Information on EC 1.2.1.46 - formaldehyde dehydrogenase

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

EC NUMBER
COMMENTARY
1.2.1.46
-
RECOMMENDED NAME
GeneOntology No.
formaldehyde dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
formaldehyde + NAD+ + H2O = formate + NADH + 2 H+
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
oxidation
-
-
redox reaction
-
-
-
-
redox reaction
-
-
reduction
-
-
-
-
reduction
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Chloroalkane and chloroalkene degradation
-
-
formaldehyde oxidation IV (thiol-independent)
-
-
Metabolic pathways
-
-
Methane metabolism
-
-
methanol oxidation to carbon dioxide
-
-
Microbial metabolism in diverse environments
-
-
SYSTEMATIC NAME
IUBMB Comments
formaldehyde:NAD+ oxidoreductase
-
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dehydrogenase, formaldehyde
-
-
-
-
DL-FDH
Hyphomicrobium zavarzinii ZV 580
-
-
-
dlFalDH
Hyphomicrobium zavarzinii ZV 580
-
-
-
dye-linked formaldehyde dehydrogenase
-
-
dye-linked formaldehyde dehydrogenase
Hyphomicrobium zavarzinii ZV 580
-
;
-
FALDH
-
-
-
-
FDH
Methylococcus capsulatus Bath
-
-
-
FDH
Ogataea angusta Tf 11-6
-
;
-
FDH
Ogataea angusta Tf-11-6
-
-
-
formaldehyde dehydrogenase
-
-
formaldehyde dehydrogenase
-
-
NAD+- and glutathione-dependent formaldehyde dehydrogenase
-
-
NAD+- and glutathione-dependent formaldehyde dehydrogenase
Ogataea angusta Tf 11-6
-
;
-
NAD+- and glutathione-dependent formaldehyde dehydrogenase
Ogataea angusta Tf-11-6
-
-
-
NAD+- and glutathione-independent formaldehyde dehydrogenase
-
-
NAD+- and glutathione-independent formaldehyde dehydrogenase
Hyphomicrobium zavarzinii ZV 580
-
-
-
NAD+- and glutathione_dependent formaldehyde dehydrogenase
-
-
NAD+-dependent formaldehyde dehydrogenase
-
-
NAD-dependent formaldehyde dehydrogenase
-
-
-
-
NAD-linked formaldehyde dehydrogenase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9028-84-6
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
P1 NCIB 11625
-
-
Manually annotated by BRENDA team
Hyphomicrobium zavarzinii ZV 580
strain ZV 580
-
-
Manually annotated by BRENDA team
strain NRRL Y-11430, methylotrophic yeast
-
-
Manually annotated by BRENDA team
Komagataella pastoris NRRL Y-11430
strain NRRL Y-11430, methylotrophic yeast
-
-
Manually annotated by BRENDA team
Methylococcus capsulatus Bath
Bath
-
-
Manually annotated by BRENDA team
stable recombinant strain Tf 11-6
-
-
Manually annotated by BRENDA team
strain Tf 11-6
-
-
Manually annotated by BRENDA team
Ogataea angusta Tf 11-6
strain Tf 11-6
-
-
Manually annotated by BRENDA team
Pseudomonas putida C-83
C-83
-
-
Manually annotated by BRENDA team
Pseudomonas putida C1
C1
-
-
Manually annotated by BRENDA team
Pseudomonas putida MS
MS
-
-
Manually annotated by BRENDA team
Indian mackerel
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
show the reaction diagram
-
-
-
-
-
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
show the reaction diagram
-
-
-
-
-
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
show the reaction diagram
Pseudomonas putida C-83
-
-
-
-
-
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
show the reaction diagram
Methylococcus capsulatus Bath
-
-
-
-
-
aryl alcohol + NAD+ + H2O
? + NADH
show the reaction diagram
-
-
-
-
-
benzyl alcohol + NAD+ + H2O
? + NADH
show the reaction diagram
-
-
-
-
-
formaldehyde + H2O + NAD+
formate + NADH + H+
show the reaction diagram
-
-
-
-
?
