The enzyme, characterized from the bacteria Pseudomonas sp. CF600 and Acinetobacter radioresistens, consists of a multisubunit oxygenease component that contains the active site and a dinuclear iron center, a reductase component that contains FAD and one iron-sulfur cluster, and a regulatory component. The reductase component is responsible for transferring electrons from NADH to the dinuclear iron center.
Specify your search results
The enzyme appears in viruses and cellular organisms
The enzyme, characterized from the bacteria Pseudomonas sp. CF600 and Acinetobacter radioresistens, consists of a multisubunit oxygenease component that contains the active site and a dinuclear iron center, a reductase component that contains FAD and one iron-sulfur cluster, and a regulatory component. The reductase component is responsible for transferring electrons from NADH to the dinuclear iron center.
P19729, i.e. auxiliary protein DmpK, P19734 i.e FAD- and [2Fe-2S]-containing reductase DmpP, P19731 i.e. activator protein DmpM, P19730 i.e. oxygenase component DmpL, P19732 i.e. oxygenase component DmpN, P19733 i.e. oxygenase component DmpO
P19734 i.e FAD- and [2Fe-2S]-containing reductase DmpP, P19731 i.e. activator protein DmpM, P19730 i.e. oxygenase component DmpL, P19732 i.e. oxygenase component DmpN, P19733 i.e. oxygenase component DmpO
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
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
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
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
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
Orenes-Pinero, E.; Garcixada-Carmona, F.; Sanchez-Ferrer, A.
A new process for obtaining hydroxytyrosol using transformed Escherichia coli whole cells with phenol hydroxylase gene from Geobacillus thermoglucosidasius
Food Chem.
139
377-383
2013
Parageobacillus thermoglucosidasius (Q9LAG2 and Q9LAG3)
HOME
login
history
all enzymes
BRENDA home
History
Enzyme Nomenclature
1.14.13.244 phenol 2-monooxygenase (NADH)
top
Information
