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<< < Results 11 - 20 of 119 > >>
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EC Number BRENDA No. Title Journal Volume Pages Year Organism PubMed ID
Display the word mapDisplay the reaction diagram Show all sequences 1.14.18.3690034 The binuclear iron site of membrane-bound methane hydroxylase from Methylococcus capsulatus (strain M) Russ. J. Bioorg. Chem. 34 177-185 2008 Methylococcus capsulatus -
Display the word mapDisplay the reaction diagram Show all sequences 1.14.18.3690034 The binuclear iron site of membrane-bound methane hydroxylase from Methylococcus capsulatus (strain M) Russ. J. Bioorg. Chem. 34 177-185 2008 Methylococcus capsulatus M -
Display the word mapDisplay the reaction diagram Show all sequences 1.14.18.3438940 Properties and partial purification of the methane-oxidising enzyme system from Methylosinus trichosporium FEBS Lett. 58 293-299 1975 Methylosinus trichosporium 178534
Display the word mapDisplay the reaction diagram Show all sequences 1.14.18.3713934 Detergent solubilization of membrane-bound methane monooxygenase requires plastoquinol analogs as electron donors Arch. Biochem. Biophys. 321 421-428 1995 Methylococcus capsulatus 7646068
Display the word mapDisplay the reaction diagram Show all sequences 1.14.18.3713934 Detergent solubilization of membrane-bound methane monooxygenase requires plastoquinol analogs as electron donors Arch. Biochem. Biophys. 321 421-428 1995 Methylococcus capsulatus Bath 7646068
Display the word mapDisplay the reaction diagram Show all sequences 1.14.18.3438944 Membrane-associated methane monooxygenase from Methylococcus capsulatus (Bath) J. Bacteriol. 178 1018-1029 1996 Methylococcus capsulatus 8576034
Display the word mapDisplay the reaction diagram Show all sequences 1.14.18.3438944 Membrane-associated methane monooxygenase from Methylococcus capsulatus (Bath) J. Bacteriol. 178 1018-1029 1996 Methylococcus capsulatus Bath 8576034
Display the word mapDisplay the reaction diagram Show all sequences 1.14.18.3438952 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
Display the word mapDisplay the reaction diagram Show all sequences 1.14.18.3438952 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
Display the word mapDisplay the reaction diagram Show all sequences 1.14.18.3438942 Molecular biology and regulation of methane monooxygenase Arch. Microbiol. 173 325-332 2000 Methylococcus capsulatus 10896210
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