formaldehyde + H2O + NAD+
formate + NADH + H+
show the reaction diagram
Hyphomicrobium zavarzinii ZV 580
-
-
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH
show the reaction diagram
-
-
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH
show the reaction diagram
-
-
-
-
-
formaldehyde + NAD+ + H2O
formate + NADH
show the reaction diagram
-
-
-
-
ir
formaldehyde + NAD+ + H2O
formate + NADH
show the reaction diagram
-
-
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH
show the reaction diagram
-
-
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH
show the reaction diagram
P46154
-
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH
show the reaction diagram
-
enzyme of creatinine metabolism
-
-
-
formaldehyde + NAD+ + H2O
formate + NADH
show the reaction diagram
P46154
removal of toxic formaldehyde
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH
show the reaction diagram
-
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
show the reaction diagram
Pseudomonas putida C-83
-
-
-
-
ir
formaldehyde + NAD+ + H2O
formate + NADH
show the reaction diagram
Pseudomonas putida C-83
-
enzyme of creatinine metabolism
-
-
-
formaldehyde + NAD+ + H2O
formate + NADH
show the reaction diagram
Pseudomonas putida C-83
-
-
-
-
-
formaldehyde + NAD+ + H2O
formate + NADH
show the reaction diagram
Methylococcus capsulatus Bath
-
-
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH
show the reaction diagram
Pseudomonas putida MS
-
-
-
-
-
formaldehyde + NAD+ + H2O
formate + NADH
show the reaction diagram
Pseudomonas putida C1
-
-
-
-
-
formaldehyde + NAD+ + H2O
formate + NADH
show the reaction diagram
Komagataella pastoris NRRL Y-11430
-
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 + H+
show the reaction diagram
-
-
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH + H+
show the reaction diagram
-
-
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH + H+
show the reaction diagram
-
-
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH + H+
show the reaction diagram
-
key enzyme of formaldehyde metabolism in microorganisms
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH + H+
show the reaction diagram
Ogataea angusta Tf 11-6
-
-
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH + H+
show the reaction diagram
Ogataea angusta Tf-11-6
-
-
-
-
?
glyoxal + NAD+ + H2O
glyoxylate + NADH
show the reaction diagram
Pseudomonas putida, Pseudomonas putida C-83
-
-
-
-
-
isobutanol + NAD+ + H2O
? + NADH
show the reaction diagram
-
-
-
-
-
n-butanol + NAD+ + H2O
? + NADH
show the reaction diagram
-
-
-
-
-
n-hexanol + NAD+ + H2O
? + NADH
show the reaction diagram
-
-
-
-
-
n-pentanol + NAD+ + H2O
? + NADH
show the reaction diagram
-
-
-
-
-
n-propanol + NAD+ + H2O
? + NADH
show the reaction diagram
-
-
-
-
-
propionaldehyde + NAD+ + H2O
propionate + NADH
show the reaction diagram
-
-
-
-
-
propionaldehyde + NAD+ + H2O
propionate + NADH
show the reaction diagram
Pseudomonas putida C-83
-
-
-
-
-
pyruvaldehyde + NAD+ + H2O
pyruvate + NADH
show the reaction diagram
Pseudomonas putida, Pseudomonas putida C-83
-
-
-
-
-
S-hydroxymethylglutathione + NAD+ + H2O
S-formylglutathione + NADH + H+
show the reaction diagram
-
-
-
-
?
S-nitrosoglutathione + NADH + H2O
?
show the reaction diagram
-
-
-
-
?
isopentanol + NAD+ + H2O
? + NADH
show the reaction diagram
-
-
-
-
-
additional information
?
-
-
-
-
-
-
additional information
?
-
-
specificity, best substrate: formaldehyde, reduced activity with increasing length of alkyl groups of aldehydes, no activity with n-butyraldehyde or n-valeraldehyde, no activity for methanol or ethanol
-
-
-
additional information
?
-
-
no substrates are propionaldehyde, n-butyraldehyde, isobutyraldehyde, valeraldehyde, acetaldehyde, benzaldehyde
-
-
-
additional information
?
