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Literature summary extracted from

  • Pham, M.D.; Lin, Y.P.; Van Vuong, Q.; Nagababu, P.; Chang, B.T.; Ng, K.Y.; Chen, C.H.; Han, C.C.; Chen, C.H.; Li, M.S.; Yu, S.S.; Chan, S.I.
    Inactivation of the particulate methane monooxygenase (pMMO) in Methylococcus capsulatus (Bath) by acetylene (2015), Biochim. Biophys. Acta, 1854, 1842-1852 .
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.14.18.3 Acetylene a suicide inhibitor of pMMO, inactivation of the particulate methane monooxygenase (pMMO): the enzyme oxidizes acetylene to the ketene (C2H2O) intermediate, which then forms an acetylation adduct with the transmembrane PmoC subunit. LC-MS/MS analysis of the peptides derived fromin-gel proteolytic digestion of the protein subunit identifies K196 of PmoC as the site of acetylation. No evidence is obtained for chemical modification of the PmoA or PmoB subunit. The inactivation of pMMO by a single adduct in the transmembrane PmoC domain is intriguing given the complexity of the structural fold of this large membrane-protein complex as well as the complicated roles played by the various metal cofactors in the enzyme catalysis. Computational studies suggest that the entry of hydrophobic substrates to, and migration of products from, the catalytic site of pMMO are controlled tightly within the transmembrane domain Methylococcus capsulatus
1.14.18.3 additional information inhibitor docking study, computational simulation of the structure and mechanism, modeling, overview Methylococcus capsulatus
1.14.18.3 propyne
-
 Methylococcus capsulatus
1.14.18.3 trifluoropropyne
-
 Methylococcus capsulatus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.18.3 Cu2+ the enzyme complex contains multiple copper ions, 12-15 copper ions per protein monomer Methylococcus capsulatus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.14.18.3 98000
-
 about Methylococcus capsulatus

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
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.18.3 additional information membrane-bound pMMO can efficiently oxidize straight-chain hydrocarbons from C1 to C5 with high regiospecificity and unusual stereoselectivity. Acetylene is a suicide substrate/inhibitor, the enzyme oxidizes acetylene to the ketene (C2H2O) intermediate, which then forms an acetylation adduct with the transmembrane PmoC subunit, there is a thermodynamic driving force for a ketene formed at the catalytic site to find its way to the water-exposed domain of subunit PmoB for acetylation, residue K196 of subunit PmoC that is acetylated, overview Methylococcus capsulatus ?
-
 ?
1.14.18.3 additional information membrane-bound pMMO can efficiently oxidize straight-chain hydrocarbons from C1 to C5 with high regiospecificity and unusual stereoselectivity. Acetylene is a suicide substrate/inhibitor, the enzyme oxidizes acetylene to the ketene (C2H2O) intermediate, which then forms an acetylation adduct with the transmembrane PmoC subunit, there is a thermodynamic driving force for a ketene formed at the catalytic site to find its way to the water-exposed domain of subunit PmoB for acetylation, residue K196 of subunit PmoC that is acetylated, overview Methylococcus capsulatus Bath ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.14.18.3 More enzyme pMMO is a large protein complex with three subunits, PmoA, PmoB and PmoC, and many copper ions, three-dimensional structure of pMMO, overview Methylococcus capsulatus
1.14.18.3 trimer 1 * 26690, subunit pmoB + 1 * 29000, subunit pmoA, + 1 * 42000, subunit pmoB, SDS-PAGE Methylococcus capsulatus

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.14.18.3 additional information
-
 additional information inhibition kinetic study Methylococcus capsulatus

General Information

EC Number General Information Comment Organism
1.14.18.3 malfunction inactivation of the particulate methane monooxygenase (pMMO): the enzyme oxidizes acetylene to the ketene (C2H2O) intermediate, which then forms an acetylation adduct with the transmembrane PmoC subunit. LC-MS/MS analysis of the peptides derived from in-gel proteolytic digestion of the protein subunit identifies K196 of PmoC as the site of acetylation. No evidence is obtained for chemical modification of the PmoA or PmoB subunit. The inactivation of pMMO by a single adduct in the transmembrane PmoC domain is intriguing given the complexity of the structural fold of this large membrane-protein complex as well as the complicated roles played by the various metal cofactors in the enzyme catalysis. Computational studies suggest that the entry of hydrophobic substrates to, and migration of products from, the catalytic site of pMMO are controlled tightly within the transmembrane domain Methylococcus capsulatus