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acetaldehyde + NAD+ + H2O
acetate + NADH + H+
aryl alcohol + NAD+ + H2O
? + NADH
-
-
-
-
-
benzyl alcohol + NAD+ + H2O
? + NADH
-
-
-
-
-
formaldehyde + H2O + NAD+
formate + NADH + H+
formaldehyde + NAD+ + H2O
formate + NADH
formaldehyde + NAD+ + H2O
formate + NADH + 2 H+
formaldehyde + NAD+ + H2O
formate + NADH + H+
glyoxal + NAD+ + H2O
glyoxylate + NADH
isobutanol + NAD+ + H2O
? + NADH
-
-
-
-
-
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
S-hydroxymethylglutathione + NAD+ + H2O
S-formylglutathione + NADH + H+
-
-
-
-
?
S-nitrosoglutathione + NADH + H2O
?
-
-
-
-
?
additional information
?
-
acetaldehyde + NAD+ + H2O

acetate + NADH + H+
-
-
-
-
-
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
-
-
-
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
-
-
-
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
-
-
-
formaldehyde + H2O + NAD+

formate + NADH + H+
-
-
-
-
?
formaldehyde + H2O + NAD+
formate + NADH + H+
-
-
-
-
?
formaldehyde + NAD+ + H2O

formate + NADH
-
-
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH
-
-
-
-
?
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
-
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
-
-
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH
-
-
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH
-
-
-
-
-
formaldehyde + NAD+ + H2O
formate + NADH
-
-
-
-
ir
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
-
-
-
-
ir
formaldehyde + NAD+ + H2O
formate + NADH
-
enzyme of creatinine metabolism
-
-
-
formaldehyde + NAD+ + H2O
formate + NADH
-
-
-
-
-
formaldehyde + NAD+ + H2O
formate + NADH
-
-
-
-
-
formaldehyde + NAD+ + H2O
formate + NADH
-
-
-
-
-
formaldehyde + NAD+ + H2O

formate + NADH + 2 H+
-
-
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH + 2 H+
-
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH + 2 H+
-
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH + 2 H+
-
-
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH + 2 H+
-
-
-
-
?
formaldehyde + NAD+ + H2O

formate + NADH + H+
-
-
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH + H+
-
-
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH + H+
-
key enzyme of formaldehyde metabolism in microorganisms
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH + H+
-
-
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH + H+
-
-
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH + H+
-
-
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH + H+
-
-
-
-
?
glyoxal + NAD+ + H2O

glyoxylate + NADH
-
-
-
-
-
glyoxal + NAD+ + H2O
glyoxylate + NADH
-
-
-
-
-
propionaldehyde + NAD+ + H2O

propionate + NADH
-
-
-
-
-
propionaldehyde + NAD+ + H2O
propionate + NADH
-
-
-
-
-
pyruvaldehyde + NAD+ + H2O

pyruvate + NADH
-
-
-
-
-
pyruvaldehyde + NAD+ + H2O
pyruvate + NADH
-
-
-
-
-
additional information

?
-
-
no substrates are propionaldehyde, n-butyraldehyde, isobutyraldehyde, valeraldehyde, acetaldehyde, benzaldehyde
-
-
-
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
-
-
-
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
?
-
-
-
-
-
-
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biotechnology
-
development of novel formaldehyde-selective amperometric biosensors based on immobilized NAD+- and glutathione dependent formaldehyde dehydrogenase with high selectivity to formaldehyde and a low cross-sensitivity to other substances, the laboratory prototype of the sensor is applied for FA testing in some real samples of pharmaceutical (formidron), disinfectant (descoton forte) and industrial product (formalin)
analysis

-
presence of enzyme can be used as a selectable marker in DNA-mediated transformations
analysis
-
presence of enzyme can be used as a selectable marker in DNA-mediated transformations
-
degradation

-
physiological significance of dlFalDH in the formaldehyde metabolism in Hyphomicrobium zavarzinii ZV 580 cultured on C1 compounds
degradation
-
physiological significance of dlFalDH in the formaldehyde metabolism in Hyphomicrobium zavarzinii ZV 580 cultured on C1 compounds
-
industry