-
Pseudomonas putida C-83
-
specificity, best substrate: formaldehyde, reduced activity with increasing length of alkyl groups of aldehydes, no activity with n-butyraldehyde or n-valeraldehyde, no activity for methanol or ethanol
-
-
-
additional information
?
-
Pseudomonas putida C-83
-
-
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
formaldehyde + NAD+ + H2O
formate + NADH
show the reaction diagram
-
enzyme of creatinine metabolism
-
-
-
formaldehyde + NAD+ + H2O
formate + NADH
show the reaction diagram
P46154
removal of toxic formaldehyde
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH
show the reaction diagram
-
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 + H+
show the reaction diagram
-
-
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH + H+
show the reaction diagram
-
-
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH + H+
show the reaction diagram
-
-
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH + H+
show the reaction diagram
-
key enzyme of formaldehyde metabolism in microorganisms
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH
show the reaction diagram
Pseudomonas putida C-83
-
enzyme of creatinine metabolism
-
-
-
formaldehyde + NAD+ + H2O
formate + NADH
show the reaction diagram
Komagataella pastoris NRRL Y-11430
-
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
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
glutathione
-
dependent on
NAD+
-
coenzyme binding domain: Gly-Xaa-Gly-Xaa-Xaa-Gly
NAD+
-
tightly but not covalently bound to protein
NAD+
P46154
tightly but not covalently bound to protein, one molecule bound per subunit
NAD+
-
dependent on
NADH
-
-
additional information
-
no activity with NADP+
-
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
-
pyrroloquinoline quinone may be the bound cofactor
-
additional information
-
processes formaldehyde in a highly selective manner and without need for NAD(P). The dlFalDH cofactor is an unidentified quinone
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
-
active-site zinc-liganding amino acids: Cys-47 and His-68; structural zinc-liganding amino acids: Cys-97, Cys-100, Cys-103, Cys-111
Zn2+
-
two ions bound per subunit
Zn2+
P46154
two ions bound per subunit
Zn2+
-
-
Ca2+
-
is required for the stabilization of the tetrameric structure of dlFalDH and for its optimal functionality
additional information
-
independent of Mg2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,2'-bipyridine
-
-
2,2'-bipyridine
-
reversible inactivation, formation of an enzyme-Zn-bipyridine complex
4-Methylpyrazole
-
native and recombinant protein
5,5'-dithiobis(2-nitrobenzoate)
-
partial
8-hydroxyquinoline
-
-
8-hydroxyquinoline
-
-
acetaldehyde
-
substrate n-butanol
diisopropylphosphofluoridate
-
partial
dodecanoic acid
-
-
EDTA
-
partial
ethanol
-
substrate n-butanol
N-Acetylimidazole
-
partial
n-butanol
-
; substrate formaldehyde
n-Butyraldehyde
-
substrate formaldehyde or n-butanol
n-Hexanol
-
; substrate formaldehyde
n-Propanol
-
substrate n-butanol
n-Valeraldehyde
-
substrate n-butanol
o-phenanthroline
-
-
o-phenanthroline
-
partial
o-phenanthroline
-
-
p-chloromercuribenzoate
-
-
phenylmethanesulfonyl fluoride
-
-
propionaldehyde
-
substrate formaldehyde
Sodium tetrathionate
-
partial
Zn2+
-
partial
Mn2+
-
partial
additional information
-
biosensor output signal decreases substantially with the increase of borate buffer concentration. Sensitivity of the biosensor in 2.5 mM Tris-HCl buffer is decreased dramatically
-
additional information
-
down-regulation of the dlFalDH production in correlation with the absence of methylamine hydrochloride consumption
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
methanol
-
cultivation on 1% methanol provides the highest level of enzyme synthesis for recipient and overproducing strains
methanol
-
stabilizes
additional information
-
best sensitivity of the biosensor is observed in 2.5 mM borate buffer, pH 8.4
-
additional information
-
culture in the fed-batch mode in the bioreactor and active methylamine consumption positively affect dlFalDH productivity
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5.9
acetaldehyde
-
-
100
aryl alcohol
-
-
-
5.5
benzyl alcohol
-
-
0.067
formaldehyde
-
-
0.074
formaldehyde
-
-
0.09
formaldehyde
-
-
0.18
formaldehyde
-
KM value of the used FdDH in solution from the wild strains
0.2
