Information on EC 1.14.13.7 - phenol 2-monooxygenase:
   PRINT
Please wait a moment until all data are loaded. This message will disappear when all data are loaded.
Mark a special word or phrase in this record:  
Select one or more organisms in this record:

Show additional data Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)

Please login to have access to the AMENDA and FRENDA data

EC NUMBERCOMMENTARY
1.14.13.7-

RECOMMENDED NAMEGeneOntology No.
phenol 2-monooxygenaseGO:0018662

REACTIONREACTION DIAGRAMCOMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
phenol + NADPH + H+ + O2 = catechol + NADP+ + H2O
show the reaction diagram		----
phenol + NADPH + H+ + O2 = catechol + NADP+ + H2O
show the reaction diagram		catalytic mechanism, conformational changes upon binding of the regulatory protein comonent and effects on catalytic activityPseudomonas sp.-672112

REACTION TYPEORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
oxidation----
redox reaction----
reduction----

PATHWAYKEGG LinkMetaCyc Link
phenol degradation I (aerobic)-PWY-5418

SYSTEMATIC NAMEIUBMB Comments
phenol,NADPH:oxygen oxidoreductase (2-hydroxylating)A flavoprotein (FAD). Also active with resorcinol and 2-methylphenol.

SYNONYMSORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
LmPHAlcaligenes faecalisA5HMH6, A5HMH7, A5HMH8, A5HMH9, A5HMI0, A5HMI1, Q6V9W5; 701413
LmPHuncultured microorganismA5YUW2, A5YUW3, A5YUW6, A5YUY2, A5YUY5, A5YUY6, A5YUY7, A5YUZ3, A5YUZ5, A5YUZ6, A5YUZ7, A5YUZ8, A5YUZ9, A5YV00, A5YV01, A5YV02, A5YV03, A5YV04, A5YV05, A5YV06, A5YV08, A5YV10, A5YV11, A5YV12, A5YV13, A5YV14, A5YV15, A5YV16, A5YV18, A5YV19, A5YV20-701833
LmPHAcinetobacter sp. PND-4A5Z0R4-704033
LmPHAcinetobacter sp. PND-5A5Z0R5-704033
LmPHComamonas sp. PND-3A7L9S9-704033
LmPHCupriavidus sp. PND-6A7L9T0-704033
LmPHPseudomonas sp. PND-1A7L9S7-704033
LmPHPseudomonas sp. PND-2A7L9S8-704033
MphPseudomonas sp.--659881
MphPseudomonas fluorescens, Pseudomonas mendocina, Pseudomonas putida--685427
MphAlcaligenes faecalisA5HMH6, A5HMH7, A5HMH8, A5HMH9, A5HMI0, A5HMI1, Q6V9W5; 701413
MphNAcinetobacter calcoaceticus--703338
multi-component phenol hydroxylaseAcinetobacter calcoaceticus--703338
multicomponent PHPseudomonas fluorescens, Pseudomonas mendocina, Pseudomonas putida--685427
multicomponent phenol hydroxylasePseudomonas sp.--659881, 675732
multicomponent phenol hydroxylaseAlcaligenes faecalisA5HMH6, A5HMH7, A5HMH8, A5HMH9, A5HMI0, A5HMI1, Q6V9W5; 701413
multicomponent phenol hydroxylaseAcinetobacter sp. PND-4A5Z0R4-704033
multicomponent phenol hydroxylaseAcinetobacter sp. PND-5A5Z0R5-704033
multicomponent phenol hydroxylaseComamonas sp. PND-3A7L9S9-704033
multicomponent phenol hydroxylaseCupriavidus sp. PND-6A7L9T0-704033
multicomponent phenol hydroxylasePseudomonas sp. PND-1A7L9S7-704033
multicomponent phenol hydroxylasePseudomonas sp. PND-2A7L9S8-704033
oxygenase, phenol 2-mono-----
PHEuncultured microorganism--703484
PheAGeobacillus thermoglucosidasius-the two-protein system phenol hydroxylase, encoded by the pheA1 and pheA2 genes, consists of an oxygenase (PheA1) and a flavin reductase (PheA2)659279
PheA1Geobacillus stearothermophilus--691504
PheA1Rhodococcus erythropolisA7LCL0, A7LCL1-701875
PheA2Geobacillus stearothermophilus--691504
PheA2Rhodococcus erythropolisA7LCL0, A7LCL1-701875
phenol hydroxylase----
phenol hydroxylaseAcinetobacter radioresistens-multicomponent enzyme made up of three moieties: a reductase (PHR), and an oxygenase (PHO) and a regulative component658619
phenol hydroxylaseGeobacillus thermoglucosidasius-the two-protein system, encoded by the pheA1 and pheA2 genes, consists of an oxygenase (PheA1) and a flavin reductase (PheA2)659279
phenol hydroxylasePseudomonas stutzeri--671421, 671422
phenol hydroxylasePseudomonas sp.--671532, 671645, 672112, 711022
phenol hydroxylaseCandida albicans--672664
phenol hydroxylasePseudomonas fluorescens, Pseudomonas mendocina, Pseudomonas putida--685427
phenol hydroxylaseTrichosporon cutaneum--690215, 690216
phenol hydroxylaseGeobacillus stearothermophilus--691504
phenol hydroxylaseAlcaligenes faecalisA5HMH6, A5HMH7, A5HMH8, A5HMH9, A5HMI0, A5HMI1, Q6V9W5-701413
phenol hydroxylaseuncultured microorganismA5YUW2, A5YUW3, A5YUW6, A5YUY2, A5YUY5, A5YUY6, A5YUY7, A5YUZ3, A5YUZ5, A5YUZ6, A5YUZ7, A5YUZ8, A5YUZ9, A5YV00, A5YV01, A5YV02, A5YV03, A5YV04, A5YV05, A5YV06, A5YV08, A5YV10, A5YV11, A5YV12, A5YV13, A5YV14, A5YV15, A5YV16, A5YV18, A5YV19, A5YV20-701833
phenol hydroxylaseRhodococcus erythropolisA7LCL0, A7LCL1; 701875
phenol hydroxylaseuncultured microorganism--703484
phenol hydroxylaseTrametes versicolor--704952
phenol o-hydroxylase----
PHHPseudomonas sp.--672112
PHOAcinetobacter radioresistens-oxygenase component of the phenyl hydroxylase658619
PHRAcinetobacter radioresistens-reductase component of phenyl hydroxylase658619
single-component PHPseudomonas fluorescens, Pseudomonas putida--685427
SPHPseudomonas fluorescens, Pseudomonas putida--685427

