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Information on EC 1.2.1.46 - formaldehyde dehydrogenase and Organism(s) Pseudomonas aeruginosa and UniProt Accession Q9HTE3
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EC Tree
1.2.1.46 formaldehyde dehydrogenaseSpecify your search results
Word Map
- 1.2.1.46
- methanol
-
gsh-dependent
- s-hydroxymethylglutathione
- boidinii
- hyphomicrobium
- s-formylglutathione
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methanol-utilizing
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1.2.1.1
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methanol-grown
- industry
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formaldehyde-induced
- analysis
- degradation
- biotechnology
The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
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+-dependent formaldehyde dehydrogenase, nad-linked formaldehyde dehydrogenase, dlfaldh, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dehydrogenase, formaldehyde
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FALDH
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NAD-dependent formaldehyde dehydrogenase
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NAD-linked formaldehyde dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
formaldehyde + NAD+ + H2O = formate + NADH + 2 H+
Pseudomonas aeruginosa FDH has a conserved glutathione-independent ping pong mechanism of formaldehyde oxidization
formaldehyde + NAD+ + H2O = formate + NADH + 2 H+
the catalytic reaction proceeds by a Ping Pong mechanism as designated by the Michaelis-Menten model of bi-substrate enzymatic kinetics
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
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oxidation
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reduction
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PATHWAY SOURCE
PATHWAYS
KEGG
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SYSTEMATIC NAME
IUBMB Comments
formaldehyde:NAD+ oxidoreductase
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CAS REGISTRY NUMBER
COMMENTARY
9028-84-6
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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
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
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
NAD+-binding mode analysis, with two bound zinc ions per monomer of the tetrameric enzyme
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
the enzyme from Pseudomonas putida is an exception in that it does not depend on glutathione for catalysis
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additional information
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the enzyme from Pseudomonas putida is an exception in that it does not depend on glutathione for catalysis
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additional information
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the enzyme from Pseudomonas aeruginosa does not depend on glutathione for catalysis. The enzyme requires only NAD+ as the electron carrier, and addition of glutathione has no effect on the catalytic activity, indicating glutathione-independent catalysis
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
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bi-substrate kinetics modelling
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
formaldehyde dehydrogenase (FDH) is a member of the zinc-containing medium-chain alcohol dehydrogenase family
physiological function
the enzyme oxidizes toxic formaldehyde to formate using NAD+ as an electron carrier
evolution
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the enzyme is a member of zinc-containing medium-chain alcohol dehydrogenase family
physiological function
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the enzyme oxidizes toxic formaldehyde to less active formate using NAD+ as a cofactor. The enzyme requires only NAD+ as the electron carrier, and addition of glutathione has no effect on the catalytic activity, indicating glutathione-independent catalysis
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
the active form with each monomer (350-400 amino-acid residues) consisting of catalytic and coenzyme binding domains together with two bound zinc ions
homotetramer
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4 * 44000, recombinant His-tagged enzyme, SDS-PAGE, 4 * 43252, recombinant His-tagged enzyme, mass spectrometry
additional information
additional information
three-dimensional structure modelling and analysis
additional information
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three-dimensional structure modelling and analysis
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme, sitting drop vapour diffusion method, mixing of 0.001 ml of 15 mg/ml FDH protein and 4 mg/ml NAD+ in 10 mM Tris-HCl, pH 8.0, and 1 mM DTT, with 0.001 ml of reservoir solution containing 0.1 M Bis-Tris, pH 5.5, and 1.8 M ammonium sulfate, at 18°C, method optimization, X-ray diffraction structure determination and analysis at 2.7 A resolution, molecular replacement method, and modelling
purified recombinant His-tagged enzyme, sitting drop vapor diffusion method, mixing of 0.001 ml of 15 mg/ml protein in 10 mM Tris-HCl. pH 8.0, and 1 mM DTT with 0.001 ml of reservoir solution containing 0.1 M Bis-Tris, pH 5.5, and 1.8 M ammonium sulfate, at 18°C, X-ray diffraction structure determination and analysis at 2.7 A resolution, molecular replacement method, and modelling
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3)/pG-TF2 by nickel affinity chromatography dialysis, anion exchange chromatography, and dialysis against crystallization buffer
recombinant His-tagged enzyme 94.1fold from Escherichia coli strain BL21(DE3)/pG-TF2 by nickel affinity chromatography dialysis, anion exchange chromatography, and gelfiltration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene fdhA, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)/pG-TF2
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)/pG-TF2. 50% of the recombinant proteins are localized in the supernatant fraction of cell-free extract, suggesting that coexpression with chaperones GroES, GroEL, and Tig has significantly improved the solubilization of Pseudomonas aeruginosa FDH in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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 (Q9HTE3), Pseudomonas aeruginosa, Pseudomonas aeruginosa LESB58 (Q9HTE3)
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Release 2023.1 (January 2023)
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