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Enzyme Nomenclature
Information on EC 1.2.2.B2 - quinoprotein formaldehyde dehydrogenase (cytochrome cL)
for references in articles please use BRENDA:EC1.2.2.B2preliminary BRENDA-supplied EC number
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EC Tree
1.2.2.B2 quinoprotein formaldehyde dehydrogenase (cytochrome cL)Specify your search results
The enzyme appears in viruses and cellular organisms
Reaction Schemes
+
2
+
=
+
2
+
2
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REACTION 
REACTION DIAGRAM
COMMENTARY 
ORGANISM
UNIPROT
LITERATURE
formaldehyde + 2 ferricytochrome cL + H2O = formate + 2 ferrocytochrome cL + 2 H+
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-
-
-
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SYSTEMATIC NAME
IUBMB Comments
formaldehyde:ferricytochrome cL oxidoreductase
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetaldehyde + 2,6-dichlorophenolindophenol
acetate + reduced 2,6-dichlorophenolindophenol
acetaldehyde + oxidized 2,6-dichlorophenolindophenol
acetate + reduced 2,6-dichlorophenolindophenol
formaldehyde + 2,6-dichlorophenolindophenol
formate + reduced 2,6-dichlorophenolindophenol
formaldehyde + oxidized 2,6-dichlorophenolindophenol
formate + reduced 2,6-dichlorophenolindophenol
propionaldehyde + 2,6-dichlorophenolindophenol
propionate + reduced 2,6-dichlorophenolindophenol
propionaldehyde + oxidized 2,6-dichlorophenolindophenol
propionate + reduced 2,6-dichlorophenolindophenol
acetaldehyde + 2,6-dichlorophenolindophenol
acetate + reduced 2,6-dichlorophenolindophenol
-
with phenazine methosulfate
-
-
?
acetaldehyde + 2,6-dichlorophenolindophenol
acetate + reduced 2,6-dichlorophenolindophenol
-
with phenazine methosulfate
-
-
?
acetaldehyde + oxidized 2,6-dichlorophenolindophenol
acetate + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
acetaldehyde + oxidized 2,6-dichlorophenolindophenol
acetate + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
formaldehyde + 2,6-dichlorophenolindophenol
formate + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
formaldehyde + 2,6-dichlorophenolindophenol
formate + reduced 2,6-dichlorophenolindophenol
-
with phenazine methosulfate
-
-
?
formaldehyde + 2,6-dichlorophenolindophenol
formate + reduced 2,6-dichlorophenolindophenol
-
with phenazine methosulfate
-
-
?
formaldehyde + oxidized 2,6-dichlorophenolindophenol
formate + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
formaldehyde + oxidized 2,6-dichlorophenolindophenol
formate + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
formaldehyde + oxidized 2,6-dichlorophenolindophenol
formate + reduced 2,6-dichlorophenolindophenol
-
-
-
?
propionaldehyde + 2,6-dichlorophenolindophenol
propionate + reduced 2,6-dichlorophenolindophenol
-
with phenazine methosulfate
-
-
?
propionaldehyde + 2,6-dichlorophenolindophenol
propionate + reduced 2,6-dichlorophenolindophenol
-
with phenazine methosulfate
-
-
?
propionaldehyde + oxidized 2,6-dichlorophenolindophenol
propionate + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
propionaldehyde + oxidized 2,6-dichlorophenolindophenol
propionate + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
additional information
?
-
-
the enzyme from Methylosinus sp. WI 14 oxidizes only primary alcohols up to octanol and several aldehydes
-
-
?
additional information
?
-
-
the enzyme from Methylosinus sp. WI 14 oxidizes only primary alcohols up to octanol and several aldehydes
-
-
?
additional information
?
-
acetaldehyde is oxidized very slowly
-
-
?
additional information
?
-
-
broad substrate specificity, MDH from Methylosinus sp. strain WI 14 oxidises only primary alcohols up to octanol and several aldehydes
-
-
?
additional information
?
-
-
broad substrate specificity, MDH from Methylosinus sp. strain WI 14 oxidises only primary alcohols up to octanol and several aldehydes
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyrroloquinoline quinone
-
prosthetic group, 1.3 molecules per enzyme molecule
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
no or poor inhibition by Ca2+, Co2+, Li+, Mg2+, Mn2+, and KCN, EDTA, and DTE
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NH4+
-
absolute requirement, NH4+ can be replaced by methylamine but not by di- or triamines
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.12
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
P38539 (large subunit, alpha) and P38540 (small subunit, beta)
UniProt
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
the enzyme is loosely bound to the intracellular membrane
brenda
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
140000
70000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-18°C, purified native enzyme, 0.05 M sodium phosphate buffer, pH 7.5, loss of 10% of activity after 1 month
-
-18°C, 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
-
4°C, purified native enzyme, 0.05 M sodium phosphate buffer, pH 7.5, loss of 30% of activity after 24 h
-
4°C, 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
-
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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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ghosh, R.; Quayle, J.R.
Purification and properties of the methanol dehydrogenase from Methylophilus methylotrophus
Biochem. J.
199
245-250
1981
Methylophilus methylotrophus (P38539 and P38540)
brenda
Ohta, S.; Fujita, T.; Tobari, J.
Methanol dehydrogenase of Methylomonas J: purification, crystallization, and some properties
J. Biochem.
90
205-213
1981
Methylomonas sp. J
brenda
Grosse, S.; Voigt, C.; Wendlandt, K.D.; Kleber, H.P.
Purification and properties of methanol dehydrogenase from Methylosinus sp. WI 14
J. Basic Microbiol.
38
189-196
1998
Methylosinus sp., Methylosinus sp. WI 14
brenda
Grosse, S.; Voigt, C.; Wendlandt, K.D.; Kleber, H.P.
Purification and properties of methanol dehydrogenase from Methylosinus sp. WI 14
J. Basic Microbiol.
8
189-196
1998
Methylocystis sp., Methylocystis sp. WI14
brenda
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Release 2023.1 (January 2023)
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