Information on EC 1.2.2.B2 - quinoprotein formaldehyde dehydrogenase (cytochrome cL)

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.2.2.B2
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
quinoprotein formaldehyde dehydrogenase (cytochrome cL)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
formaldehyde + 2 ferricytochrome cL + H2O = formate + 2 ferrocytochrome cL + 2 H+
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
formaldehyde:ferricytochrome cL oxidoreductase
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Methylocystis sp.
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
P38539 (large subunit, alpha) and P38540 (small subunit, beta)
P38539 and P38540
UniProt
Manually annotated by BRENDA team
strain WI 14
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Manually annotated by BRENDA team
strain WI 14
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetaldehyde + 2,6-dichlorophenolindophenol
acetate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
acetaldehyde + oxidized 2,6-dichlorophenolindophenol
acetate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
formaldehyde + 2,6-dichlorophenolindophenol
formate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
formaldehyde + oxidized 2,6-dichlorophenolindophenol
formate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
propionaldehyde + 2,6-dichlorophenolindophenol
propionate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
propionaldehyde + oxidized 2,6-dichlorophenolindophenol
propionate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyrroloquinoline quinone
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Cu2+
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38% inhibition at 0.1 mM
Fe2+
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complete inhibition at 1 mM
phenazine methosulfate
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39% inhibition at 3 mM
additional information
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no or poor inhibition by Ca2+, Co2+, Li+, Mg2+, Mn2+, and KCN, EDTA, and DTE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
methylamine
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can replace NH4+
NH4+
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absolute requirement, NH4+ can be replaced by methylamine but not by di- or triamines
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.01 - 2.3
formaldehyde
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 60
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
P38539 and P38540
the enzyme is loosely bound to the intracellular membrane
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
115000
P38539 and P38540
gel filtration
135000
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gel filtration
140000
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
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30 min, purified enzyme, loss of 25% activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-18C, purified native enzyme, 0.05 M sodium phosphate buffer, pH 7.5, loss of 10% of activity after 1 month
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-18C, solutions of the purified enzyme stored in 0.05 M sodium phosphate buffer, pH 7.5, show about 10% loss of activity during 24 h
Methylocystis sp.
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4C, purified native enzyme, 0.05 M sodium phosphate buffer, pH 7.5, loss of 30% of activity after 24 h
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4C, solutions of the purified enzyme stored in 0.05 M sodium phosphate buffer, pH 7.5, show about 30% loss of activity during 24 h
Methylocystis sp.
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme 9fold to homogeneity by anion exchange chromatography, ammonium sulfate fractionation, and hydrophobic interaction chromatography, followed by ultrafiltration and gel filtration
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