Any feedback?
Information on EC 1.2.1.46 - formaldehyde dehydrogenase
for references in articles please use BRENDA:EC1.2.1.46Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.2.1.46 formaldehyde dehydrogenaseSpecify your search results
Word Map
- 1.2.1.46
- methanol
-
gsh-dependent
- s-hydroxymethylglutathione
- boidinii
- hyphomicrobium
- s-formylglutathione
-
methanol-utilizing
-
1.2.1.1
-
methanol-grown
- industry
-
formaldehyde-induced
- analysis
- degradation
- biotechnology
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
formaldehyde dehydrogenase, dye-linked formaldehyde dehydrogenase, nad-dependent formaldehyde dehydrogenase, glutathione-independent formaldehyde dehydrogenase, nad-linked formaldehyde dehydrogenase, nad+-dependent formaldehyde dehydrogenase, dlfaldh, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ADH3
dehydrogenase, formaldehyde
-
-
-
-
DL-FDH
dlFalDH
dye-linked formaldehyde dehydrogenase
FADH
FALDH
FdDH
FDH
fdhA
Fldh1
formaldehyde dehydrogenase
glutathione-dependent formaldehyde dehydrogenase/alcohol dehydrogenase
glutathione-independent formaldehyde dehydrogenase
GSH-FDH/ADH
NAD+- and glutathione-dependent formaldehyde dehydrogenase
NAD+- and glutathione-independent formaldehyde dehydrogenase
NAD-dependent formaldehyde dehydrogenase
-
-
-
-
NAD-linked formaldehyde dehydrogenase
-
-
-
-
FALDH
-
-
-
-
glutathione-dependent formaldehyde dehydrogenase/alcohol dehydrogenase
-
cf. EC 1.1.1.1
glutathione-dependent formaldehyde dehydrogenase/alcohol dehydrogenase
-
cf. EC 1.1.1.1
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
formaldehyde + NAD+ + H2O = formate + NADH + H+
-
-
-
-
formaldehyde + NAD+ + H2O = formate + NADH + H+
Pseudomonas aeruginosa FDH has a conserved glutathione-independent ping pong mechanism of formaldehyde oxidization
formaldehyde + NAD+ + H2O = formate + NADH + H+
the catalytic reaction proceeds by a Ping Pong mechanism as designated by the Michaelis-Menten model of bi-substrate enzymatic kinetics
-
formaldehyde + NAD+ + H2O = formate + NADH + H+
Pseudomonas aeruginosa FDH has a conserved glutathione-independent ping pong mechanism of formaldehyde oxidization
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
redox reaction
reduction
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
KEGG
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
formaldehyde:NAD+ oxidoreductase
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
9028-84-6
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
formate + reduced methyl viologen + 2 H+
formaldehyde + oxidized methyl viologen + H2O
-
single-electron reduced methyl viologen activates the enzyme activity for formate reduction to formaldehyde
-
-
?
propionaldehyde + NAD+ + H2O
propionate + NADH + H+
-
95% activity compared to propionaldehyde
-
-
?
S-hydroxymethylglutathione + NAD+ + H2O
S-formylglutathione + NADH + H+
-
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
95% activity compared to propionaldehyde
-
-
?
formaldehyde + H2O + NAD+
formate + NADH + H+
-
-
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH
-
required for growth on methanol as carbon source or methylamine as nitrogen source, reaction provides energy as NADH and protects against a toxic excess of formaldehyde
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH
-
required for growth on methanol as carbon source or methylamine as nitrogen source, reaction provides energy as NADH and protects against a toxic excess of formaldehyde
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH
-
-
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH
-
enzyme of creatinine metabolism
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH
removal of toxic formaldehyde
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH
-
enzyme of creatinine metabolism
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH + H+
-
78% activity compared to propionaldehyde
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH + H+
-
-
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH + H+
-
key enzyme of formaldehyde metabolism in microorganisms
-
-
?
additional information
?
-
-
no substrates are propionaldehyde, n-butyraldehyde, isobutyraldehyde, valeraldehyde, acetaldehyde, benzaldehyde
-
-
?
additional information
?
-
-
specificity, best substrate: formaldehyde
-
-
?
additional information
?
-
-
reduced activity with increasing length of alkyl groups of aldehydes
-
-
?
additional information
?
-
-
no activity with n-butyraldehyde or n-valeraldehyde
-
-
?
additional information
?
-
-
specificity, best substrate: formaldehyde
-
-
?
additional information
?
-
-
reduced activity with increasing length of alkyl groups of aldehydes
-
-
?
additional information
?
-
-
no activity with n-butyraldehyde or n-valeraldehyde
-
-
?
additional information
?
-
-
no activity for methanol or ethanol
-
-
?
additional information
?
-
-
by using natural co-enzyme NADH, no formaldehyde production due to formate reduction with the enzyme is observed
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL 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
formaldehyde + NAD+ + H2O
formate + NADH
-
required for growth on methanol as carbon source or methylamine as nitrogen source, reaction provides energy as NADH and protects against a toxic excess of formaldehyde
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH
-
required for growth on methanol as carbon source or methylamine as nitrogen source, reaction provides energy as NADH and protects against a toxic excess of formaldehyde
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH
-
enzyme of creatinine metabolism
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH
removal of toxic formaldehyde
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH
-
enzyme of creatinine metabolism
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH + H+
-
key enzyme of formaldehyde metabolism in microorganisms
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
tightly but not covalently bound to protein, one molecule bound per subunit
NAD+
NAD+-binding mode analysis, with two bound zinc ions per monomer of the tetrameric enzyme
additional information
-
substrate specificity is regulated by modifin, FDH oxidizes formaldehyde exclusively and only in the presence of modifin, whereas a range of aldehydes and alcohols are oxidized in the absence of modifin, modifin cannot be replaced by glutathione
-
additional information
-
processes formaldehyde in a highly selective manner and without need for NAD(P). The dlFalDH cofactor is an unidentified quinone
-
additional information
-
pyrroloquinoline quinone may be the bound cofactor
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Cu2+
-
the protein contains 1.3 mol of Cu2+. The highest activity, 22fold increase, is found in the protein produced in the presence of 0.025 mM Cu2+
Fe2+
-
a 20fold increase in activity is found in the protein produced in the presence of 0.025 mM Fe2+
Zinc
Zn2+
additional information
Ca2+
-
is required for the stabilization of the tetrameric structure of dlFalDH and for its optimal functionality
Ca2+
-
plays an important role in the active centre of DL-FDH and for the sensing purpose
Zinc
-
zinc metalloenzyme, 2 zinc atoms per subunit, one participates in catalytic activity, the other is involved in maintaining the native conformation of the enzyme
Zinc
-
structural zinc-liganding amino acids: Cys-97, Cys-100, Cys-103, Cys-111
Zn2+
-
the protein contains 1.5 mol of Zn2+. An increase in activity is found in the protein produced in the presence of 0.025 mM Zn2+
additional information
-
the presence or absence of metal ions (0.1 mM) in the reaction mixture does not affect the enzyme activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SDS
-
1 mM, over 50% loss of activity for the free enzyme, about 10% loss of activity for the immobilized enzymes
2,2'-bipyridine
-
reversible inactivation, formation of an enzyme-Zn-bipyridine complex
additional information