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Literature summary for 1.14.13.7 extracted from

  • Griva, E.; Pessione, E.; Divari, S.; Valetti, F.; Cavaletto, M.; Rossi, G.L.; Giunta, C.
    Phenol hydroxylase from Acinetobacter radioresistens S13. Isolation and characterization of the regulatory component (2003), Eur. J. Biochem., 270, 1434-1440.
    View publication on PubMed

Metals/Ions

Metals/Ions Comment Organism Structure
Iron the reductase component PHR contains one iron-sulfur cluster, whose function is electron transfer from NADH to the dinuclear iron centre of the oxygenase Acinetobacter radioresistens

Organism

Organism UniProt Comment Textmining
Acinetobacter radioresistens
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S13
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Acinetobacter radioresistens S13
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S13
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Source Tissue

Source Tissue Comment Organism Textmining
culture condition:phenol-grown cell
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Acinetobacter radioresistens
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Subunits

Subunits Comment Organism
More the whole enzyme phenol hydroxylase comprises an oxygenase component (PHO), a reductase component (PHR) and a regulatory component (PHI). PHI is required for catalysis of the conversion of phenol to catechol in vitro, but is not required for PHR activity towards alternative electron acceptors such as cytochrome c and Nitro Blue Tetrazolium. The molecular mass of PHI is determined to be 10000 Da by SDS-PAGE, 8800 Da by MALDI-TOF spectrometry and 18000 Da by gel filtration. PHI is in the native state a homodimer. In the reconstituted system, optimal rate is achieved when the stoichiometry of the components is 2 reductase monomers:1 PHI dimer: 1 PHO (alphabetagamma)2 Acinetobacter radioresistens

Cofactor

Cofactor Comment Organism Structure
FAD the reductase component PHR contains one FAD Acinetobacter radioresistens

pI Value

Organism Comment pI Value Maximum pI Value
Acinetobacter radioresistens isoelectric point of the regulatory component PHI is 4.1
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additional information