We're sorry, but BRENDA doesn't work properly without JavaScript. Please make sure you have JavaScript enabled in your browser settings.
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
The taxonomic range for the selected organisms is: Pseudomonas putida 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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
dehydrogenase, formaldehyde
-
-
-
-
NAD-dependent formaldehyde dehydrogenase
-
-
-
-
NAD-linked formaldehyde dehydrogenase
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
formaldehyde:NAD+ oxidoreductase
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
formaldehyde + NAD+ + H2O
formate + NADH
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
-
-
?
aryl alcohol + NAD+ + H2O
? + NADH
-
-
-
-
?
benzyl alcohol + NAD+ + H2O
? + NADH
-
-
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH
formaldehyde + NAD+ + H2O
formate + NADH + 2 H+
-
-
-
-
?
glyoxal + NAD+ + H2O
glyoxylate + NADH
-
-
-
-
?
isobutanol + NAD+ + H2O
? + NADH
-
-
-
-
?
isobutyraldehyde + NAD+ + H2O
isobutyrate + NADH + H+
-
-
-
-
r
isopentanol + NAD+ + H2O
? + NADH
-
-
-
-
?
n-butanol + NAD+ + H2O
? + NADH
-
-
-
-
?
n-hexanol + NAD+ + H2O
? + NADH
-
-
-
-
?
n-pentanol + NAD+ + H2O
? + NADH
-
-
-
-
?
n-propanol + NAD+ + H2O
? + NADH
-
-
-
-
?
propionaldehyde + NAD+ + H2O
propionate + NADH
-
-
-
-
?
pyruvaldehyde + NAD+ + H2O
pyruvate + NADH
-
-
-
-
?
additional information
?
-
formaldehyde + NAD+ + H2O
formate + NADH
-
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH
removal of toxic formaldehyde
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH
-
-
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH
-
-
-
-
ir
formaldehyde + NAD+ + H2O
formate + NADH
-
enzyme of creatinine metabolism
-
-
?
additional information
?
-
-
-
-
-
?
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
formaldehyde + NAD+ + H2O
formate + NADH
removal of toxic formaldehyde
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH
-
enzyme of creatinine metabolism
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH + 2 H+
-
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NAD+
tightly but not covalently bound to protein, one molecule bound per subunit
NAD+
-
-
NAD+
-
coenzyme binding domain: Gly-Xaa-Gly-Xaa-Xaa-Gly
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Zn2+
two ions bound per subunit
additional information
-
independent of Mg2+
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
Zinc
-
active-site zinc-liganding amino acids: Cys-47 and His-68
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2,2'-bipyridine
-
reversible inactivation, formation of an enzyme-Zn-bipyridine complex
4-Methylpyrazole
-
native and recombinant protein
5,5'-dithiobis(2-nitrobenzoate)
-
partial
acetaldehyde
-
substrate n-butanol
diisopropylphosphofluoridate
-
partial
ethanol
-
substrate n-butanol
N-Acetylimidazole
-
partial
n-Butyraldehyde
-
substrate formaldehyde or n-butanol
n-Propanol
-
substrate n-butanol
n-Valeraldehyde
-
substrate n-butanol
p-chloromercuribenzoate
-
-
phenylmethanesulfonyl fluoride
-
-
propionaldehyde
-
substrate formaldehyde
SDS
-
1 mM, over 50% loss of activity for the free enzyme, about 10% loss of activity for the immobilized enzymes
Sodium tetrathionate
-
partial
EDTA
-
-
n-butanol
-
-
n-butanol
-
substrate formaldehyde
n-Hexanol
-
-
n-Hexanol
-
substrate formaldehyde
o-phenanthroline
-
-
o-phenanthroline
-
partial
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.067 - 10.6
formaldehyde
additional information
additional information
-
Km for NAD+ with various aldehydes and alcohols
-
0.067
formaldehyde
-
-
0.438
formaldehyde
-
enzyme immobilized on phenyl-functionalized MPS-4, pH 7.0, 22°
0.926
formaldehyde
-
pH 7.0, 22°C, free enzyme
2.84
formaldehyde
-
enzyme immobilized on MPS-4, pH 7.0, 22°
10.6
formaldehyde
-
enzyme immobilized on methyl-functionalized MPS-4, pH 7.0, 22°
0.056
NAD+
-
-
0.35
NAD+
-
+ formaldehyde
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.136 - 0.48
formaldehyde
0.136
formaldehyde
-
enzyme immobilized on MPS-4, pH 7.0, 22°
0.177
formaldehyde
-
enzyme immobilized on phenyl-functionalized MPS-4, pH 7.0, 22°
0.247
formaldehyde
-
enzyme immobilized on methyl-functionalized MPS-4, pH 7.0, 22°
0.48
formaldehyde
-
pH 7.0, 22°C, free enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.023 - 0.518
formaldehyde
0.023
formaldehyde
-
enzyme immobilized on methyl-functionalized MPS-4, pH 7.0, 22°
0.047
formaldehyde
-
enzyme immobilized on MPS-4, pH 7.0, 22°
0.404
formaldehyde
-
enzyme immobilized on phenyl-functionalized MPS-4, pH 7.0, 22°
0.518
formaldehyde
-
pH 7.0, 22°C, free enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.03
4-Methylpyrazole
-
native and recombinant protein
6.1
acetaldehyde
-
substrate n-butanol
90
ethanol
-
substrate n-butanol
5.4
n-butanol
-
substrate formaldehyde
0.27 - 2.6
n-Butyraldehyde
