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EC Number
BRENDA No.
Title
Journal
Volume
Pages
Year
Organism
PubMed ID
1.14.18.3
702170
The metal centres of particulate methane mono-oxygenase
Biochem. Soc. Trans.
36
1134-1137
2008
Methylococcus capsulatus Bath
19021511
1.14.18.3
701759
The methane monooxygenase intrinsic activity of kinds of methanotrophs
Appl. Biochem. Biotechnol.
157
431-441
2009
Methylococcus capsulatus
19052919
1.14.18.3
701759
The methane monooxygenase intrinsic activity of kinds of methanotrophs
Appl. Biochem. Biotechnol.
157
431-441
2009
Methylomonas sp.
19052919
1.14.18.3
701759
The methane monooxygenase intrinsic activity of kinds of methanotrophs
Appl. Biochem. Biotechnol.
157
431-441
2009
Methylosinus trichosporium
19052919
1.14.18.3
701759
The methane monooxygenase intrinsic activity of kinds of methanotrophs
Appl. Biochem. Biotechnol.
157
431-441
2009
Methylococcus capsulatus HD6T
19052919
1.14.18.3
438952
The particulate methane monooxygenase from Methylococcus capsulatus (Bath) is a novel copper-containing three-subunit enzyme. Isolation and characterization
J. Biol. Chem.
273
7957-7966
1998
Methylococcus capsulatus
9525893
1.14.18.3
438952
The particulate methane monooxygenase from Methylococcus capsulatus (Bath) is a novel copper-containing three-subunit enzyme. Isolation and characterization
J. Biol. Chem.
273
7957-7966
1998
Methylococcus capsulatus Bath
9525893
1.14.18.3
689789
Two isozymes of particulate methane monooxygenase with different methane oxidation kinetics are found in Methylocystis sp. strain SC2
Proc. Natl. Acad. Sci. USA
105
10203-10208
2008
Methylocystis sp.
18632585
1.14.18.3
689789
Two isozymes of particulate methane monooxygenase with different methane oxidation kinetics are found in Methylocystis sp. strain SC2
Proc. Natl. Acad. Sci. USA
105
10203-10208
2008
Methylocystis sp. Sc2
18632585
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