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Literature summary for 1.2.7.6 extracted from

  • Hagedoorn, P.L.
    Steady-state kinetics of the tungsten containing aldehyde ferredoxin oxidoreductases from the hyperthermophilic archaeon Pyrococcus furiosus (2019), J. Biotechnol., 306, 142-148 .
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
NaCl enzyme shows partial substrate inhibition, inhibition is alleviated completely by a 1M NaCl resulting in increased enzyme activity at high substrate concentrations Pyrococcus furiosus

Inhibitors

Inhibitors Comment Organism Structure
D-glyceraldehyde 3-phosphate partial substrate inhibition, inhibition is alleviated completely by a 1M NaCl resulting in increased enzyme activity at high substrate concentrations Pyrococcus furiosus

Organism

Organism UniProt Comment Textmining
Pyrococcus furiosus Q8U3K2
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glyceraldehyde 3-phosphate + H2O + 2 oxidized benzyl viologen D-glyceraldehyde 3-phosphate is the only substrate oxidized by GAPOR, and the kinetics of the enzyme are unaffected by the presence of L-glyceraldehyde 3-phosphate Pyrococcus furiosus 3-phospho-D-glycerate + 2 H+ + 2 reduced benzyl viologen
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?
additional information substrate glyceraldehyde-3-phosphate degrades at 60°C by non-enzymatic elimination of the phosphate group to methylglyoxal with a half-life of 6.5 min. Methylglyoxal is not a substrate or inhibitor of GAPOR Pyrococcus furiosus ?
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Synonyms

Synonyms Comment Organism
Gor
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Pyrococcus furiosus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9
-
at pH 9, the substrate is a divalent anion Pyrococcus furiosus