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Literature summary for 1.14.13.7 extracted from

  • Cadieux, E.; Vrajmasu, V.; Achim, C.; Powlowski, J.; Muenck, E.
    Biochemical, Mossbauer, and EPR studies of the diiron cluster of phenol hydroxylase from Pseudomonas sp. strain CF 600 (2002), Biochemistry, 41, 10680-10691.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
dithiothreitol dithiothreitol acts as H2O2 generator and inhibits the oxygenase component of the enzyme, catalase protects the loss of activity Pseudomonas sp.

Organism

Organism UniProt Comment Textmining
Pseudomonas sp.
-
-
-
Pseudomonas sp. CF 600
-
-
-

Purification (Commentary)

Purification (Comment) Organism
purification of the oxygenase component Pseudomonas sp.

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.78 1.4
-
Pseudomonas sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
phenol + NADPH + O2
-
Pseudomonas sp. catechol + NADP+ + H2O
-
?
phenol + NADPH + O2
-
Pseudomonas sp. CF 600 catechol + NADP+ + H2O
-
?

Subunits

Subunits Comment Organism
dimer SDS-PAGE shows three polypeptides with molecular masses of 13000, 39000 and 60000, gel filtration experiments are consistent with the existence of a dimer Pseudomonas sp.