CAS REGISTRY NUMBERCOMMENTARY
37256-84-1-

ORGANISMCOMMENTARYLITERATURESEQUENCE CODESEQUENCE DB SOURCE
Acinetobacter calcoaceticusstrains PHEA-2 or PHEA-12703338--Manually annotated by BRENDA team
Acinetobacter radioresistens-438797--Manually annotated by BRENDA team
Acinetobacter radioresistensS13658615, 658619--Manually annotated by BRENDA team
Acinetobacter sp. PND-4-704033A5Z0R4UniProtManually annotated by BRENDA team
Acinetobacter sp. PND-5-704033A5Z0R5UniProtManually annotated by BRENDA team
Alcaligenes faecalisstrain IS-46701413A5HMH6, A5HMH7, A5HMH8, A5HMH9, A5HMI0, A5HMI1, Q6V9W5UniProtManually annotated by BRENDA team
Alcaligenes faecalisstrain IS-67701413--Manually annotated by BRENDA team
Alcaligenes faecalis IS-46strain IS-46701413A5HMH6, A5HMH7, A5HMH8, A5HMH9, A5HMI0, A5HMI1, Q6V9W5UniProtManually annotated by BRENDA team
Alcaligenes faecalis IS-67strain IS-67701413--Manually annotated by BRENDA team
Alcaligenes sp. A7strain A7659279--Manually annotated by BRENDA team
Bacillus subtilis R5strain R5662875--Manually annotated by BRENDA team
Brevibacterium fuscum-438778--Manually annotated by BRENDA team
Candida albicansstrain TL3672664--Manually annotated by BRENDA team
Candida tropicalis-394993, 658813, 660560--Manually annotated by BRENDA team
Comamonas sp. PND-3-704033A7L9S9UniProtManually annotated by BRENDA team
Comamonas testosteronistrain R5662875--Manually annotated by BRENDA team
Cupriavidus necatorstrain E2, formerly Alcaligenes sp.438792--Manually annotated by BRENDA team
Cupriavidus oxalaticus OX1strain OX1672112--Manually annotated by BRENDA team
Cupriavidus sp. PND-6-704033A7L9T0UniprotManually annotated by BRENDA team
Escherichia coli JM109strain JM109690216--Manually annotated by BRENDA team
Geobacillus stearothermophilus-691504--Manually annotated by BRENDA team
Geobacillus thermoglucosidasiusstrain A7659279--Manually annotated by BRENDA team
no activity in Escherichia colistrain JM109690216--Manually annotated by BRENDA team
no activity in Lactobacillus acidophilusstrain ATCC 4356690216--Manually annotated by BRENDA team
Pseudomonas fluorescensgene pheBA, single and multicomponent enzyme containing strains C PC24, F PC20, C PC31, F P69, B PC18, and F PC17685427--Manually annotated by BRENDA team
Pseudomonas mendocinamulticomponent enzyme containing strain PC1685427--Manually annotated by BRENDA team
Pseudomonas putidagene pheBA, single and multicomponent enzyme containing strains B PC30, B PC16, and EST1412685427--Manually annotated by BRENDA team
Pseudomonas sp.-711022--Manually annotated by BRENDA team
Pseudomonas sp.diverse strains, overview671645--Manually annotated by BRENDA team
Pseudomonas sp.strain CF600438790, 671532--Manually annotated by BRENDA team
Pseudomonas sp.strain KL28659881--Manually annotated by BRENDA team
Pseudomonas sp.strain OX1672112--Manually annotated by BRENDA team
Pseudomonas sp.strains KL28 and KL33675732--Manually annotated by BRENDA team
Pseudomonas sp. KL28strain KL28659881--Manually annotated by BRENDA team
Pseudomonas sp. OX1-711022--Manually annotated by BRENDA team
Pseudomonas sp. PND-1-704033A7L9S7UniProtManually annotated by BRENDA team
Pseudomonas sp. PND-2-704033A7L9S8UniProtManually annotated by BRENDA team
Pseudomonas stutzeristrain OX1657596, 671421, 671422--Manually annotated by BRENDA team
Rhodococcus erythropolisUPV-1701875A7LCL0, A7LCL1UniProtManually annotated by BRENDA team
Rhodococcus erythropolis UPV-1UPV-1701875A7LCL0, A7LCL1UniProtManually annotated by BRENDA team
Rhodococcus sp.strain P1438788--Manually annotated by BRENDA team
Sulfolobus solfataricus P1strain P1438788--Manually annotated by BRENDA team
Trametes versicolorstrain 1704952--Manually annotated by BRENDA team
Trichosporon cutaneum-438779, 438781, 438782, 438784, 438785, 438789, 438791, 438793, 438794, 438796, 438798, 438799, 438800, 438801, 657449--Manually annotated by BRENDA team
Trichosporon cutaneumR57, mutants able to degrade higher phenol concentration exhibits elevated specific activity658569--Manually annotated by BRENDA team
Trichosporon cutaneumstrain NBIMCC 2414, strain ATCC 46490, and strain ATCC 58094, isolated from different waste waters, gene phyA690216--Manually annotated by BRENDA team
Trichosporon cutaneumstrain R57690215--Manually annotated by BRENDA team
Trichosporon cutaneumyeast438777, 438780, 438783, 438786, 438795--Manually annotated by BRENDA team
Trichosporon cutaneum R57strain R57690215--Manually annotated by BRENDA team
uncultured microorganism-701833A5YUW2, A5YUW3, A5YUW6, A5YUY2, A5YUY5, A5YUY6, A5YUY7, A5YUZ3, A5YUZ5, A5YUZ6, A5YUZ7, A5YUZ8, A5YUZ9, A5YV00, A5YV01, A5YV02, A5YV03, A5YV04, A5YV05, A5YV06, A5YV08, A5YV10, A5YV11, A5YV12, A5YV13, A5YV14, A5YV15, A5YV16, A5YV18, A5YV19, A5YV20UniProtManually annotated by BRENDA team
uncultured microorganism-703484--Manually annotated by BRENDA team
Vibrio sp. 1strain 1704952--Manually annotated by BRENDA team

GENERAL INFORMATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
physiological functionGeobacillus stearothermophilus-the enzyme is a component of the operon encoding the meta-pathway genes, it catalyzes the first step of the phenol degradative meta-pathway691504
metabolismuncultured microorganism-the enzyme is an indicator of aerobic benzene, toluene, ethylbenzene, and xylenes biodegradation potential703484
additional informationPseudomonas sp.-PHK, the accessory component of the phenol hydroxylase, is neither involved in the catalytic activity of the phenol hydroxylase complex nor required for the assembly of apo-hydroxylase, but may be responsible for enhancing iron incorporation into the active site of the apo-hydroxylase711022

