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Literature summary extracted from

  • Cunane, L.M.; Chen, Z.W.; Shamala, N.; Mathews, F.S.; Cronin, C.N.; McIntire, W.S.
    Structures of the flavocytochrome p-cresol methylhydroxylase and its enzyme-substrate complex: Gated substrate entry and proton relays support the proposed catalytic mechanism (2000), J. Mol. Biol., 295, 357-374.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.17.9.1 X-ray crystal structure at 2.5 resolution Pseudomonas putida

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.17.9.1 4-cresol + acceptor + H2O Pseudomonas putida degradation of the toxic p-cresol 4-hydroxybenzaldehyde + reduced acceptor
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Organism

EC Number Organism UniProt Comment Textmining
1.17.9.1 Pseudomonas putida
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-
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.17.9.1 4-cresol + acceptor + H2O the enzyme catalyzes both 4-cresol hydroxylation and further oxidation of the product, 4-hydroxybenzyl alcohol to 4-hydroxybenzaldehyde Pseudomonas putida 4-hydroxybenzaldehyde + reduced acceptor
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 ?
1.17.9.1 4-cresol + acceptor + H2O degradation of the toxic p-cresol Pseudomonas putida 4-hydroxybenzaldehyde + reduced acceptor
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 ?
1.17.9.1 4-hydroxybenzyl alcohol + acceptor
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 Pseudomonas putida 4-hydroxybenzaldehyde + reduced acceptor
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 ?

Cofactor

EC Number Cofactor Comment Organism Structure
1.17.9.1 cytochrome c a flavocytochrome c Pseudomonas putida
1.17.9.1 FAD a flavocytochrome c Pseudomonas putida