2.3
n-Hexanol
-
substrate formaldehyde
70
n-Propanol
-
substrate n-butanol
1.9
n-Valeraldehyde
-
substrate n-butanol
35
propionaldehyde
-
substrate formaldehyde
0.27
n-Butyraldehyde
-
substrate formaldehyde
2.6
n-Butyraldehyde
-
substrate n-butanol
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
24.1
-
recombinant protein, expressed in Escherichia coli
additional information
-
-
additional information
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
6.6 - 8.3
-
at pH 6.6 and 8.3 about 50% of activity maximum
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
22
-
assay at room temperature
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
SwissProt
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
FADH_PSEPU
399
0
42082
Swiss-Prot
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
42000
-
4 * 42000, recombinant protein, expressed in Escherichia coli, SDS-PAGE, calculation from gene sequence
75000
-
2 * 75000, SDS-PAGE
150000
-
gel filtration
150000
-
recombinant protein, expressed in E. coli, gel filtration
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
dimer
-
2 * 75000, SDS-PAGE
tetramer
-
4 * 42000, recombinant protein, expressed in Escherichia coli, SDS-PAGE, calculation from gene sequence
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
hanging drop vapor diffusion method
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
additional information
-
immobilization of the purified enzyme on seven types of mesoporous silica (MPS), whose pores are from 2.4 to 31.2 nm sized, avaluatio of the enzyme activity in oxidation of formaldehyde, method overview. Enhancement of catalytic activity is obtained by immobilizing onto MPS, whose pore (mesopore) size is similar to the molecular size of enzyme FDH. FDH immobilized on phenyl-functionalized MPS-4 (MPS-4-Ph) has higher activity than FDH immobilized on non-functionalized one. Immobilized FDH on MPS-4-Ph is active for low formaldehyde concentration form 6.0 M and more sensitive than conventional formaldehyde detectors. The high-order structure of the FDH does not alter upon binding to the non-functionalized MPS surface. But FDH immobilized on functionalized-MPS is changed by hydrophobic interaction or covalent binding
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
8
-
15 h, 20% loss of activity
288248
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
40
-
30 min, pH 7.5, stable
55
-
pH 7.5, 30 min, 50% loss of activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Methanol
-
5%, high loss of activity for the free enzyme, while the immobilzed enzymes are stable
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
recombinant protein, expressed in Escherichia coli
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
expressed in Escherichia coli
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Hohnloser, W.; Osswald, B.; Lingens, F.
Enzymological aspects of caffeine demethylation and formaldehyde oxidation by Pseudomonas putida C1
Hoppe-Seyler's Z. Physiol. Chem.
361
1763-1766
1980
Pseudomonas putida, Pseudomonas putida C1 / ATCC 17453
brenda
Ogushi, S.; Ando, M.; Tsuru, D.
Substrate specificity of formaldehyde dehydrogenase from Pseudomonas putida
Agric. Biol. Chem.
48
597-601
1984
Pseudomonas putida, Pseudomonas putida C-83
-
brenda
Ando, M.; Yoshimoto, T.; Ogushi, S.; Rikitake, K.; Shibata, S.; Tsuru, D.
Formaldehyde dehydrogenase from Pseudomonas putida. Purification and some properties
J. Biochem.
85
1165-1172
1979
Pseudomonas putida, Pseudomonas putida C-83
brenda
Ogushi, S.; Ando, M.; Tsuru, D.
Formaldehyde dehydrogenase from Pseudomonas putida: the role of a cysteinyl residue in the enzyme activity
Agric. Biol. Chem.
50
2503-2507
1986
Pseudomonas putida, Pseudomonas putida C-83
-
brenda
Ogushi, S.; Ando, M.; Tsuru, D.
Formaldehyde dehydrogenase from Pseudomonas putida: a zinc metalloenzyme
J. Biochem.
96
1587-1591
1984
Pseudomonas putida, Pseudomonas putida C-83
brenda
Kung, H.F.; Wagner, C.
Oxidation of C-1 compounds by Pseudomonas sp. MS
Biochem. J.
116
357-365
1970
Pseudomonas putida, Pseudomonas putida MS
brenda
Ito, K.; Takahashi, M.; Yoshimoto, T.; Tsuru, D.
Cloning and high-level expression of the glutathione-independent formaldehyde dehydrogenase gene from Pseudomonas putida
J. Bacteriol.
176
2483-2491
1994
Pseudomonas putida
brenda
Tanaka, N.; Kusakabe, Y.; Ito, K.; Yoshimoto, T.; Nakamura, K.T.
Crystal structure of formaldehyde dehydrogenase from Pseudomonas putida: the structural origin of the tightly bound cofactor in nicotinoprotein dehydrogenases
J. Mol. Biol.
324
519-533
2002
Pseudomonas putida (P46154), Pseudomonas putida
brenda
Ashraf, R.; Rashid, N.; Basheer, S.; Aziz, I.; Akhtar, M.
Glutathione-dependent formaldehyde dehydrogenase homolog from Bacillus subtilis strain R5 is a propanol-preferring alcohol dehydrogenase
Biochemistry (Moscow)
82
13-23
2017
Pseudomonas putida
-
brenda