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Literature summary for 1.97.1.1 extracted from

  • Oltmann, L.F.; Claassen, V.P.; Kastelein, P.; Reijnders, W.N.M.; Stouthamer, A.H.
    Influence of tungstate on the formation and activities of four reductases in Proteus mirabilis: identification of two new molybdo-enzymes: chlorate reductase and tetrathionate reductase (1979), FEBS Lett., 106, 43-46.
    View publication on PubMed

Metals/Ions

Metals/Ions Comment Organism Structure
Mo molybdo-enzyme Proteus mirabilis

Organism

Organism UniProt Comment Textmining
Proteus mirabilis
-
enzyme formed during anaerobic growth without nitrate
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Proteus mirabilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
chlorate + reduced electron acceptor the only known substrate is chlorate Proteus mirabilis chlorite + H2O + oxidized electron acceptor
-
?

Cofactor

Cofactor Comment Organism Structure
molybdenum cofactor molybdo-enzyme Proteus mirabilis