SUBSTRATEPRODUCT                      REACTION DIAGRAMORGANISM UNIPROT ACCESSION NO. COMMENTARY/
Substrate		 LITERATURE/
Substrate		 COMMENTARY/
Product		 LITERATURE/
Product		 Reversibility
r=reversible
ir=irreversible
?=not specified
2,3,4-trifluorophenol + O2 + NADPH?
show the reaction diagram		Trichosporon cutaneum--438795--?
2,3,5,6-tetrafluorophenol + O2 + NADPH?
show the reaction diagram		Trichosporon cutaneum--438795--?
2,3,5,6-tetrafluorophenol + O2 + NADPH3,4,6-trifluoro-2-benzoquinone + NADP+ + F-
show the reaction diagram		Trichosporon cutaneum--438782-438782?
2,3,5-trifluorophenol + O2 + NADPH?
show the reaction diagram		Trichosporon cutaneum--438795--?
2,3,6-trifluorophenol + O2 + NADPH?
show the reaction diagram		Trichosporon cutaneum--438795--?
2,3-difluorophenol + O2 + NADPH?
show the reaction diagram		Trichosporon cutaneum--438795--?
2,4-difluorophenol + O2 + NADPH?
show the reaction diagram		Trichosporon cutaneum--438795--?
2,5-difluorophenol + O2 + NADPH?
show the reaction diagram		Trichosporon cutaneum--438795--?
2,6-difluorophenol + O2 + NADPH?
show the reaction diagram		Trichosporon cutaneum--438795--?
2-amino-3-methylphenol + O2 + NADPH?
show the reaction diagram		Brevibacterium fuscum--438778--?
2-aminophenol + O2 + NADPH?
show the reaction diagram		Candida tropicalis--394993--?
2-aminophenol + O2 + NADPH?
show the reaction diagram		Rhodococcus sp.--438788--?
2-aminophenol + O2 + NADPH?
show the reaction diagram		Trichosporon cutaneum--438777--?
2-aminophenol + O2 + NADPH?
show the reaction diagram		Brevibacterium fuscum--438778--?
2-chlorophenol + O2 + NADPH?
show the reaction diagram		Candida tropicalis--394993--?
2-chlorophenol + O2 + NADPH?
show the reaction diagram		Rhodococcus sp.--438788--?
2-chlorophenol + O2 + NADPH?
show the reaction diagram		Trichosporon cutaneum--438777, 438783--?
2-chlorophenol + O2 + NADPH?
show the reaction diagram		Brevibacterium fuscum--438778--?
2-cresol + NADPH + O22-methylcatechol + 4-methylcatechol + NADP+ + H2O
show the reaction diagram		Pseudomonas stutzeri--671421--?
2-ethylphenol + NADPH + O23-ethyl-benzene-1,2-diol + NADP+ + H2O
show the reaction diagram		Comamonas testosteroni-18% of the activity with phenol662875--?
2-fluorophenol + O2 + NADPH?
show the reaction diagram		Trichosporon cutaneum--438777, 438783, 438789, 438795--?
2-hydroxyphenol + NADPH + H+ + O2?
show the reaction diagram		Trichosporon cutaneum-about 70% of the activity with phenol690215--?
2-methyl-phenol + O2 + NADPH?
show the reaction diagram		Rhodococcus sp.--438788--?
2-methyl-phenol + O2 + NADPH?
show the reaction diagram		Trichosporon cutaneum--438783--?
2-methyl-phenol + O2 + NADPH?
show the reaction diagram		Candida tropicalis-i.e. o-cresol394993--?
2-methyl-phenol + O2 + NADPH?
show the reaction diagram		Brevibacterium fuscum-i.e. o-cresol438778--?
2-methylindole + NADPH + O2?
show the reaction diagram		Pseudomonas sp.--675732--?
2-nitrophenol + NADPH + H+ + O2?
show the reaction diagram		Trichosporon cutaneum-about 80% of the activity with phenol690215--?
2-xylene + NADPH + O22,3-dimethylphenol + 3,4-dimethylphenol + NADP+ + H2O
show the reaction diagram		Pseudomonas stutzeri--671421, 671422--?
3,4,5-trifluorophenol + O2 + NADPH?
show the reaction diagram		Trichosporon cutaneum--438795--?
3,4-difluorophenol + O2 + NADPH?
show the reaction diagram		Trichosporon cutaneum--438795--?
3,4-dimethylphenol + NADH + H+ + O21,2-dihydroxy-3,4-dimethylbenzene + NAD+ + H2O
show the reaction diagram		Acinetobacter radioresistens-85% of the activity with phenol658619--?
3,4-dimethylphenol + NADPH + O2?
show the reaction diagram		Comamonas testosteroni-72% of the activity with phenol662875--?
3,5-difluorophenol + O2 + NADPH?
show the reaction diagram		Trichosporon cutaneum--438795--?
3-aminophenol + O2 + NADPH?
show the reaction diagram		Candida tropicalis--394993--?
3-aminophenol + O2 + NADPH?
show the reaction diagram		Rhodococcus sp.--438788--?
3-aminophenol + O2 + NADPH?
show the reaction diagram		Trichosporon cutaneum--438777, 438782--?
3-aminophenol + O2 + NADPH?
show the reaction diagram		Brevibacterium fuscum--438778--?
3-chloro-4-fluorophenol + O2 + NADPH?
show the reaction diagram		Trichosporon cutaneum--438795--?
3-chlorophenol + NADH + H+ + O24-chlorocatechol + NAD+ + H2O
show the reaction diagram		Acinetobacter radioresistens-15% of the activity with phenol658619--?
3-chlorophenol + O2 + NADPH?
show the reaction diagram		Candida tropicalis--394993--?
3-chlorophenol + O2 + NADPH?
show the reaction diagram		Rhodococcus sp.--438788--?
3-chlorophenol + O2 + NADPH?
show the reaction diagram		Trichosporon cutaneum--438777, 438782, 438783, 438789--?
3-chlorophenol + O2 + NADPH?
show the reaction diagram		Brevibacterium fuscum--438778--?
3-cresol + NADPH + O23-methylcatechol + 4-methylcatechol + NADP+ + H2O
show the reaction diagram		Pseudomonas stutzeri--671421--?
3-cyanoindole + NADPH + O2?
show the reaction diagram		Pseudomonas sp.-substrate only of strain KL28675732--?
3-ethylphenol + NADH + H+ + O24-ethylcatechol + NAD+ + H2O
show the reaction diagram		Pseudomonas sp.--659881--?
3-fluorophenol + O2 + NADPH?
show the reaction diagram		Trichosporon cutaneum--438777, 438783, 438789, 438795--?
3-fluorophenol + O2 + NADPH?
show the reaction diagram		Trichosporon cutaneum-below pH 6.5 3-fluorophenol is preferentially hydroxylated at the C6 ortho position, at increasing pH the C2 ortho-hydroxylation becomes more predominant438796--?
3-hydroxyphenol + NADPH + H+ + O2?
show the reaction diagram		Trichosporon cutaneum-about 60% of the activity with phenol690215--?
3-hydroxyphenol + O2 + NADPH?
show the reaction diagram		Trichosporon cutaneum--438782--?
3-methylphenol + O2 + NADPH?
show the reaction diagram		Rhodococcus sp.--438788--?
3-methylphenol + O2 + NADPH?
show the reaction diagram		Trichosporon cutaneum--438782, 438783, 438789--?
3-methylphenol + O2 + NADPH?
show the reaction diagram		Candida tropicalis-i.e. m-cresol394993--?
3-methylphenol + O2 + NADPH?
show the reaction diagram		Trichosporon cutaneum-i.e. m-cresol438801--?
3-methylphenol + O2 + NADPH?
show the reaction diagram		Brevibacterium fuscum-i.e. m-cresol438778--?
3-nitrophenol + NAD(P)H + H+ + O2? + NAD(P)+ + H2O
show the reaction diagram		Rhodococcus erythropolisA7LCL0, A7LCL1-701875--?
3-nitrophenol + NADPH + H+ + O2?
show the reaction diagram		Trichosporon cutaneum-about 45% of the activity with phenol690215--?
4-aminophenol + O2 + NADPH?
show the reaction diagram		Candida tropicalis--394993--?
4-aminophenol + O2 + NADPH?
show the reaction diagram		Rhodococcus sp.--438788--?
4-aminophenol + O2 + NADPH?
show the reaction diagram		Trichosporon cutaneum--438777--?
4-aminophenol + O2 + NADPH?
show the reaction diagram		Brevibacterium fuscum--438778--?
4-chloro-3-fluorophenol + O2 + NADPH?
show the reaction diagram		Trichosporon cutaneum--438795--?
4-chlorocatechol + O2 + NADPH?
show the reaction diagram		Candida tropicalis--394993--?
4-chlorophenol + NADH + H+ + O21,2-dihydroxy-4-methylbenzene + NAD+ + H2O
show the reaction diagram		Acinetobacter radioresistens--658619--?
4-chlorophenol + NADH + H+ + O24-chlorocatechol + NAD+ + H2O
show the reaction diagram		Acinetobacter radioresistens-27% of the activity with phenol658619--?
4-chlorophenol + O2 + NADPH?
show the reaction diagram		Candida tropicalis--394993--?
4-chlorophenol + O2 + NADPH?
show the reaction diagram		Rhodococcus sp.--438788--?
4-chlorophenol + O2 + NADPH?
show the reaction diagram		Trichosporon cutaneum--438777, 438783, 438789, 438793--?
4-chlorophenol + O2 + NADPH?
show the reaction diagram		Brevibacterium fuscum--438778--?
4-cresol + NADPH + O24-methylcatechol + NADP+ + H2O
show the reaction diagram		Pseudomonas stutzeri-best substrate671421--?
4-ethylphenol + NADH + H+ + O24-ethylcatechol + NAD+ + H2O
show the reaction diagram		Pseudomonas sp.--659881--?
4-fluorophenol + NADH + H+ + O21,2-dihydroxy-4-fluorobenzene + NAD+ + H2O
show the reaction diagram		Acinetobacter radioresistens--658619--?
4-fluorophenol + O2 + NADPH?
show the reaction diagram		Trichosporon cutaneum--438777, 438783, 438789, 438793, 438795--?
4-hydroxyindole + NADPH + O2?
show the reaction diagram		Pseudomonas sp.--675732--?
4-hydroxyphenol + NADPH + H+ + O2?
show the reaction diagram		Trichosporon cutaneum-about 120% of the activity with phenol690215--?
4-hydroxyphenol + O2 + NADPH?
show the reaction diagram		Trichosporon cutaneum--438782--?
4-methoxyindole + NADPH + O2?
show the reaction diagram		Pseudomonas sp.-substrate only of strain KL28675732--?
4-methyl-phenol + O2 + NADPH?
show the reaction diagram		Rhodococcus sp.--438788--?
4-methyl-phenol + O2 + NADPH?
show the reaction diagram		Trichosporon cutaneum--438783, 438789, 438793--?
4-methyl-phenol + O2 + NADPH?
show the reaction diagram		Brevibacterium fuscum--438778--?
4-methyl-phenol + O2 + NADPH?
show the reaction diagram		Candida tropicalis-i.e. p-cresol394993--?
4-methylindole + NADPH + O2?
show the reaction diagram		Pseudomonas sp.-substrate only of strain KL28675732--?
4-methylphenol + NADH + H+ + O21,2-dihydroxy-4-methylbenzene + NAD+ + H2O
show the reaction diagram		Acinetobacter radioresistens--658619--?
4-nitrophenol + NAD(P)H + H+ + O2? + NAD(P)+ + H2O
show the reaction diagram		Rhodococcus erythropolisA7LCL0, A7LCL1-701875--?
4-nitrophenol + NADPH + H+ + O2?
show the reaction diagram		Trichosporon cutaneum-about 50% of the activity with phenol690215--?
4-propylphenol + NADH + H+ + O24-propylcatechol + NAD+ + H2O
show the reaction diagram		Pseudomonas sp.-low activity659881--?
5-aminoindole + NADPH + O2?
show the reaction diagram		Pseudomonas sp.--675732--?
5-fluoroindole + NADPH + O2?
show the reaction diagram		Pseudomonas sp.-substrate only of strain KL33675732--?
5-hydroxyindole + NADPH + O2?
show the reaction diagram		Pseudomonas sp.--675732--?
5-methoxyindole + NADPH + O2?
show the reaction diagram		Pseudomonas sp.--675732--?
5-methylindole + NADPH + O2?
show the reaction diagram		Pseudomonas sp.-substrate only of strain KL33675732--?
6-chloroindole + NADPH + O2?
show the reaction diagram		Pseudomonas sp.-substrate only of strain KL33675732--?
6-methoxyindole + NADPH + O2?
show the reaction diagram		Pseudomonas sp.--675732--?
6-methylindole + NADPH + O2?
show the reaction diagram		Pseudomonas sp.-substrate only of strain KL33675732--?
7-chloroindole + NADPH + O2?
show the reaction diagram		Pseudomonas sp.-substrate only of strain KL33675732--?
7-methylindole + NADPH + O2?
show the reaction diagram		Pseudomonas sp.--675732--?
benzene + NADPH + O2?
show the reaction diagram		Comamonas testosteroni-26% of the activity with phenol662875--?
benzene + NADPH + O2 + H+toluene + NADP+ + H2O
show the reaction diagram		Pseudomonas sp.--671532--?
benzene + NADPH + O2 + H+toluene + NADP+ + H2O
show the reaction diagram		Pseudomonas stutzeri--671421--?
catechol + O2 + NADPH?
show the reaction diagram		Candida tropicalis--394993--?
catechol + O2 + NADPH?
show the reaction diagram		Trichosporon cutaneum--438783, 438789--?
catechol + O2 + NADPH?
show the reaction diagram		Rhodococcus sp.-not438788---
ethynylbenzene + NADPH + O22-ethynylphenol + 2-hydroxy-6-oxo-octa-2,4-dien-7-ynoic acid + NADP+ + H2O
show the reaction diagram		Pseudomonas sp.--671532product identification by GC-MS-?
ethynylbenzene + NADPH + O22-ethynylphenol + 2-hydroxy-6-oxo-octa-2,4-dien-7-ynoic acid + NADP+ + H2O
show the reaction diagram		Pseudomonas sp.-substrate only for phenol-grown cells671532--?
indole + NADPH + O27-hydroxyindole + NADP+ + H2O
show the reaction diagram		Pseudomonas sp.--675732--?
m-chlorophenol + NADPH + O24-chloro-benzene-1,2-diol + NADP+ + H2O
show the reaction diagram		Comamonas testosteroni-18% of the activity with phenol662875--?
m-cresol + NADH + H+ + O24-methylcatechol + NAD+ + H2O
show the reaction diagram		Pseudomonas sp.--659881--?
m-cresol + NADH + H+ + O24-methylcatechol + NAD+ + H2O
show the reaction diagram		Acinetobacter radioresistens-60% of the activity with phenol658619--?
m-cresol + NADPH + O2?
show the reaction diagram		Comamonas testosteroni-114% of the activity with phenol662875--?
o-chlorophenol + NADPH + O23-chloro-benzene-1,2-diol + NADP+ + H2O
show the reaction diagram		Comamonas testosteroni-20% of the activity with phenol662875--?
o-cresol + NADH + H+ + O23-methylcatechol + NAD+ + H2O
show the reaction diagram		Pseudomonas sp.-low activity659881--?
o-cresol + NADH + H+ + O23-methylcatechol + NAD+ + H2O
show the reaction diagram		Acinetobacter radioresistens-60% of the activity with phenol658619--?
o-cresol + NADPH + O23-methylcatechol + NADP+ + H2O
show the reaction diagram		Comamonas testosteroni-37% of the activity with phenol, measured as substrate-dependent oxygen uptake rate by derivatives of Pseudomonas aeruginosa PAO1c carrying the enzyme genes after induction with phenol662875--?
orcinol + NADPH + O2?
show the reaction diagram		Comamonas testosteroni-46% of the activity with phenol662875--?
orcinol + O2 + NADPH?
show the reaction diagram		Brevibacterium fuscum--438778--?
orcinol + O2 + NADPH?
show the reaction diagram		Candida tropicalis-weak394993--?
oxindole + NADPH + O2?
show the reaction diagram		Pseudomonas sp.--675732--?
p-chlorophenol + NADPH + O2?
show the reaction diagram		Comamonas testosteroni-84% of the activity with phenol662875--?
p-cresol + NADH + H+ + O24-methylcatechol + NAD+ + H2O
show the reaction diagram		Pseudomonas sp.--659881--?
p-cresol + NADH + H+ + O24-methylcatechol + NAD+ + H2O
show the reaction diagram		Acinetobacter radioresistens-60% of the activity with phenol658619--?
p-cresol + NADPH + O24-methylcatechol + NADP+ + H2O
show the reaction diagram		Comamonas testosteroni-114% of the activity with phenol662875--?
pentafluorophenol + O2 + NADPH?
show the reaction diagram		Trichosporon cutaneum--438795--?
phenol + NAD(P)H + H+ + O2catechol + NAD(P)+ + H2O
show the reaction diagram		Alcaligenes faecalisA5HMH6, A5HMH7, A5HMH8, A5HMH9, A5HMI0, A5HMI1, Q6V9W5-701413--?
phenol + NAD(P)H + H+ + O2catechol + NAD(P)+ + H2O
show the reaction diagram		Geobacillus stearothermophilus--691504--?
phenol + NAD(P)H + H+ + O2catechol + NAD(P)+ + H2O
show the reaction diagram		Acinetobacter calcoaceticus--703338--?
phenol + NAD(P)H + H+ + O2catechol + NAD(P)+ + H2O
show the reaction diagram		Trametes versicolor--704952--?
phenol + NAD(P)H + H+ + O2catechol + NAD(P)+ + H2O
show the reaction diagram		uncultured microorganism--703484--?
phenol + NAD(P)H + H+ + O2catechol + NAD(P)+ + H2O
show the reaction diagram		Comamonas sp. PND-3A7L9S9can tolerate the phenol concentration up to 1 mM, harbors the both ortho and meta fission pathways simultaneously704033--?
phenol + NAD(P)H + H+ + O2catechol + NAD(P)+ + H2O
show the reaction diagram		Pseudomonas sp. PND-1A7L9S7can tolerate the phenol concentration up to 6 mM, degrades phenol through catechol ortho fission pathway704033--?
phenol + NAD(P)H + H+ + O2catechol + NAD(P)+ + H2O
show the reaction diagram		Pseudomonas sp. PND-2A7L9S8can tolerate the phenol concentration up to 6 mM, degrades phenol through catechol ortho fission pathway704033--?
phenol + NAD(P)H + H+ + O2catechol + NAD(P)+ + H2O
show the reaction diagram		Acinetobacter sp. PND-4A5Z0R4can tolerate the phenol concentration up to 6 mM, degrades phenol through catechol ortho fission pathway704033--?
phenol + NAD(P)H + H+ + O2catechol + NAD(P)+ + H2O
show the reaction diagram		Acinetobacter sp. PND-5A5Z0R5can tolerate the phenol concentration up to 6 mM, degrades phenol through catechol ortho fission pathway704033--?
phenol + NAD(P)H + H+ + O2catechol + NAD(P)+ + H2O
show the reaction diagram		Cupriavidus sp. PND-6A7L9T0can tolerate the phenol concentration up to 6 mM, harbors the both ortho and meta fission pathways simultaneously704033--?
phenol + NAD(P)H + H+ + O2catechol + NAD(P)+ + H2O
show the reaction diagram		Rhodococcus erythropolisA7LCL0, A7LCL1hydroxylation 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 reaction701875--?
phenol + NAD(P)H + H+ + O2catechol + NAD(P)+ + H2O
show the reaction diagram		uncultured microorganismA5YUW2, A5YUW3, A5YUW6, A5YUY2, A5YUY5, A5YUY6, A5YUY7, A5YUZ3, A5YUZ5, A5YUZ6, A5YUZ7, A5YUZ8, A5YUZ9, A5YV00, A5YV01, A5YV02, A5YV03, A5YV04, A5YV05, A5YV06, A5YV08, A5YV10, A5YV11, A5YV12, A5YV13, A5YV14, A5YV15, A5YV16, A5YV18, A5YV19, A5YV20phenol degradation in the activated sludge depends on the combined activity of a number of redundant species701833--?
phenol + NADH + H+ + O2catechol + NAD+ + H2O
show the reaction diagram		Pseudomonas fluorescens--685427--?
phenol + NADH + H+ + O2catechol + NAD+ + H2O
show the reaction diagram		Pseudomonas sp.--659881--?
phenol + NADH + H+ + O2catechol + NAD+ + H2O
show the reaction diagram		Pseudomonas putida--685427--?
phenol + NADH + H+ + O2catechol + NAD+ + H2O
show the reaction diagram		Pseudomonas stutzeri--657596--?
phenol + NADH + H+ + O2catechol + NAD+ + H2O
show the reaction diagram		Pseudomonas mendocina--685427--?
phenol + NADH + H+ + O2catechol + NAD+ + H2O
show the reaction diagram		Candida tropicalis--658813--?
phenol + NADH + H+ + O2catechol + NAD+ + H2O
show the reaction diagram		Acinetobacter radioresistens--658619--?
phenol + NADH + H+ + O2catechol + NAD+ + H2O
show the reaction diagram		Pseudomonas stutzeri-coupling between phenol hydroxylase and toluene/o-xylene monooxygenase optimizes the use of nonhydroxylated aromatic molecules by the draining effect of phenol hydroxylase on the products of oxidation catalyzed by toluene/o-xylene monooxygenase, thus avoiding phenol accumulation657596--?
phenol + NADH + H+ + O2catechol + NADP+ + H2O
show the reaction diagram		Geobacillus thermoglucosidasius-the two-protein system phenol hydroxylase consists of an oxygenase (PheA1) and a flavin reductase (PheA2). PheA1 catalyzes the efficient ortho-hydroxylation of phenol to catechol when supplemented with PheA2 and FAD/NADH. PheA1 catalyzes the NADH-dependent reduction of free flavins according to a ping pong bi bi mechanism659279--?
phenol + NADPH + H+ + O2catechol + NADP+ + H2O
show the reaction diagram		Pseudomonas sp.--711022--?
phenol + NADPH + H+ + O2catechol + NADP+ + H2O
show the reaction diagram		Candida tropicalis--658813--?
phenol + NADPH + H+ + O2catechol + NADP+ + H2O
show the reaction diagram		Trichosporon cutaneum--690215, 690216--?
phenol + NADPH + H+ + O2catechol + NADP+ + H2O
show the reaction diagram		Trichosporon cutaneum-the enzyme catalyzes the conversion of phenols to their 2-diol derivatives690216--?
phenol + NADPH + H+ + O2catechol + NADP+ + H2O
show the reaction diagram		Pseudomonas sp.-monitoring the production of catechol in a continuous coupled assay with recombinant catechol 2,3-dioxygenase from Pseudomonas sp. OX1711022--?
phenol + NADPH + O2catechol + NADP+ + H2O
show the reaction diagram		Pseudomonas sp.--438790, 671532, 675732--?
phenol + NADPH + O2catechol + NADP+ + H2O
show the reaction diagram		Pseudomonas stutzeri--671421, 671422--?
phenol + NADPH + O2catechol + NADP+ + H2O
show the reaction diagram		Candida albicans--672664--?
phenol + NADPH + O2catechol + NADP+ + H2O
show the reaction diagram		Candida tropicalis--394993-394993?
phenol + NADPH + O2catechol + NADP+ + H2O
show the reaction diagram		Cupriavidus necator--438792--?
phenol + NADPH + O2catechol + NADP+ + H2O
show the reaction diagram		Comamonas testosteroni--662875--?
phenol + NADPH + O2catechol + NADP+ + H2O
show the reaction diagram		Rhodococcus sp.--438788--?
phenol + NADPH + O2catechol + NADP+ + H2O
show the reaction diagram		Trichosporon cutaneum--438777, 438779--?
phenol + NADPH + O2catechol + NADP+ + H2O
show the reaction diagram		Trichosporon cutaneum--438780-438780?
phenol + NADPH + O2catechol + NADP+ + H2O
show the reaction diagram		Trichosporon cutaneum--438782, 438783, 438786, 438789--?
phenol + NADPH + O2catechol + NADP+ + H2O
show the reaction diagram		Trichosporon cutaneum--438793-438793?
phenol + NADPH + O2catechol + NADP+ + H2O
show the reaction diagram		Trichosporon cutaneum--438801--?
phenol + NADPH + O2catechol + NADP+ + H2O
show the reaction diagram		Brevibacterium fuscum--438778--?
phenol + NADPH + O2catechol + NADP+ + H2O
show the reaction diagram		Trichosporon cutaneum-reaction mechanism438781--?
phenol + NADPH + O2catechol + NADP+ + H2O
show the reaction diagram		Acinetobacter radioresistens-cytochrome c, 2,6-dichlorophenolindophenol, potassium ferricyanide and nitro blue tetrazolium can act as electron acceptors in vitro438797---
phenol + NADPH + O2catechol + NADP+ + H2O
show the reaction diagram		Comamonas testosteroni-initial step in phenol-degrading pathway662875--?
phenol + NADPH + O2catechol + NADP+ + H2O
show the reaction diagram		Candida albicans-high phenol degradation activity in vivo in strain TL3, catabolic pathway overview672664--?
phenol + NADPH + O2?
show the reaction diagram		Rhodococcus sp.-first step of phenol degradation438788--?
phenol + NADPH + O2?
show the reaction diagram		Candida tropicalis-enzyme of phenol degradation pathway394993--?
phenol + O2?
show the reaction diagram		Alcaligenes faecalisA5HMH6, A5HMH7, A5HMH8, A5HMH9, A5HMI0, A5HMI1, Q6V9W5assay at 28°C, pH 6.8-7.0, concentration of phenol diversify from 25 mg/l to 800 mg/l701413--?
phenol + O2?
show the reaction diagram		Alcaligenes faecalisA5HMH6, A5HMH7, A5HMH8, A5HMH9, A5HMI0, A5HMI1, Q6V9W5utilize phenol as sole carbon and energy source, concentration of phenol diversify from 25 mg/l to 1000 mg/l, assay at 28°C, pH 6.8-7.0701413--?
phloroglucinol + O2 + NADPH?
show the reaction diagram		Candida tropicalis--394993--?
phloroglucinol + O2 + NADPH?
show the reaction diagram		Rhodococcus sp.--438788--?
phloroglucinol + O2 + NADPH?
show the reaction diagram		Brevibacterium fuscum--438778--?
pyrogallol + O2 + NADPH?
show the reaction diagram		Rhodococcus sp.--438788--?
quinol + NADPH + O2?
show the reaction diagram		Comamonas testosteroni-63% of the activity with phenol662875--?
quinol + O2 + NADPH1,2,4-trihydroxybenzene + NADP+ + H2O
show the reaction diagram		Candida tropicalis--394993--?
quinol + O2 + NADPH1,2,4-trihydroxybenzene + NADP+ + H2O
show the reaction diagram		Rhodococcus sp.--438788--?
quinol + O2 + NADPH1,2,4-trihydroxybenzene + NADP+ + H2O
show the reaction diagram		Trichosporon cutaneum--438777--?
resorcinol + NAD(P)H + H+ + O2? + NAD(P)+ + H2O
show the reaction diagram		Rhodococcus erythropolisA7LCL0, A7LCL1-701875--?
resorcinol + NADPH + O2?
show the reaction diagram		Candida tropicalis--394993--?
resorcinol + NADPH + O2?
show the reaction diagram		Rhodococcus sp.--438788--?
resorcinol + NADPH + O2?
show the reaction diagram		Trichosporon cutaneum--438783, 438789, 438793, 438801--?
resorcinol + NADPH + O2?
show the reaction diagram		Brevibacterium fuscum--438778--?
resorcinol + NADPH + O2?
show the reaction diagram		Trichosporon cutaneum-reaction mechanism438794--?
resorcinol + NADPH + O2?
show the reaction diagram		Comamonas testosteroni-27% of the activity with phenol662875--?
thiophenol + O2 + NADPH?
show the reaction diagram		Trichosporon cutaneum--438782--?
toluene + NADPH + O2?
show the reaction diagram		Comamonas testosteroni-28% of the activity with phenol662875--?
toluene + NADPH + O22-cresol + 3-cresol + 4-cresol + NADP+ + H2O
show the reaction diagram		Pseudomonas sp.--671532--?
toluene + NADPH + O22-cresol + 3-cresol + 4-cresol + NADP+ + H2O
show the reaction diagram		Pseudomonas stutzeri--671422--?
toluene + NADPH + O22-cresol + 3-cresol + 4-cresol + NADP+ + H2O
show the reaction diagram		Pseudomonas stutzeri-regioselectivity, overview671421--?
metol + O2 + NADPH?
show the reaction diagram		Candida tropicalis--394993--?
additional information?-Candida tropicalis-broad specificity394993---
additional information?-Trichosporon cutaneum-broad specificity, reaction results in the formation of the corresponding o-diols438777---
additional information?-Rhodococcus sp.-not: 3-nitrophenol, 4-nitrophenol438788---
additional information?-Trichosporon cutaneum-overview of possible reaction products of fluorinated phenols438795---
additional information?-Brevibacterium fuscum-not: p-hydroxyphenylacetic acid, not: 2,4-, 2,5- and 2,6-dimethylphenols, not: p-hydroxybenzoic acid438778---
additional information?-Candida tropicalis-not: salicylic acid394993---
additional information?-Brevibacterium fuscum-not: salicylic acid438778---
additional information?-Trichosporon cutaneum-first enzyme of phenol biodegradation658569---
additional information?-Acinetobacter radioresistens-no PHO activity with p-hydroxybenzoic acid, m-hydroxybenzoic acid, 2,3-dinitrophenol, 3,4-dichlorophenol, 2,4,5-trichlorophenol, 2,2'-dihydroxybiphenyl and L-Tyr658619---
additional information?-Pseudomonas sp.-phenol degradation pathway, overview675732---
additional information?-Pseudomonas stutzeri-the enzyme hydroxylates benzenes to catechols via the intermediate production of phenols671421---
additional information?-Pseudomonas sp.-the enzyme is a hydrocarbon-oxidizing multicomponent monooxygenase, important for activity is formation of a complex between the hydroxylase and a regulatory protein component672112---
additional information?-Pseudomonas sp.-the enzyme is a multicomponent phenol hydroxylase, production of dyes from indole derivatives by recombinant enzymes expressed in Escherichia coli, substrate specificities of the enzyme from strain KL28 and KL33, the products formed by the enzyme from the two strain are different, detailed overview675732---
additional information?-Trichosporon cutaneum-the enzyme hydroxylates phenol and several different toxic phenol derivatives, e.g. cresols, nitrophenols and hydroxyphenols, substrate specificity, overview690215---
additional information?-Rhodococcus erythropolisA7LCL0, A7LCL1the two-component phenol hydroxylase is completely unable to hydroxylate benzoate, 4-hydroxybenzoate, and orcinol701875---