-
construction of a formaldehyde-selective biosensor using NAD+- and glutathione-dependent recombinant formaldehyde dehydrogenase as a bio-recognition element immobilised on the surface of Si/SiO2/Si3N4 structure
industry
-
high thermostability makes FdDH potentially useful for bioanalytic purposes, namely, for formaldehyde assay in food products, wastewater, and pharmaceuticals, and for biotransformation of formaldehyde to formic acid
industry
-
development of a bi-enzyme biosensor for formaldehyde using diaphorase from Bacillus stearothermophilus, NAD+- and glutathione-dependent FDH as bio-recognition elements. Both enzymes can be immobilized on the top of a graphite electrode together with two osmium-redox polymers. Characteristics of the optimized formaldehyde biosensor are sensitivity, detection limit, and linear dynamic range
industry
-
amperometric enzyme-based sensor-system for the direct detection of formaldehyde in air, based on a native bacterial NAD+- and glutathione-independent formaldehyde dehydrogenase as biorecognition element. With the elimination of NAD+ it is much more promising to obtain a sensor device with higher long-term stability
industry
-
amperometric enzyme-based sensor-system for the direct detection of formaldehyde in air, based on a native bacterial NAD+- and glutathione-independent formaldehyde dehydrogenase as biorecognition element. With the elimination of NAD+ it is much more promising to obtain a sensor device with higher long-term stability
-
industry
-
high thermostability makes FdDH potentially useful for bioanalytic purposes, namely, for formaldehyde assay in food products, wastewater, and pharmaceuticals, and for biotransformation of formaldehyde to formic acid
-
industry
-
construction of a formaldehyde-selective biosensor using NAD+- and glutathione-dependent recombinant formaldehyde dehydrogenase as a bio-recognition element immobilised on the surface of Si/SiO2/Si3N4 structure
-
industry
-
construction of a formaldehyde-selective biosensor using NAD+- and glutathione-dependent recombinant formaldehyde dehydrogenase as a bio-recognition element immobilised on the surface of Si/SiO2/Si3N4 structure
-
industry
-
development of a bi-enzyme biosensor for formaldehyde using diaphorase from Bacillus stearothermophilus, NAD+- and glutathione-dependent FDH as bio-recognition elements. Both enzymes can be immobilized on the top of a graphite electrode together with two osmium-redox polymers. Characteristics of the optimized formaldehyde biosensor are sensitivity, detection limit, and linear dynamic range
-
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Attwood, M.M.
Formaldehyde dehydrogenases from methylotrophs
Methods Enzymol.
188
314-330
1990
Arthrobacter sp., Methylophilus methylotrophus
-
brenda
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
Tate, S.; Dalton, H.
A low-molecular-mass protein from Methylococcus capsulatus (Bath) is responsible for the regulation of formaldehyde dehydrogenase activity in vitro
Microbiology
145
159-167
1999
Methylococcus capsulatus, Methylococcus capsulatus Bath
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
Sunga, A.J.; Cregg, J.M.
The Pichia pastoris formaldehyde dehydrogenase gene (FLD1) as a marker for selection of multicopy expression strains of P. pastoris
Gene
330
39-47
2004
Komagataella pastoris, Komagataella pastoris NRRL Y-11430
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
