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 | UniProt | Comment | Textmining |
---|---|---|---|
Acinetobacter radioresistens | - |
S13 | - |
Acinetobacter radioresistens S13 | - |
S13 | - |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
culture condition:phenol-grown cell | - |
Acinetobacter radioresistens | - |
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 | Comment | Organism | Structure |
---|---|---|---|
FAD | the reductase component PHR contains one FAD | Acinetobacter radioresistens |
Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|
Acinetobacter radioresistens | isoelectric point of the regulatory component PHI is 4.1 | - |
additional information |