NATURAL SUBSTRATESNATURAL PRODUCTSREACTION DIAGRAMORGANISM UNIPROT ACCESSION NO.COMMENTARY SUBSTRATELITERATURE
(Substrate)		COMMENTARY PRODUCTLITERATURE
(Product)
2-xylene + NADPH + O22,3-dimethylphenol + 3,4-dimethylphenol + NADP+ + H2O
show the reaction diagram		Pseudomonas stutzeri--671422--
benzene + NADPH + O2 + H+toluene + NADP+ + H2O
show the reaction diagram		Pseudomonas sp.--671532--
phenol + NADH + H+ + O2catechol + NAD+ + H2O
show the reaction diagram		Pseudomonas fluorescens, Pseudomonas putida, Pseudomonas mendocina--685427--
phenol + NADH + H+ + O2catechol + NAD+ + H2O
show the reaction diagram		Pseudomonas stutzeri-coupling between phenol hydroxylase and toluene/o-xylene monooxygenase optimizes the use of nonhydroxylated aromatic molecules by the draining effect of phenol hydroxylase on the products of oxidation catalyzed by toluene/o-xylene monooxygenase, thus avoiding phenol accumulation657596--
phenol + NADPH + H+ + O2catechol + NADP+ + H2O
show the reaction diagram		Pseudomonas sp.--711022--
phenol + NADPH + H+ + O2catechol + NADP+ + H2O
show the reaction diagram		Trichosporon cutaneum--690215, 690216--
phenol + NADPH + O2catechol + NADP+ + H2O
show the reaction diagram		Pseudomonas sp.--671532, 675732--
phenol + NADPH + O2catechol + NADP+ + H2O
show the reaction diagram		Pseudomonas stutzeri--671422--
phenol + NADPH + O2catechol + NADP+ + H2O
show the reaction diagram		Comamonas testosteroni-initial step in phenol-degrading pathway662875--
phenol + NADPH + O2catechol + NADP+ + H2O
show the reaction diagram		Candida albicans-high phenol degradation activity in vivo in strain TL3, catabolic pathway overview672664--
phenol + NADPH + O2?
show the reaction diagram		Rhodococcus sp.-first step of phenol degradation438788--
phenol + NADPH + O2?
show the reaction diagram		Candida tropicalis-enzyme of phenol degradation pathway394993--
toluene + NADPH + O22-cresol + 3-cresol + 4-cresol + NADP+ + H2O
show the reaction diagram		Pseudomonas sp.--671532--
toluene + NADPH + O22-cresol + 3-cresol + 4-cresol + NADP+ + H2O
show the reaction diagram		Pseudomonas stutzeri--671422--
ethynylbenzene + NADPH + O22-ethynylphenol + 2-hydroxy-6-oxo-octa-2,4-dien-7-ynoic acid + NADP+ + H2O
show the reaction diagram		Pseudomonas sp.-substrate only for phenol-grown cells671532--
additional information?-Trichosporon cutaneum-first enzyme of phenol biodegradation658569--
additional information?-Pseudomonas sp.-phenol degradation pathway, overview675732--

COFACTORORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATUREIMAGE
cytochrome P450Candida tropicalis-essential component of the enzyme system658813-
FADCandida tropicalis-activates394993 2D-image
FADTrichosporon cutaneum-1 mol FAD per mol of enzyme; flavoprotein438777 2D-image
FADTrichosporon cutaneum-2 FAD groups per enzyme molecule438779, 438780 2D-image
FADTrichosporon cutaneum--438784, 438785, 438791 2D-image
FADTrichosporon cutaneum-1 FAD per monomer438798 2D-image
FADTrichosporon cutaneum-2 FAD per dimer and 3 FAD per tetramer after removing FAD and reconstituting the apoenzyme with the cofactor438799 2D-image
FADAcinetobacter radioresistens-the reductase component PHR contains one FAD658615 2D-image
FADGeobacillus thermoglucosidasius-PheA2 uses FAD both as a substrate and as a prosthetic group, strictly dependent on, neither FMN nor riboflavin can replace FAD in this reaction. PheA2 is a a homodimer, with each subunit containing a highly fluorescent FAD prosthetic group659279 2D-image
FADRhodococcus erythropolisA7LCL0, A7LCL1; activity of the oxygenase component His6PheA1 of phenol hydroxylase is strictly dependent on FAD701875 2D-image
FMNRhodococcus erythropolisA7LCL0, A7LCL1-701875 2D-image
NAD+Candida tropicalis--658813 2D-image
NADHBrevibacterium fuscum-less active than NADPH438778 2D-image
NADHPseudomonas stutzeri-the phenol hydrolxylase component P reduces several artificial electron acceptors such as horse heart cytochrome c, 2,6-dichlorophenolindophenol, and potassium ferricyanide, with either NADH or NADPH as electron donor. NADH is preferentially used657596 2D-image
NADHAcinetobacter radioresistens--658619 2D-image
NADHGeobacillus thermoglucosidasius--659279 2D-image
NADHPseudomonas sp.--659881 2D-image
NADHPseudomonas fluorescens, Pseudomonas mendocina, Pseudomonas putida--685427 2D-image
NADHRhodococcus erythropolisA7LCL0, A7LCL1PheA2 uses NADH in order to reduce FAD, according to a random sequential kinetic mechanism701875 2D-image
NADP+Candida tropicalis--658813 2D-image
NADPHCandida tropicalis--394993 2D-image
NADPHTrichosporon cutaneum--438777, 438779, 438780, 438781, 438782, 438783, 438784, 438785, 438786, 438789, 438791, 690215, 690216 2D-image
NADPHBrevibacterium fuscum--438778 2D-image
NADPHRhodococcus sp.--438788 2D-image
NADPHPseudomonas stutzeri-the phenol hydrolxylase component P reduces several artificial electron acceptors such as horse heart cytochrome c, 2,6-dichlorophenolindophenol, and potassium ferricyanide, with either NADH or NADPH as electron donor. NADH is preferentially used657596 2D-image
NADPHPseudomonas stutzeri--671421, 671422 2D-image
NADPHPseudomonas sp.--671532, 675732 2D-image
NADPHCandida albicans--672664 2D-image
NADPHRhodococcus erythropolisA7LCL0, A7LCL1can be used instead of NADH as electron donor, using either FAD or FMN as electron acceptor, but with an affinity 5fold or 10fold lower than NADH, respectively701875 2D-image

