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Literature summary extracted from

  • McCormick, M.S.; Lippard, S.J.
    Analysis of substrate access to active sites in bacterial multicomponent monooxygenase hydroxylases: X-ray crystal structure of xenon-pressurized phenol hydroxylase from Pseudomonas sp. OX1 (2011), Biochemistry, 50, 11058-11069.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.14.13.7 computational analyses of the hydrophobic cavities in the hydroxylase alpha-subunits of phenol hydroxylase. Among the xenon-binding sites observed in phenol hydroxylase, more than 80% are localized entirely within the alpha-subunit, and 70% of those occur in the hydrophobic cavities. The hydrophobicity of a large majority of side chain residues contributing to the xenon-binding sites in the phenol hyroxylase alpha-subunit are conserved among bacterial multicomponent monooxygenases. The xenon sites delineate the path of transport of dioxygen to the diiron center during catalysis Pseudomonas sp.

Organism

EC Number Organism UniProt Comment Textmining
1.14.13.7 Pseudomonas sp.
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-
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1.14.13.7 Pseudomonas sp. OX1
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-
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Synonyms

EC Number Synonyms Comment Organism
1.14.13.7 PHH
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Pseudomonas sp.