EC Number   |
General Information |
Reference |
|---|
  1.14.13.244 | physiological function |
auxiliary protein DmpK lacks redox cofactors and strongly inhibits phenol hydroxylase in vitro. DmpK binds to the two largest subunits of the oxygenase component of the hydroxylase and plays a role in assembly of the active form of the oxygenase component of phenol hydroxylase |
751006 |
| 1.14.13.244 | physiological function |
expression of phenol hydroxylase in a laboratory Pseudomonas strain allows growth on phenol |
750938 |
| 1.14.13.244 | physiological function |
phenol hydroxylase comprises three components: DmpP is an FAD- and [2Fe-2S]-containing reductase, DmpM is a cofactorless activator protein, and DmpLNO is the oxygenase. DmpLNO contains the active site, but requires DmpM for efficient turnover. The steady-state turnover rate reaches a maximum at 1.5 DmpM:1 DmpLNO. DmpM interacts with the large subunit of the DmpLNO oxygenase complex. The active site of the oxygenase can accommodate two types of diiron clusters |
749875 |
| 1.14.13.244 | physiological function |
recombinant His6PheA1 exists as a homotetramer of four identical subunits of 62 kDa that has no phenol hydroxylase activity on its own. Recombinant His6PheA2 is a homodimeric flavin reductase, that uses NAD(P)H in order to reduce flavin adenine dinucleotide (FAD), according to a random sequential kinetic mechanism. The hydroxylation of phenol in vitro requires the presence of both His6PheA1 and His6PheA2 components, in addition to NADH and FAD, but the physical interaction between the proteins is not necessary for the reaction |
749721 |
| 1.14.13.244 | physiological function |
subunit DmpP is a flavin adenine dinucleotide containing iron-sulfur protein and probably functions to transfer electrons from NAD(P)H to the iron-requiring oxygenase component |
750939 |
| 1.14.13.244 | physiological function |
the PhP component transfers electrons from NADH to a subcomplex endowed with hydroxylase activity. Subunit PhM displays a regulatory function. Cupling between phenol hydroxylase and toluene/o-xylene monooxygenase optimizes the use of nonhydroxylated aromatic molecules |
749646 |