METALS and IONS ORGANISM UNIPROT ACCESSION NO.COMMENTARY LITERATURE
AnionsTrichosporon cutaneum-effect of anions on attachment of flavin438784
Cu2+Brevibacterium fuscum-participation of Cu2+ in reaction438778
Fe2+Acinetobacter radioresistens-iron-sulfur cluster of the type 2Fe-2S438797
Fe2+Pseudomonas sp.-the enzyme contains dinuclear iron active site, structure with a Fe(II)Fe(III) oxidation state, helix E comprises part of the iron-coordinating four-helix bundle672112
Fe2+Pseudomonas sp.-PHK, the accessory component of the phenol hydroxylase, may be responsible for enhancing iron incorporation into the active site of the apo-hydroxylase711022
IronAcinetobacter radioresistens-the reductase component PHR contains one iron-sulfur cluster, whose function is electron transfer from NADH to the dinuclear iron centre of the oxygenase658615
Mg2+Rhodococcus erythropolisA7LCL0, A7LCL11 mM activates by 27%701875
Mn2+Rhodococcus erythropolisA7LCL0, A7LCL11 mM activates by 13%701875
Monovalent anionsTrichosporon cutaneum-effect on mechanism438781
additional informationTrichosporon cutaneum-does not contain heme, non-heme iron or copper438777

INHIBITORSORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
1,10-phenanthrolineTrichosporon cutaneum-slight inhibition at 0.0005 to 0.001 mM438777 2D-image
2-FluorophenolTrichosporon cutaneum-substrate inhibition438789 2D-image
3-chlorophenolTrichosporon cutaneum-substrate inhibition438789 2D-image
3-FluorophenolTrichosporon cutaneum-substrate inhibition438789 2D-image
4-ChlorophenolTrichosporon cutaneum-substrate inhibition438789 2D-image
4-FluorophenolTrichosporon cutaneum-substrate inhibition438789 2D-image
5,5'-dithiobis(2-nitrobenzoate)Trichosporon cutaneum--438779 2D-image
acetateTrichosporon cutaneum-50% inhibition at 0.123 M438784 2D-image
Ag+Rhodococcus erythropolisA7LCL0, A7LCL10.02 mM completely inhibits701875 2D-image
AgNO3Trichosporon cutaneum-0.01 mM438777 2D-image
Ammonium sulfateTrichosporon cutaneum--438777 2D-image
ascorbateTrichosporon cutaneum-52% inhibition at 50 mM438777 2D-image
azideTrichosporon cutaneum--438781 2D-image
Br-Trichosporon cutaneum-50% inhibition at 0.072 M438784 2D-image
catecholTrichosporon cutaneum-substrate inhibition438789 2D-image
Cl-Trichosporon cutaneum-90% inhibition at 0.1 M, irreversible438777 2D-image
Cl-Trichosporon cutaneum--438781 2D-image
Cl-Trichosporon cutaneum-50% inhibition at 0.022 M438784 2D-image
CN-Trichosporon cutaneum-50% inhibition at 0.004 M438784 2D-image
Co2+Rhodococcus erythropolisA7LCL0, A7LCL11 mM inhibits by 20%701875 2D-image
Copper-chelating agentsTrichosporon cutaneum-not438777-
Copper-chelating agentsBrevibacterium fuscum--438778-
Cu2+Rhodococcus erythropolisA7LCL0, A7LCL10.02 mM completely inhibits701875 2D-image
CuSO4Trichosporon cutaneum-0.01 mM438777 2D-image
dithiothreitolPseudomonas sp.-dithiothreitol acts as H2O2 generator and inhibits the oxygenase component of the enzyme, catalase protects the loss of activity438790 2D-image
ethylene glycolTrichosporon cutaneum--438784 2D-image
ethynylbenzenePseudomonas sp.-reversible, competitive inhibition at concentrations above 1 mM671532 2D-image
F-Trichosporon cutaneum-50% inhibition at 0.01 M438784 2D-image
FADRhodococcus erythropolisA7LCL0, A7LCL1with respect to the total phenol hydroxylase activity, concentrations higher than 0.01 mM inhibit the catalyzed reaction; with respect to the total phenol hydroxylase activity, concentrations higher than 0.01 mM inhibit the catalyzed reaction701875 2D-image
Fe2+Rhodococcus erythropolisA7LCL0, A7LCL11 mM inhibits by 49%701875 2D-image
Fe3+Rhodococcus erythropolisA7LCL0, A7LCL10.1 mM inhibits by 23%, 1 mM completely inhibits701875 2D-image
FeSO4Trichosporon cutaneum-0.1 mM438777 2D-image
formaldehydeTrichosporon cutaneum--438785 2D-image
GlutardialdehydeTrichosporon cutaneum--438785 2D-image
glutathioneBrevibacterium fuscum--438778 2D-image
Guanidinium chlorideTrichosporon cutaneum-70-80% inhibition at 0.1 M438777 2D-image
H2O2Trichosporon cutaneum-71% inhibition at 0.1 M438777 2D-image
HgCl2Trichosporon cutaneum-0.01 mM438777 2D-image
I-Trichosporon cutaneum-50% inhibition at 0.05 M438784 2D-image
N-ethylmaleimideRhodococcus erythropolisA7LCL0, A7LCL10.1 mM inhibits by 38%, 1 mM completely inhibits701875 2D-image
Ni2+Rhodococcus erythropolisA7LCL0, A7LCL10.1 mM inhibits by 79%, 1 mM completely inhibits701875 2D-image
NO3-Trichosporon cutaneum-50% inhibition at 0.035 M438784 2D-image
p-chloromercuribenzoateTrichosporon cutaneum-inhibition is reversed by dithiothreitol438777 2D-image
p-hydroxymercuribenzoateTrichosporon cutaneum--438779 2D-image
p-hydroxymercuribenzoateRhodococcus erythropolisA7LCL0, A7LCL10.0005 mM inhibits by 53%,0.02 mM completely inhibits the enzymic activity701875 2D-image
PeroxidaseTrichosporon cutaneum--438777-
PhenolTrichosporon cutaneum-excess phenol inhibits438785, 438793 2D-image
PhenolTrichosporon cutaneum-substrate inhibition438786, 438789 2D-image
PhenolPseudomonas fluorescens, Pseudomonas mendocina, Pseudomonas putida--685427 2D-image
PHKPseudomonas sp.-the accessory component of the phenol hydroxylase mediates inhibition of phenol hydroxylase activity, overview711022-
phosphateTrichosporon cutaneum-60-70% inhibition at 5 mM438785 2D-image
Potassium ethylxanthateBrevibacterium fuscum-1 mM438778 2D-image
pyridoxal 5'-phosphateTrichosporon cutaneum-reversible, 50% loss of activity in 2 min at 0.5 mM438785 2D-image
pyridoxamine phosphateTrichosporon cutaneum-slight438785 2D-image
resorcinolTrichosporon cutaneum-substrate inhibition438789 2D-image
SDSTrichosporon cutaneum--438777 2D-image
Sodium borohydrideTrichosporon cutaneum--438777 2D-image
Sodium diethyldithiocarbamateBrevibacterium fuscum-1 mM438778 2D-image
Sodium dithioniteTrichosporon cutaneum--438777 2D-image
trichloroacetateTrichosporon cutaneum-complete inhibition at 0.1 M438784 2D-image
Triton X-100Trichosporon cutaneum--438777 2D-image
UreaTrichosporon cutaneum-70-80% inhibition at 2 M438777 2D-image
Zn2+Rhodococcus erythropolisA7LCL0, A7LCL11 mM inhibits by 77%701875 2D-image
Mg2+Trichosporon cutaneum--438784 2D-image
additional informationAlcaligenes faecalisA5HMH6, A5HMH7, A5HMH8, A5HMH9, A5HMI0, A5HMI1, Q6V9W5strain IS-67 could not grow in medium supplemented with 1000 mg/l of phenol701413-
additional informationAcinetobacter calcoaceticus-benzoate causes transcriptional repression of phenol utilization by transcriptional inhibition of the mph operon. MphR encoding the transcriptional activator and mphN encoding the largest subunit of multi-component phenol hydroxylase in the benA mutant are significantly downregulated (about 7- and 70fold) on the basis of mRNA levels when benzoate is added to the medium703338-

