1.14.13.244: phenol 2-monooxygenase (NADH)
This is an abbreviated version!
For detailed information about phenol 2-monooxygenase (NADH), go to the full flat file.
Reaction
Synonyms
dmpLMNOP, DmpM, PheA
ECTree
1.14.13.244 phenol 2-monooxygenase (NADH)Advanced search results
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General Information on EC 1.14.13.244 - phenol 2-monooxygenase (NADH)
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
physiological function
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
physiological function
expression of phenol hydroxylase in a laboratory Pseudomonas strain allows growth on phenol
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
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
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
physiological function
Q84AQ4; Q84AQ3; Q84AQ2; Q84AQ1; Q84AQ0
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
