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Literature summary 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)

EC Number Cloned (Comment) Organism
1.14.13.7
-
Cutaneotrichosporon cutaneum

Protein Variants

EC Number Protein Variants Comment Organism
1.14.13.7 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

EC Number Organism UniProt Comment Textmining
1.14.13.7 Cutaneotrichosporon cutaneum
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.13.7
-
Cutaneotrichosporon cutaneum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.13.7 3-methylphenol + O2 + NADPH i.e. m-cresol Cutaneotrichosporon cutaneum ?
-
?
1.14.13.7 phenol + NADPH + O2
-
Cutaneotrichosporon cutaneum catechol + NADP+ + H2O
-
?
1.14.13.7 resorcinol + NADPH + O2
-
Cutaneotrichosporon cutaneum ?
-
?