Sanghani, P.C.; Davis, W.I.; Zhai, L.; Robinson, H.
Structure-function relationships in human glutathione-dependent formaldehyde dehydrogenase. Role of Glu-67 and Arg-368 in the catalytic mechanism
Biochemistry
45
4819-4830
2006
Homo sapiens
brenda
Ben Ali, M.; Gonchar, M.; Gayda, G.; Paryzhak, S.; Maaref, M.A.; Jaffrezic-Renault, N.; Korpan, Y.
Formaldehyde-sensitive sensor based on recombinant formaldehyde dehydrogenase using capacitance versus voltage measurements
Biosens. Bioelectron.
22
2790-2795
2007
Ogataea angusta, Ogataea angusta Tf 11-6
brenda
Demkiv, O.M.; Paryzhak, S.Y.; Gayda, G.Z.; Sibirny, V.A.; Gonchar, M.V.
Formaldehyde dehydrogenase from the recombinant yeast Hansenula polymorpha: isolation and bioanalytic application
FEMS Yeast Res.
7
1153-1159
2007
Ogataea angusta
brenda
Nikitina, O.; Shleev, S.; Gayda, G.; Demkiv, O.; Gonchar, M.; Gorton, L.; Csoeregi, E.; Nistor, M.
Bi-enzyme biosensor based on NAD+- and glutathione-dependent recombinant formaldehyde dehydrogenase and diaphorase for formaldehyde assay
Sens. Actuators B Chem.
B125
1-9
2007
Ogataea angusta, Ogataea angusta Tf 11-6
-
brenda
Achmann, S.; Hermann, M.; Hilbrig, F.; Jerome, V.; Haemmerle, M.; Freitag, R.; Moos, R.
Direct detection of formaldehyde in air by a novel NAD+- and glutathione-independent formaldehyde dehydrogenase-based biosensor
Talanta
75
786-791
2008
Hyphomicrobium zavarzinii, Hyphomicrobium zavarzinii ZV 580
brenda
Jerome, V.; Hermann, M.; Hilbrig, F.; Freitag, R.
Development of a fed-batch process for the production of a dye-linked formaldehyde dehydrogenase in Hyphomicrobium zavarzinii ZV 580
Appl. Microbiol. Biotechnol.
77
779-788
2007
Hyphomicrobium zavarzinii, Hyphomicrobium zavarzinii ZV 580
brenda
Demkiv, O.; Smutok, O.; Paryzhak, S.; Gayda, G.; Sultanov, Y.; Guschin, D.; Shkil, H.; Schuhmann, W.; Gonchar, M.
Reagentless amperometric formaldehyde-selective biosensors based on the recombinant yeast formaldehyde dehydrogenase
Talanta
76
837-846
2008
Ogataea angusta
brenda
Marzuki, N.; Bakar, F.; Salleh, A.; Heng, L.; Yusof, N.; Siddiquee, S.
Electrochemical biosensor immobilization of formaldehyde dehydrogenase with Nafion for determination of formaldehyde from Indian mackerel (Rastrelliger kanagurta) fish
Curr. Anal. Chem.
8
534-542
2012
Rastrelliger kanagurta
-
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Demkiv, O.; Paryzhak, S.; Ishchuk, E.; Gayda, G.; Gonchar, M.
Activities of the enzymes of formaldehyde catabolism in recombinant strains of Hansenula polymorpha
Microbiology
80
307-313
2011
Ogataea angusta
-
brenda
Liao, Y.; Chen, S.; Wang, D.; Zhang, W.; Wang, S.; Ding, J.; Wang, Y.; Cai, L.; Ran, X.; Wang, X.; Zhu, H.
Structure of formaldehyde dehydrogenase from Pseudomonas aeruginosa the binary complex with the cofactor NAD+
Acta Crystallogr. Sect. F
69
967-972
2013
Pseudomonas aeruginosa, Pseudomonas aeruginosa (Q9HTE3), Pseudomonas aeruginosa LESB58 (Q9HTE3)
brenda
Nakamura, H.; Kato, K.; Masuda, Y.; Kato, K.
Activity of formaldehyde dehydrogenase on titanium dioxide films with different crystallinities
Appl. Surf. Sci.
329
262-268
2015
Pseudomonas sp.
-
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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
Zhang, W.; Chen, S.; Liao, Y.; Wang, D.; Ding, J.; Wang, Y.; Ran, X.; Lu, D.; Zhu, H.
Expression, purification, and characterization of formaldehyde dehydrogenase from Pseudomonas aeruginosa
Protein Expr. Purif.
92
208-213
2013
Pseudomonas aeruginosa
brenda