofactor in the vicinity of the Cu metal centers confirming its functional relationship with particulate methane monooxygenase Methylocystis sp.
quinol
-
Methylococcus capsulatus

General Information

General Information Comment Organism
additional information analysis of structural and functional differences of sMMO, EC 1.14.13.25, and pMMO, substrate/product/cofactor-active site interactions, docking analysis of interactions between cofactors and corresponding enzymes. Molecular simulations and modeling, overview Methylococcus capsulatus
physiological function MMO is an enzyme complex that can oxidize the C-H bonds in methane and other alkanes. As one of the oxidoreductase group,MMOplays a critical role in the first step of methanotrophs metabolism where methane is transformed into methanol Methylococcus capsulatus