formaldehyde
-
-
119.9
formaldehyde
-
immobilized enzyme in a bioactive layer on the transducer surface, apparent Michaelis-Menten constant derived from the formaldehyde calibration curves is 120 mM with a linear detection range for formaldehyde up to 20 mM
30
isobutanol
-
-
6.2
Isobutyraldehyde
-
-
10.6
n-butanol
-
-
4
n-Hexanol
-
-
6.5
n-Pentanol
-
-
50
n-Propanol
-
-
0.0033
NAD+
-
reduction of NAD+, formaldehyde dehydrogenase
0.0144
NAD+
-
reduction of NAD+, R368L mutant
0.056
NAD+
-
-
0.116
NAD+
-
reduction of NAD+, E67L mutant
0.35
NAD+
-
+ formaldehyde
0.45
NAD+
-
-
0.5
NAD+
-
-
0.002
NADH
-
oxidation of NADH, formaldehyde dehydrogenase
0.011
NADH
-
oxidation of NADH, R368L mutant
47
propionaldehyde
-
-
0.0017
S-hydroxymethylglutathione
-
oxidation of S-hydroxymethylglutathione, formaldehyde dehydrogenase
0.038
S-hydroxymethylglutathione
-
oxidation of S-hydroxymethylglutathione, R368L mutant
2.65
S-hydroxymethylglutathione
-
oxidation of S-hydroxymethylglutathione, E67L mutant
0.0048
S-nitrosoglutathione
-
reduction of S-nitrosoglutathione, formaldehyde dehydrogenase
0.16
S-nitrosoglutathione
-
reduction of S-nitrosoglutathione, R368L mutant
4.2
Isopentanol
-
-
additional information
additional information
-
Km for NAD+ with various aldehydes and alcohols
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.03
4-Methylpyrazole
-
native and recombinant protein
6.1
acetaldehyde
-
substrate n-butanol
0.148
dodecanoic acid
-
formaldehyde dehydrogenase
0.161
dodecanoic acid
-
R368L mutant
0.617
dodecanoic acid
-
E67L mutant
90
ethanol
-
substrate n-butanol
5.4
n-butanol
-
substrate formaldehyde
0.27
n-Butyraldehyde
-
substrate formaldehyde
2.6
n-Butyraldehyde
-
substrate n-butanol
2.3
n-Hexanol
-
substrate formaldehyde
70
n-Propanol
-
substrate n-butanol
1.9
n-Valeraldehyde
-
substrate n-butanol
35
propionaldehyde
-
substrate formaldehyde
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5
-
the stable recombinant strain Tf 11-6 in cell-free extract
7
-
FdDH specific activity in cell-free extract of Tf 11-6, cultivated in methanol medium supplemented with 10 mM formaldehyde
12
-
at 20C
17
-
3.8fold purified enzyme at 25C
24.1
-
recombinant protein, expressed in Escherichia coli
27
-
3.8fold purified enzyme at 37C
additional information
-
-
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
-
maximum response of the biosensor
7.8
-
formaldehyde
8
-
Nafion membrane-immobilized enzyme
8.1 - 8.5
-
-
8.4
-
best sensitivity of the biosensor output signal is observed in 2.5 mM borate buffer, pH 8.4
8.9
-
formaldehyde
10.8
-
n-butanol
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.6 - 8.3
-
at pH 6.6 and 8.3 about 50% of activity maximum
7.5 - 8.5
-
-
7.6 - 8.3
-
optimal pH-value for the developed FdDH-based biosensor
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
-
S-nitrosoglutathione
30
-
S-hydroxymethylglutathione
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45 - 50
-
optimal temperature for the developed FdDH-based biosensor
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
43500
-
gel filtration
288245
150000
-
gel filtration
288248
150000
-
recombinant protein, expressed in E. coli, gel filtration
288253
170000
P46154
-
656507
250000
-
gel filtration
288246
250000
-
gel filtration
288252
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
-
2 * 75000, SDS-PAGE
dimer
-
2 * 40000, SDS-PAGE
dimer
Pseudomonas putida C-83
-
2 * 75000, SDS-PAGE
-
homodimer
-
-
monomer
-
1 * 48000, SDS-PAGE
tetramer
-
4 * 63000, ESI-MS
tetramer
-
4 * 42000, recombinant protein, expressed in Escherichia coli, SDS-PAGE, calculation from gene sequence
tetramer
P46154
4 * 42000
tetramer
-
4 * 45000-55000, SDS-PAGE
tetramer
Hyphomicrobium zavarzinii ZV 580
-
4 * 45000-55000, SDS-PAGE
-
tetramer
Methylococcus capsulatus Bath
-
4 * 63000, ESI-MS
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
formaldehyde dehydrogenase-adenosine 5'-diphosphate ribose and E67L-NADH binary complexes are determined
-
hanging drop vapor diffusion method
P46154
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 8.5
-
-
686818
8
-
15 h, 20% loss of activity
288248
8.5 - 10
-
stable
288248
additional information
-
FDH is not stable at a pH below 6.5, but shows higher stability in an alkaline pH domain
690067
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 65
-
