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Literature summary extracted from

  • Kim, J.; Fuller, J.H.; Kuusk, V.; Cunane, L.; Chen, Z.; Mathews, F.S.; McIntire, W.S.
    The cytochrome subunit is necessary for covalent FAD attachment to the flavoprotein subunit of p-cresol methylhydroxylase (1995), J. Biol. Chem., 270, 31202-31209.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.17.9.1 additional information
-
additional information
-
Pseudomonas putida

Organism

EC Number Organism UniProt Comment Textmining
1.17.9.1 Pseudomonas putida
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.17.9.1 4-cresol + acceptor + H2O
-
Pseudomonas putida 4-hydroxybenzaldehyde + reduced acceptor
-
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Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.17.9.1 additional information
-
additional information
-
Pseudomonas putida

Cofactor

EC Number Cofactor Comment Organism Structure
1.17.9.1 cytochrome c the cytochrome subunit is necessary for covalent FAD attachment to the flavoprotein subunit Pseudomonas putida
1.17.9.1 FAD FAD is covalently attached to Tyr384 of the alpha subunit. Covalent flavinylation occurs by a self-catalytic mechanism. The cytochrome subunit is necessary for covalent FAD attachment to the flavoprotein subunit Pseudomonas putida