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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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1.2.1.46 formaldehyde dehydrogenaseSpecify your search results
Word Map
- 1.2.1.46
- methanol
-
gsh-dependent
- s-hydroxymethylglutathione
- boidinii
- hyphomicrobium
- s-formylglutathione
-
methanol-utilizing
-
1.2.1.1
-
methanol-grown
- industry
-
formaldehyde-induced
- analysis
- degradation
- biotechnology
The taxonomic range for the selected organisms is: Pseudomonas putida
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dehydrogenase, formaldehyde
-
-
-
-
FALDH
-
-
-
-
NAD-dependent formaldehyde dehydrogenase
-
-
-
-
NAD-linked formaldehyde dehydrogenase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
-
-, -
SYSTEMATIC NAME
IUBMB Comments
formaldehyde:NAD+ oxidoreductase
-
CAS REGISTRY NUMBER
COMMENTARY
9028-84-6
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
formaldehyde + NAD+ + H2O
formate + NADH
removal of toxic formaldehyde
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH
-
-
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH
-
enzyme of creatinine metabolism
-
-
?
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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
formaldehyde + NAD+ + H2O
formate + NADH
removal of toxic formaldehyde
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH
-
enzyme of creatinine metabolism
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
tightly but not covalently bound to protein, one molecule bound per subunit
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zinc
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,2'-bipyridine
-
reversible inactivation, formation of an enzyme-Zn-bipyridine complex
SDS
-
1 mM, over 50% loss of activity for the free enzyme, about 10% loss of activity for the immobilized enzymes
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
Km for NAD+ with various aldehydes and alcohols
-
0.438
formaldehyde
-
enzyme immobilized on phenyl-functionalized MPS-4, pH 7.0, 22°
10.6
formaldehyde
-
enzyme immobilized on methyl-functionalized MPS-4, pH 7.0, 22°
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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°
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.023
formaldehyde
-
enzyme immobilized on methyl-functionalized MPS-4, pH 7.0, 22°
0.404
formaldehyde
-
enzyme immobilized on phenyl-functionalized MPS-4, pH 7.0, 22°
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
150000
42000
-
4 * 42000, recombinant protein, expressed in Escherichia coli, SDS-PAGE, calculation from gene sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
-
4 * 42000, recombinant protein, expressed in Escherichia coli, SDS-PAGE, calculation from gene sequence
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
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
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Methanol
-
5%, high loss of activity for the free enzyme, while the immobilzed enzymes are stable
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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
-
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
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
-
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
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
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
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
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
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