Information on EC 1.2.98.1 - formaldehyde dismutase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
1.2.98.1
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RECOMMENDED NAME
GeneOntology No.
formaldehyde dismutase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 formaldehyde + H2O = formate + methanol
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cannizzaro reaction
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cross-dismutation
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dismutation
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oxidation
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redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Chloroalkane and chloroalkene degradation
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Methane metabolism
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Microbial metabolism in diverse environments
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SYSTEMATIC NAME
IUBMB Comments
formaldehyde:formaldehyde oxidoreductase
The enzyme contains a tightly but noncovalently bound NADP(H) cofactor, as well as Zn2+ and Mg2+. Enzyme-bound NADPH formed by oxidation of formaldehyde to formate is oxidized back to NADP+ by reaction with a second formaldehyde, yielding methanol. The enzyme from the bacterium Mycobacterium sp. DSM 3803 also catalyses the reactions of EC 1.1.99.36, alcohol dehydrogenase (nicotinoprotein) and EC 1.1.99.37, methanol dehydrogenase (nicotinoprotein) [3]. Formaldehyde and acetaldehyde can act as donors; formaldehyde, acetaldehyde and propanal can act as acceptors [1,2].
CAS REGISTRY NUMBER
COMMENTARY hide
85204-94-0
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
liver alcoholdehydrogenase class II, class I isoenzymes beta1,beta1 and gamma2,gamma2
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Manually annotated by BRENDA team
bifunctional enzyme. In addition to dismutase activity, enzyme oxidizes ethanol and formaldehyde as well as methanol
UniProt
Manually annotated by BRENDA team
bifunctional enzyme. In addition to dismutase activity, enzyme oxidizes ethanol and formaldehyde as well as methanol
UniProt
Manually annotated by BRENDA team
no activity in Rattus norvegicus
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Manually annotated by BRENDA team
strain 9816
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Manually annotated by BRENDA team
strain A2, constitutive enzyme
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-butanol + p-nitroso-N,N-dimethylaniline
n-butanal + reduced p-nitroso-N,N-dimethylaniline
show the reaction diagram
1-pentanol + p-nitroso-N,N-dimethylaniline
n-pentanal + reduced p-nitroso-N,N-dimethylaniline
show the reaction diagram
1-propanol + p-nitroso-N,N-dimethylaniline
n-propanal + reduced p-nitroso-N,N-dimethylaniline
show the reaction diagram
2 formaldehyde
formate + methanol
show the reaction diagram
2-oxo-propanal + H2O + propanal
pyruvate + propanol
show the reaction diagram
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?
acetaldehyde + H2O
acetate + ethanol
show the reaction diagram
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?
cyclohexanol + p-nitroso-N,N-dimethylaniline
cyclohexanal + reduced p-nitroso-N,N-dimethylaniline
show the reaction diagram
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50% of activity with ethanol
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?
ethanol + p-nitroso-N,N-dimethylaniline
ethanal + reduced p-nitroso-N,N-dimethylaniline
show the reaction diagram
formaldehyde + H2O
formate + methanol
show the reaction diagram
formaldehyde + H2O + acrolein
formate + allyl alcohol
show the reaction diagram
formaldehyde + H2O + butyraldehyde
formate + butanol
show the reaction diagram
formaldehyde + H2O + crotonaldehyde
formate + crotonyl alcohol
show the reaction diagram
formaldehyde + H2O + ethanal
formate + ethanol
show the reaction diagram
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?
formaldehyde + H2O + isobutyraldehyde
formate + isobutanol
show the reaction diagram
formaldehyde + H2O + propionaldehyde
formate + propanol
show the reaction diagram
formate + methanol
formaldehyde
show the reaction diagram
n-butanol + H2O + isobutyraldehyde
butyraldehyde + isobutanol
show the reaction diagram
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in general: RCH2OH + R'CHO = RCHO + R'CH2OH, aliphatic alcohols with longer carbon chains than C-5, secondary alcohols, diols and aromatic alcohols and the corresponding aldehydes are no substrates
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r
n-hexanol + p-nitroso-N,N-dimethylaniline
n-hexanal + reduced p-nitroso-N,N-dimethylaniline
show the reaction diagram
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14% of activity with ethanol
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?
pyruvaldehyde + H2O
pyruvate + methylglycol
show the reaction diagram
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?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
formaldehyde + H2O
formate + methanol
show the reaction diagram
formate + methanol
formaldehyde
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
hydroxylamine
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iodoacetate
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p-chloromercuribenzoate
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pyrazole
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Semicarbazide
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thiosulfate
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additional information
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not inhibited by AMP, ADP, ATP and N-methylnicotinamide chloride
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0014
1-butanol
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+ p-nitroso-N,N-dimethylaniline
0.0032
1-propanol
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+ p-nitroso-N,N-dimethylaniline
1.2 - 13
Butanal
0.02
ethanol
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+ p-nitroso-N,N-dimethylaniline
0.35
formaldehyde
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0.04
methanol
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+ p-nitroso-N,N-dimethylaniline
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1 - 21.7
Butanal
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0002
Hg2+
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noncompetitive inhibition
0.52
Semicarbazide
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noncompetitive inhibition
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
177
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recombinant enzyme coexpressed with GroESL
215.6
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recombinant enzyme
6000
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enzyme activity in resting cells grown on mineral salts medium with 0.04% formaldehyde
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 9.5
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pH 5: about 10% of activity maximum, pH 9.5: about 50% of activity maximum, no activity at pH 10
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
44000
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4 * 44000, SDS-PAGE
55000
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4 * 55000, SDS-PAGE
180000
220000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Pseudomonas putida F61
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recombinant enzyme
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 7
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390491
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
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10 min, no loss of activity
30
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10 min, 21% loss of activity
35
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10 min, 50% loss of activity
45
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10 min, 82% loss of activity
50
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10 min, 100% loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme is stabilized by immobilization in an urethane prepolymer
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
class I beta1,beta1 and class I gamma2,gamma2 enzyme exressed in Escherichia coli
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coexpression in Escherichia coli with GroESL
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expression in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
transcription is upregulated in cells growing on methanol
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
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