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Information on EC 1.2.1.46 - formaldehyde dehydrogenase and Organism(s) Pseudomonas putida and UniProt Accession P46154

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This record set is specific for:
Pseudomonas putida
UNIPROT: P46154 not found.
Word Map
The taxonomic range for the selected organisms is: Pseudomonas putida
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
formaldehyde dehydrogenase, dye-linked formaldehyde dehydrogenase, nad-dependent formaldehyde dehydrogenase, nad-linked formaldehyde dehydrogenase, glutathione-independent formaldehyde dehydrogenase, nad+-dependent formaldehyde dehydrogenase, dlfaldh, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dehydrogenase, formaldehyde
-
-
-
0
FALDH
-
-
-
0
NAD-dependent formaldehyde dehydrogenase
-
-
-
0
NAD-linked formaldehyde dehydrogenase
-
-
-
0
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
0
oxidation
-
-
-
0
reduction
-
-
-
0
SYSTEMATIC NAME
IUBMB Comments
formaldehyde:NAD+ oxidoreductase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9028-84-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
formaldehyde + NAD+ + H2O
formate + NADH
show the reaction diagram
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
show the reaction diagram
-
-
-
-
?
aryl alcohol + NAD+ + H2O
? + NADH
show the reaction diagram
-
-
-
-
?
benzyl alcohol + NAD+ + H2O
? + NADH
show the reaction diagram
-
-
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH
show the reaction diagram
formaldehyde + NAD+ + H2O
formate + NADH + 2 H+
show the reaction diagram
-
-
-
-
?
glyoxal + NAD+ + H2O
glyoxylate + NADH
show the reaction diagram
-
-
-
-
?
isobutanol + NAD+ + H2O
? + NADH
show the reaction diagram
-
-
-
-
?
isobutyraldehyde + NAD+ + H2O
isobutyrate + NADH + H+
show the reaction diagram
-
-
-
-
r
isopentanol + 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
-
-
-
-
?
pyruvaldehyde + NAD+ + H2O
pyruvate + NADH
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
formaldehyde + NAD+ + H2O
formate + NADH
show the reaction diagram
removal of toxic formaldehyde
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH
show the reaction diagram
-
enzyme of creatinine metabolism
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH + 2 H+
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
tightly but not covalently bound to protein, one molecule bound per subunit
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
two ions bound per subunit
additional information
-
independent of Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
-
-
acetaldehyde
-
substrate n-butanol
diisopropylphosphofluoridate
-
partial
ethanol
-
substrate n-butanol
Mn2+
-
partial
N-Acetylimidazole
-
partial
n-butanol
n-Butyraldehyde
-
substrate formaldehyde or n-butanol
n-Hexanol
n-Propanol
-
substrate n-butanol
n-Valeraldehyde
-
substrate n-butanol
o-phenanthroline
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
Zn2+
-
partial
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.9
acetaldehyde
-
-
100
aryl alcohol
-
-
5.5
benzyl alcohol
-
-
0.067 - 10.6
formaldehyde
30
isobutanol
-
-
6.2
Isobutyraldehyde
-
-
4.2
Isopentanol
-
-
10.6
n-butanol
-
-
4
n-Hexanol
-
-
6.5
n-Pentanol
-
-
50
n-Propanol
-
-
0.056 - 0.5
NAD+
47
propionaldehyde
-
-
additional information
additional information
-
Km for NAD+ with various aldehydes and alcohols
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.136 - 0.48
formaldehyde
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.023 - 0.518
formaldehyde
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24.1
-
recombinant protein, expressed in Escherichia coli
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10.8
-
n-butanol
7
-
assay at
7.8
-
formaldehyde
8.9
-
formaldehyde
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.6 - 8.3
-
at pH 6.6 and 8.3 about 50% of activity maximum
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
assay at room temperature
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
FADH_PSEPU
399
0
42082
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
42000
4 * 42000
150000
250000
-
gel filtration
42000
-
4 * 42000, recombinant protein, expressed in Escherichia coli, SDS-PAGE, calculation from gene sequence
75000
-
2 * 75000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
4 * 42000
dimer
-
2 * 75000, SDS-PAGE
tetramer
-
4 * 42000, recombinant protein, expressed in Escherichia coli, SDS-PAGE, calculation from gene sequence
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
-
15 h, 20% loss of activity
288248
8.5 - 10
-
stable
288248
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
-
30 min, pH 7.5, stable
55
-
pH 7.5, 30 min, 50% loss of activity
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Methanol
-
5%, high loss of activity for the free enzyme, while the immobilzed enzymes are stable
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant protein, expressed in Escherichia coli
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
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