at 65C, the enzyme retains about 60% of its highest activity (assay time of ca. 5 min), which is equal to the level of FdDH activity at 30C
686818
40
-
30 min, pH 7.5, stable
288248
45
-
stable for 6 min
288245
55
-
pH 7.5, 30 min, 50% loss of activity
288248
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, stable for at least 1 month
-
-10C, ammonium sulfate solution (80% saturation), 2 mM DTT
-
14 h and 1 mM during 22 h, the storage stability of the developed biosensors is found to be longer than 18 days at 4C
-
the developed sensors demonstrate a good operational stability at comparatively low formaldehyde concentrations of 2 mM during
-
4C, Nafion membrane-immobilized enzyme, more than 6 months, remains stable
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DE52, Q-sepharose and Sephacryl S-100HR chromatographic steps
-
partially purified
-
by ion-exchange chromatography
-
by two-step anion-exchange chromatography and precipitation by 80% (NH4)2SO4, precipitate, 3.8fold purified
-
FdDH ss isolated from the cell-free extract by a two-step ion exchange chromatography
-
; recombinant protein, expressed in Escherichia coli
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
for expression in Escherichia coli BL21 cells
-
construction of a recombinant yeast clone originated from the recipient strain of thermotolerant methylotrophic yeast Hansenula polymorpha which is a NAD+- and glutathione dependent FdDH over-producer
-
FLD1 gene with its own promoter is recloned into LEU2-containing integrative plasmid pYT1 devoid of the autonomously replicating sequence to be used for multicopy integration of the gene into chromosome of the recipient strain NCYC 495
-
FLD1 gene with the own promoter inserted into the integrative plasmid pYT1 containing LEU2 gene of Saccharomyces cerevisiae (as a selective marker). The constructed vector is used for multi-copy integration of the target gene into genome by transformation of the recipient cells of the strain NCYC 495
-
expressed in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E67L
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mutant shows, that Glu67 is critical for capturing the substrates for catalysis
R368L
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mutant shows, that the predominant role of Arg-368 is in the binding of the coenzyme
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
degradation
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physiological significance of dlFalDH in the formaldehyde metabolism in Hyphomicrobium zavarzinii ZV 580 cultured on C1 compounds
industry
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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
degradation
Hyphomicrobium zavarzinii ZV 580
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physiological significance of dlFalDH in the formaldehyde metabolism in Hyphomicrobium zavarzinii ZV 580 cultured on C1 compounds
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industry
Hyphomicrobium zavarzinii ZV 580
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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
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analysis
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presence of enzyme can be used as a selectable marker in DNA-mediated transformations
analysis
Komagataella pastoris NRRL Y-11430
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presence of enzyme can be used as a selectable marker in DNA-mediated transformations
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biotechnology
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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)
industry
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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
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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
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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
Ogataea angusta Tf 11-6
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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, 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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industry
Ogataea angusta Tf-11-6
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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
-