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Information on EC 1.14.13.244 - phenol 2-monooxygenase (NADH)
for references in articles please use BRENDA:EC1.14.13.244
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EC Tree 1 Oxidoreductases
1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
1.14.13 With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor
1.14.13.244 phenol 2-monooxygenase (NADH)
IUBMB Comments
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.
The enzyme appears in viruses and cellular organisms
showSynonyms
dmpLMNOP, DmpM, PheA, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dmpLMNOP
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
phenol + NADH + H+ + O2 = catechol + NAD+ + H2O
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
KEGG
MetaCyc
benzene degradation II (aerobic)
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SYSTEMATIC NAME
IUBMB Comments
phenol,NADH:oxygen oxidoreductase (2-hydroxylating)
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.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
benzene + NADH + H+ + O2
phenol + NAD+ + H2O
Q84AQ4; Q84AQ3; Q84AQ2; Q84AQ1; Q84AQ0
Substrates: -
Products: -
Products: -
?
tyrosol + NADH + H+ + O2
hydroxytyrosol + NAD+ + H2O
Substrates: -
Products: -
Products: -
?
phenol + NADH + H+ + O2
catechol + NAD+ + H2O
Substrates: -
Products: -
Products: -
?
phenol + NADH + H+ + O2
catechol + NAD+ + H2O
Substrates: -
Products: -
Products: -
?
phenol + NADH + H+ + O2
catechol + NAD+ + H2O
Q84AQ4; Q84AQ3; Q84AQ2; Q84AQ1; Q84AQ0
Substrates: -
Products: -
Products: -
?
phenol + NADH + H+ + O2
catechol + NAD+ + H2O
Substrates: -
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
phenol + NADH + H+ + O2
catechol + NAD+ + H2O
Substrates: -
Products: -
Products: -
?
phenol + NADH + H+ + O2
catechol + NAD+ + H2O
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2Fe-2S-center
subunit DmpP is a flavin adenine dinucleotide containing iron-sulfur protein
2Fe-2S-center
subunit DmpP is a [2Fe-2S]-containing reductase
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Iron
subunit DmpP is a [2Fe-2S]-containing reductase
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
p-hydroxymercuribenzoate
0.02 mM, no residual activity
additional information
not inhibitory: phenol at 0.5 mM
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00061
phenol
Q84AQ4; Q84AQ3; Q84AQ2; Q84AQ1; Q84AQ0
25Ā°C, pH not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.286
phenol
Q84AQ4; Q84AQ3; Q84AQ2; Q84AQ1; Q84AQ0
25Ā°C, pH not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
469
phenol
Q84AQ4; Q84AQ3; Q84AQ2; Q84AQ1; Q84AQ0
25Ā°C, pH not specified in the publication
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Q9LAG2 i.e. subunit PheA2, Q9LAG3 i.e. subunit PheA1
UniProt
brenda
Q84AQ4 i.e. subunit PhL, Q84AQ3 i.e. subunit PhM, Q84AQ2 i.e. subunit PhN, Q84AQ1 i.e. subunit PhO, Q84AQ0 i.e. subunit PhP
Q84AQ4; Q84AQ3; Q84AQ2; Q84AQ1; Q84AQ0
UniProt
brenda
A7LCL0 i.e. subunit PheA1, A7LCL1 i.e subunit PheA2
UniProt
brenda
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
UniProt
brenda
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
UniProt
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). DMPL_ACICP
Acinetobacter calcoaceticus (strain PHEA-2)
332
0
38226
Swiss-Prot
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 17800, subunit PheA2, x * 57000, subunit PheA1, calculated from sequence
heteromer
4 * 60720, His-tagged subunit PheA1, 2 * 20350, His-tagged subunit PheA2, calculated from sequence. 4 * 62000, His-tagged subunit PheA1, 2 * 22000, His-tagged subunit PheA2, SDS-PAGE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
subunit DmpK, expression in Escherichia coli
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
degradation
strain is able to degrade phenol at levels to 15 mM at a rate of 0.85 micromol/h
synthesis
production of hydroxytyrosol by conversion of tyrosol using phenol hydroxylase
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Gurujeyalakshmi, G.; Oriel, P.
Isolation of phenol-degrading Bacillus stearothermophilus and partial characterization of the phenol hydroxylase
Appl. Environ. Microbiol.
55
500-502
1989
Geobacillus stearothermophilus (Q45413)
-
brenda
Cafaro, V.; Izzo, V.; Scognamiglio, R.; Notomista, E.; Capasso, P.; Casbarra, A.; Pucci, P.; Di Donato, A.
Phenol hydroxylase and toluene/o-xylene monooxygenase from Pseudomonas stutzeri OX1 interplay between two enzymes
Appl. Environ. Microbiol.
70
2211-2219
2004
Pseudomonas stutzeri (Q84AQ4 and Q84AQ3 and Q84AQ2 and Q84AQ1 and Q84AQ0)
brenda
Saa, L.; Jaureguibeitia, A.; Largo, E.; Llama, M.; Serra, J.
Cloning, purification and characterization of two components of phenol hydroxylase from Rhodococcus erythropolis UPV-1
Appl. Microbiol. Biotechnol.
86
201-211
2010
Rhodococcus erythropolis (A7LCL0 and A7LCL1)
brenda
Qian, H.; Edlund, U.; Powlowski, J.; Shingler, V.; Sethson, I.
Solution structure of phenol hydroxylase protein component P2 determined by NMR spectroscopy
Biochemistry
36
495-504
1997
Pseudomonas sp. CF600 (P19731)
brenda
Cadieux, E.; Vrajmasu, V.; Achim, C.; Powlowski, J.; Muenck, E.
Biochemical, Moessbauer, and EPR studies of the diiron cluster of phenol hydroxylase from Pseudomonas sp. strain CF 600
Biochemistry
41
10680-10691
2002
Pseudomonas sp. CF600 (P19734 and P19731 and P19730 and P19732 and P19733)
brenda
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)
-
brenda
Nordlund, I.; Powlowski, J.; Shingler, V.
Complete nucleotide sequence and polypeptide analysis of multicomponent phenol hydroxylase from Pseudomonas sp. strain CF600
J. Bacteriol.
172
6826-6833
1990
Pseudomonas sp. CF600 (P19734 and P19731 and P19730 and P19732 and P19733)
brenda
Powlowski, J.; Shingler, V.
In vitro analysis of polypeptide requirements of multicomponent phenol hydroxylase from Pseudomonas sp. strain CF600
J. Bacteriol.
172
6834-6840
1990
Pseudomonas sp. CF600 (P19734 and P19731 and P19730 and P19732 and P19733)
brenda
Powlowski, J.; Sealy, J.; Shingler, V.; Cadieux, E.
On the role of DmpK, an auxiliary protein associated with multicomponent phenol hydroxylase from Pseudomonas sp. strain CF600
J. Biol. Chem.
272
945-951
1997
Pseudomonas sp. CF600 (P19729 and P19734 and P19731 and P19730 and P19732 and P19733)
brenda
EXTERNAL LINKS (specific for EC-Number 1.14.13.244)
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Release 2023.1 (January 2023)
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