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 ACCESSION NO.
LITERATURE
formaldehyde + NAD+ + H2O = formate + NADH + 2 H+
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
oxidation
-
-
redox reaction
-
-
-
-
redox reaction
-
-
reduction
-
-
-
-
reduction
-
-
PATHWAY
KEGG Link
MetaCyc Link
Chloroalkane and chloroalkene degradation
-
formaldehyde oxidation IV (thiol-independent)
-
Metabolic pathways
-
Methane metabolism
-
Microbial metabolism in diverse environments
-
SYSTEMATIC NAME
IUBMB Comments
formaldehyde:NAD+ oxidoreductase
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
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
SEQUENCE CODE
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 ACCESSION NO.
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 ACCESSION NO.
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 ACCESSION NO.
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
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 ACCESSION NO.
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 ACCESSION NO.
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
-
-
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
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 ACCESSION NO.
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]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
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
0.116
-
NAD+
-
reduction of NAD+, E67L mutant
0.35
-
NAD+
-
+ formaldehyde
0.45
-
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]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
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]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
16.9
-
-
-
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
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.5
-
-
-
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
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
S-nitrosoglutathione
30
-
-
S-hydroxymethylglutathione
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
45
50
-
optimal temperature for the developed FdDH-based biosensor
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
43500
-
-
gel filtration
150000
-
-
gel filtration
150000
-
-
recombinant protein, expressed in E. coli, gel filtration
170000
-
P46154
-
250000
-
-
gel filtration
250000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
LITERATURE
formaldehyde dehydrogenase-adenosine 5'-diphosphate ribose and E67L-NADH binary complexes are determined
-
hanging drop vapor diffusion method
P46154
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
8
-
-
15 h, 20% loss of activity
8.5
10
-
stable
additional information
-
-
FDH is not stable at a pH below 6.5, but shows higher stability in an alkaline pH domain
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
40
-
-
30 min, pH 7.5, stable
45
-
-
stable for 6 min
55
-
-
pH 7.5, 30 min, 50% loss of activity
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
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
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Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
for expression in Escherichia coli BL21 cells
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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
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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
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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
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expressed in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
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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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
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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
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
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