Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.14.13.7 extracted from

  • Turek, M.; Vilimkova, L.; Kremlackova, V.; Paca Jr., J.; Halecky, M.; Paca, J.; Stiborova, M.
    Isolation and partial characterization of extracellular NADPH-dependent phenol hydroxylase oxidizing phenol to catechol in Comamonas testosteroni (2011), Neuroendocrinol. Lett., 32, 137-145.
    View publication on PubMed

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol low activity Comamonas testosteroni 5829
-
extracellular 16fold higher activity than in cytosol Comamonas testosteroni
-
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
60000
-
4 * 60000, SDS-PAGE Comamonas testosteroni
240000
-
gel filtration Comamonas testosteroni

Organism

Organism UniProt Comment Textmining
Comamonas testosteroni
-
Pb50
-

Purification (Commentary)

Purification (Comment) Organism
-
Comamonas testosteroni

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
phenol + NADPH + H+ + O2
-
Comamonas testosteroni catechol + NADP+ + H2O
-
?

Subunits

Subunits Comment Organism
tetramer 4 * 60000, SDS-PAGE Comamonas testosteroni

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.6
-
-
Comamonas testosteroni

Cofactor

Cofactor Comment Organism Structure
NADPH strictly required Comamonas testosteroni