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Literature summary for 1.14.18.3 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

Inhibitors Comment Organism Structure
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
additional information inhibitor docking study, computational simulation of the structure and mechanism, modeling, overview Methylococcus capsulatus
propyne
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Methylococcus capsulatus
trifluoropropyne
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Methylococcus capsulatus

Metals/Ions

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

Molecular Weight [Da]

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

Organism

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
-
?
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

Subunits Comment Organism
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
trimer 1 * 26690, subunit pmoB + 1 * 29000, subunit pmoA, + 1 * 42000, subunit pmoB, SDS-PAGE Methylococcus capsulatus

Ki Value [mM]

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

General Information

General Information Comment Organism
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