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Literature summary extracted from

  • Zhang, J.; Zheng, H.; Groce, S.L.; Lipscomb, J.D.
    Basis for specificity in methane monooxygenase and related non-heme iron-containing biological oxidation catalysts (2006), J. Mol. Catal. A, 251, 54-65.
No PubMed abstract available

Application

EC Number Application Comment Organism
1.14.13.25 synthesis the enzyme is a base or scaffold for design of small molecule catalysts for use in large scale methanol synthesis Methylophilaceae

Protein Variants

EC Number Protein Variants Comment Organism
1.14.13.25 additional information mutagenesis of MMOB potentially broadening the substrate range of the enzyme Methylophilaceae

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.13.25 Fe2+ the enzyme contains a Fe2S2 cluster, a bis-my-hydroxo-bridged dinuclear iron cluster, that binds to the enzyme reductase domain MMOR Methylophilaceae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.13.25 methane + NADH + O2 Methylophilaceae methane is oxidized to methanol with 100% efficiency with no over-oxidation, methanol is then further oxidized by other enzymes in two electron steps to CO2 methanol + NAD+ + H2O
-
 ?
1.14.13.25 additional information Methylophilaceae access and regulation in the methane monooxygenase system via interaction of reductase protein MMOB and hydroxylase protein MMOH, regulatory effects of MMOB, overview ?
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 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.13.25 Methylophilaceae
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.14.13.25 methane + NAD(P)H + H+ + O2 = methanol + NAD(P)+ + H2O reaction mechanism and regulation, catalytic cycle of sMMO, the enzyme complex causes quantum tunneling to dominate in CĀ–H bond cleavage reaction for methane, selectively increasing the rate for this substrate, mechanism of C-H bond cleavage, overview Methylophilaceae
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.14.13.25 culture condition:methane-grown cell
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 Methylophilaceae
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.13.25 methane + NADH + O2 methane is oxidized to methanol with 100% efficiency with no over-oxidation, methanol is then further oxidized by other enzymes in two electron steps to CO2 Methylophilaceae methanol + NAD+ + H2O
-
 ?
1.14.13.25 methane + NADH + O2 for the MMOH alone the rate of turnover is increased 150fold and rate constant for O2 binding is increased 1000fold in the binary complex compared to the complete enzyme Methylophilaceae methanol + NAD+ + H2O
-
 ?
1.14.13.25 additional information access and regulation in the methane monooxygenase system via interaction of reductase protein MMOB and hydroxylase protein MMOH, regulatory effects of MMOB, overview Methylophilaceae ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.14.13.25 More three-dimensional structure, the enzyme consists as three protein component system, the regulatory protein MMOB, containing Fe2S2 cluster and a FAD cofactor, binds to the active site-containing hydroxylase protein creating a pore sized for methane into the active site, the third component is termed B, the complex appears to cause quantum tunneling to dominate in CĀ–H bond cleavage reaction for methane, selectively increasing the rate for this substrate, overview Methylophilaceae

Synonyms

EC Number Synonyms Comment Organism
1.14.13.25 sMMO
-
 Methylophilaceae
1.14.13.25 soluble methane monooxygenase
-
 Methylophilaceae

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.13.25 FAD binds to the enzyme reductase protein MMOR Methylophilaceae
1.14.13.25 NADH binds to the enzyme hydroxylase protein MMOH Methylophilaceae