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Literature summary for 1.14.13.7 extracted from

  • Xu, D.; Enroth, C.; Lindqvist, Y.; Ballou, D.P.; Massey, V.
    Studies of the mechanism of phenol hydroxylase: Effect of mutation of proline 364 to serine (2002), Biochemistry, 41, 13627-13636.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Cutaneotrichosporon cutaneum

Protein Variants

Protein Variants Comment Organism
P364S only 13% of the FAD is utilized to hydroxylate the substrate phenol, when resorcinol is used as substrate, the reaction is not significantly different from the reaction of the wild type enzyme Cutaneotrichosporon cutaneum

Organism

Organism UniProt Comment Textmining
Cutaneotrichosporon cutaneum
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Cutaneotrichosporon cutaneum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-methylphenol + O2 + NADPH i.e. m-cresol Cutaneotrichosporon cutaneum ?
-
?
phenol + NADPH + O2
-
Cutaneotrichosporon cutaneum catechol + NADP+ + H2O
-
?
resorcinol + NADPH + O2
-
Cutaneotrichosporon cutaneum ?
-
?