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EC Tree
The expected taxonomic range for this enzyme is: Methylococcus capsulatus
Synonyms
DL-FalDH, formaldehyde-cytochrome b559/569 oxidoreductase,
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formaldehyde-cytochrome b559/569 oxidoreductase
DL-FalDH
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formaldehyde-cytochrome b559/569 oxidoreductase
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formaldehyde-cytochrome b559/569 oxidoreductase
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formaldehyde + 2 ferricytochrome b559/569 + H2O = formate + 2 ferrocytochrome b559/569 + 2 H+
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formaldehyde:ferricytochrome b559/569 oxidoreductase
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formaldehyde + dichloroindophenol
formate + reduced dichloroindophenol
formaldehyde + ferricytochrome b559/569 + H2O
formate + ferrocytochrome b559/569 + 2 H+
formaldehyde + ferricytochrome b559/569 complex
formate + ferrocytochrome b559/569 complex
additional information
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formaldehyde + dichloroindophenol
formate + reduced dichloroindophenol
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formaldehyde is the only substrate that supports enzyme-mediated reduction of dichloroindophenol
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formaldehyde + dichloroindophenol
formate + reduced dichloroindophenol
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formaldehyde is the only substrate that supports enzyme-mediated reduction of dichloroindophenol
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formaldehyde + ferricytochrome b559/569 + H2O
formate + ferrocytochrome b559/569 + 2 H+
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r
formaldehyde + ferricytochrome b559/569 + H2O
formate + ferrocytochrome b559/569 + 2 H+
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r
formaldehyde + ferricytochrome b559/569 complex
formate + ferrocytochrome b559/569 complex
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formaldehyde + ferricytochrome b559/569 complex
formate + ferrocytochrome b559/569 complex
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the enzyme is involved in the pathways of methane oxidation. Cytochrome b559/569 complex is the physiological electron acceptor. The enzyme is the major formaldehyde-oxidizing enzyme in cells cultured in high (above 1 mol of Cu per mg of cell protein) copper medium
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formaldehyde + ferricytochrome b559/569 complex
formate + ferrocytochrome b559/569 complex
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formaldehyde + ferricytochrome b559/569 complex
formate + ferrocytochrome b559/569 complex
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the enzyme is involved in the pathways of methane oxidation. Cytochrome b559/569 complex is the physiological electron acceptor. The enzyme is the major formaldehyde-oxidizing enzyme in cells cultured in high (above 1 mol of Cu per mg of cell protein) copper medium
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additional information
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no activity with: methanol, acetaldehyde, glyoxal, or butyraldehyde
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additional information
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no activity with: methanol, acetaldehyde, glyoxal, or butyraldehyde
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formaldehyde + ferricytochrome b559/569 complex
formate + ferrocytochrome b559/569 complex
formaldehyde + ferricytochrome b559/569 complex
formate + ferrocytochrome b559/569 complex
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the enzyme is involved in the pathways of methane oxidation. Cytochrome b559/569 complex is the physiological electron acceptor. The enzyme is the major formaldehyde-oxidizing enzyme in cells cultured in high (above 1 mol of Cu per mg of cell protein) copper medium
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formaldehyde + ferricytochrome b559/569 complex
formate + ferrocytochrome b559/569 complex
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the enzyme is involved in the pathways of methane oxidation. Cytochrome b559/569 complex is the physiological electron acceptor. The enzyme is the major formaldehyde-oxidizing enzyme in cells cultured in high (above 1 mol of Cu per mg of cell protein) copper medium
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pyrroloquinoline quinone
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pyrroloquinoline quinone-to-subunit stochiometry of approximately 1:1, 3.6 mol of pyrroloquinoline quinone per mol of enzyme
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Cu2+
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partial inhibition
Fe2+
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partial inhibition
Zn2+
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partial inhibition
additional information
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the enzyme is insensitive to EDTA, N-ethylmaleimide, cyanide and azide
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0.143
formaldehyde
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20°C, pH 7.4
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290
dichloroindophenol
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20°C, pH 7.4
266
ferricytochrome b559/569
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20°C, pH 7.4
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brenda
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brenda
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brenda
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brenda
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associated
brenda
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associated
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brenda
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49500
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4 * 49500, SDS-PAGE
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homotetramer
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4 * 49500, SDS-PAGE
homotetramer
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4 * 49500, SDS-PAGE
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Zahn, J.A.; Bergmann, D.J.; Boyd, J.M.; Kunz, R.C.; DiSpirito, A.A.
Membrane-associated quinoprotein formaldehyde dehydrogenase from Methylococcus capsulatus bath
J. Bacteriol.
183
6832-6840
2001
Methylococcus capsulatus, Methylococcus capsulatus Bath
brenda
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1.2.2.B1 quinoprotein formaldehyde dehydrogenase (cytochrome b559/569)
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