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Literature summary for 1.2.7.B2 extracted from

  • Sevcenco, A.; Bevers, L.; Pinkse, M.; Krijger, G.; Wolterbeek, H.; Verhaert, P.; Hagen, W.; Hagedoorn, P.
    Molybdenum incorporation in tungsten aldehyde oxidoreductase enzymes from Pyrococcus furiosus (2010), J. Bacteriol., 192, 4143-4152 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.2.7.B2

Metals/Ions

Metals/Ions Comment Organism Structure
Mo5+ molybdenum can be incorporated, Mo(V) signal is observed in electron paramagnetic resonance. Aldehyde oxidation activity correlates only with the residual tungsten content. This suggests that the Mo-containing enzymes are most likely inactive. An intracellular selection mechanism for tungstate and molybdate processing has to be present, since tungsten is found to be preferentially incorporated even under conditions with comparable intracellular concentrations of tungstate and molybdate Pyrococcus furiosus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
69072
-
 tandem mass spectrometry Pyrococcus furiosus

Organism

Organism UniProt Comment Textmining
Pyrococcus furiosus Q8U1K3
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
formaldehyde + H2O + oxidized methyl viologen
-
 Pyrococcus furiosus formate + reduced methyl viologen + H+
-
 ?

Subunits

Subunits Comment Organism
? x * 69072, tandem mass spectrometry Pyrococcus furiosus

Synonyms

Synonyms Comment Organism
FOR
-
 Pyrococcus furiosus
formaldehyde:ferredoxin oxidoreductase
-
 Pyrococcus furiosus
PF1203
-
 Pyrococcus furiosus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60
-
 assay at Pyrococcus furiosus

Cofactor

Cofactor Comment Organism Structure
tungsto-bispterin cofactor
-
 Pyrococcus furiosus