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Literature summary for 1.14.13.7 extracted from

  • Tinberg, C.E.; Song, W.J.; Izzo, V.; Lippard, S.J.
    Multiple roles of component proteins in bacterial multicomponent monooxygenases: phenol hydroxylase and toluene/o-xylene monooxygenase from Pseudomonas sp. OX1 (2011), Biochemistry, 50, 1788-1798.
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Pseudomonas sp. only complete enzyme systems containing all three or four protein components are capable of oxidizing phenol. The electron-transfer components exert regulatory effects on substrate oxidation processes taking place at the hydroxylase actives sites, most likely through allostery. The regulatory proteins facilitate the electron-transfer step in the hydrocarbon oxidation cycle in the absence of phenol. Under these conditions, electron consumption is coupled to H2O2 formation in a hydroxylase-dependent manner ?
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?
additional information Pseudomonas sp. OX1 only complete enzyme systems containing all three or four protein components are capable of oxidizing phenol. The electron-transfer components exert regulatory effects on substrate oxidation processes taking place at the hydroxylase actives sites, most likely through allostery. The regulatory proteins facilitate the electron-transfer step in the hydrocarbon oxidation cycle in the absence of phenol. Under these conditions, electron consumption is coupled to H2O2 formation in a hydroxylase-dependent manner ?
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?

Organism

Organism UniProt Comment Textmining
Pseudomonas sp.
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Pseudomonas sp. OX1
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information only complete enzyme systems containing all three or four protein components are capable of oxidizing phenol. The electron-transfer components exert regulatory effects on substrate oxidation processes taking place at the hydroxylase actives sites, most likely through allostery. The regulatory proteins facilitate the electron-transfer step in the hydrocarbon oxidation cycle in the absence of phenol. Under these conditions, electron consumption is coupled to H2O2 formation in a hydroxylase-dependent manner Pseudomonas sp. ?
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?
additional information only complete enzyme systems containing all three or four protein components are capable of oxidizing phenol. The electron-transfer components exert regulatory effects on substrate oxidation processes taking place at the hydroxylase actives sites, most likely through allostery. The regulatory proteins facilitate the electron-transfer step in the hydrocarbon oxidation cycle in the absence of phenol. Under these conditions, electron consumption is coupled to H2O2 formation in a hydroxylase-dependent manner Pseudomonas sp. OX1 ?
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?

Cofactor

Cofactor Comment Organism Structure
[2Fe-2S]-center under ideal conditions, the hydroxylated product yield is about 50% of the diiron centers, suggesting that the enzyme operates by half-sites reactivity mechanisms Pseudomonas sp.