ACTIVATING COMPOUNDORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
dithiothreitolTrichosporon cutaneum-20% increase of activity at 1 mM438777 2D-image
PEG 400Trichosporon cutaneum-slight increase438789 2D-image
ThiophenolTrichosporon cutaneum-binds to the enzyme and stimulates NADPH oxidation438782 2D-image
flavin reductase PheA2Geobacillus thermoglucosidasius-the two-protein system phenol hydroxylase consists of an oxygenase (PheA1) and a flavin reductase (PheA2). PheA1 shows almost no phenol hydroxylase activity when assayed at 50°C and pH 7.0 in absence of PheA2. The PheA1-mediated conversion of phenol to catechol is strongly stimulated in presence of catalytic amounts of PheA2659279-
additional informationRhodococcus erythropolisA7LCL0, A7LCL1iodoacetamide, phenylmethylsulfonyl fluoride, and EDTA, at 1 mM, do not affect the activity of the pure enzyme701875-
additional informationuncultured microorganism-following injection, dissolved oxygen increases, whereas benzene, toluene, ethylbenzene, and xylene concentrations decrease, and copies of PHE and and ring-hydroxylating toluene monooxygenase (RMO) increase indicating growth of benzene, toluene, ethylbenzene, and xylene-utilizing bacteria harboring the RMO/PHE pathway703484-

KM VALUE [mM]KM VALUE [mM] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.0031-2-CresolPseudomonas stutzeri-25°C, recombinant enzyme671421 2D-image
0.005-2-FluorophenolTrichosporon cutaneum--438783 2D-image
0.0325-2-xylenePseudomonas stutzeri-25°C, recombinant enzyme671421 2D-image
0.055-3-chlorophenolTrichosporon cutaneum--438783 2D-image
0.0018-3-cresolPseudomonas stutzeri-25°C, recombinant enzyme671421 2D-image
0.008-3-FluorophenolTrichosporon cutaneum--438783 2D-image
0.039-4-ChlorophenolTrichosporon cutaneum--438783 2D-image
0.0006-4-CresolPseudomonas stutzeri-25°C, recombinant enzyme671421 2D-image
0.017-4-FluorophenolTrichosporon cutaneum--438783 2D-image
0.025-BenzenePseudomonas stutzeri-25°C, recombinant enzyme671421 2D-image
0.012-catecholTrichosporon cutaneum--438783 2D-image
0.0134-FADRhodococcus erythropolisA7LCL0, A7LCL1-701875 2D-image
0.03779-NADHPseudomonas stutzeri-phenol hydrolxylase component P657596 2D-image
0.0533-NADHRhodococcus erythropolisA7LCL0, A7LCL1-701875 2D-image
0.03-NADPHTrichosporon cutaneum-cosubstrate 3-fluorophenol438783 2D-image
0.04-NADPHTrichosporon cutaneum-+ 2-fluorophenol438783 2D-image
0.05-NADPHTrichosporon cutaneum-+ phenol or resorcinol438783 2D-image
0.071-NADPHTrichosporon cutaneum--438777 2D-image
0.09-NADPHTrichosporon cutaneum-+ catechol438783 2D-image
0.1-NADPHTrichosporon cutaneum-+ 4-fluorophenol438783 2D-image
0.271-NADPHRhodococcus erythropolisA7LCL0, A7LCL1with FAD as electron acceptor701875 2D-image
0.5-NADPHTrichosporon cutaneum-+ 4-chlorophenol438783 2D-image
0.6-NADPHTrichosporon cutaneum-cosubstrate 3-chlorophenol438783 2D-image
0.606-NADPHRhodococcus erythropolisA7LCL0, A7LCL1with FMN as electron acceptor701875 2D-image
0.7-NADPHTrichosporon cutaneum-+ 2-chlorophenol or 3-methylphenol438783 2D-image
0.8-NADPHTrichosporon cutaneum-+ 4-methylphenol438783 2D-image
0.9-NADPHPseudomonas stutzeri-phenol hydrolxylase component P657596 2D-image
1.3-NADPHTrichosporon cutaneum-+ 2-methylphenol438783 2D-image
1.7-NADPHTrichosporon cutaneum-in the absence of a phenolic substrate438783 2D-image
0.053-O2Trichosporon cutaneum--438777 2D-image
0.0006-PhenolPseudomonas stutzeri-25°C, recombinant enzyme671421 2D-image
0.0013-PhenolPseudomonas putida-strain B PC30685427 2D-image
0.0014-PhenolPseudomonas fluorescens-strain B PC18685427 2D-image
0.0017-PhenolPseudomonas mendocina-strain PC1685427 2D-image
0.0019-PhenolPseudomonas fluorescens-strain F PC17685427 2D-image
0.0024-PhenolPseudomonas putida-strain B PC16685427 2D-image
0.003-PhenolTrichosporon cutaneum--438793 2D-image
0.005-PhenolCandida tropicalis-crude extract394993 2D-image
0.0128-PhenolPseudomonas fluorescens-strain C PC31685427 2D-image
0.0128-PhenolPseudomonas putida-strain EST1412685427 2D-image
0.0131-PhenolPseudomonas fluorescens-strain F PC20685427 2D-image
0.018-PhenolTrichosporon cutaneum--438777 2D-image
0.0214-PhenolPseudomonas fluorescens-strain C PC24685427 2D-image
0.0271-PhenolPseudomonas fluorescens-strain F P69685427 2D-image
0.61-PhenolPseudomonas stutzeri-reconstituted enzyme complex657596 2D-image
1.7-PhenolCandida albicans--672664 2D-image
0.0015-resorcinolCandida tropicalis-crude extract394993 2D-image
0.032-resorcinolTrichosporon cutaneum--438783 2D-image
0.0677-riboflavinRhodococcus erythropolisA7LCL0, A7LCL1-701875 2D-image
0.022-ToluenePseudomonas stutzeri-25°C, recombinant enzyme671421 2D-image
0.0691-FMNRhodococcus erythropolisA7LCL0, A7LCL1-701875 2D-image
additional information-additional informationTrichosporon cutaneum-Km value is 6-20times higher when phenol derivative is added before NADPH438789-
additional information-additional informationAcinetobacter radioresistens-Km values with various electron acceptors438797-
additional information-additional informationPseudomonas stutzeri-kinetics and regioselectivity, overview671421-
additional information-additional informationPseudomonas fluorescens-kinetic analysis of the enzyme from different strains, overview685427-
additional information-additional informationPseudomonas mendocina-kinetic analysis685427-
additional information-additional informationPseudomonas putida-kinetic analysis of the enzyme from different strains, overview685427-

TURNOVER NUMBER [1/s] TURNOVER NUMBER MAXIMUM[1/s] SUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.95-2-CresolPseudomonas stutzeri-25°C, recombinant enzyme671421 2D-image
0.125-2-xylenePseudomonas stutzeri-25°C, recombinant enzyme671421 2D-image
0.61-3-cresolPseudomonas stutzeri-25°C, recombinant enzyme671421 2D-image
0.77-4-CresolPseudomonas stutzeri-25°C, recombinant enzyme671421 2D-image
1980-NADHAcinetobacter radioresistens-oxygenase component PHO658619 2D-image
2.0811.5NADPHTrichosporon cutaneum-value depends on phenolic substrate438783 2D-image
0.286-PhenolPseudomonas stutzeri-reconstituted enzyme complex657596 2D-image
1.02-PhenolPseudomonas stutzeri-25°C, recombinant enzyme671421 2D-image
12-PhenolTrichosporon cutaneum--438798 2D-image
1980-PhenolAcinetobacter radioresistens-oxygenase component PHO658619 2D-image
0.15-ToluenePseudomonas stutzeri-25°C, recombinant enzyme671421 2D-image
4.513.2various phenolic substratesTrichosporon cutaneum--438783-
0.1-BenzenePseudomonas stutzeri-25°C, recombinant enzyme671421 2D-image
additional information-additional informationTrichosporon cutaneum-various phenolic substrates438795-
additional information-additional informationAcinetobacter radioresistens-with various electron acceptors438797-

kcat/KM VALUE [1/mMs-1]kcat/KM VALUE [1/mMs-1] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

Ki VALUE [mM]Ki VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
30.8-2-FluorophenolTrichosporon cutaneum--438789 2D-image
2.3-3-chlorophenolTrichosporon cutaneum--438789 2D-image
6.3-3-FluorophenolTrichosporon cutaneum--438789 2D-image
2.6-4-ChlorophenolTrichosporon cutaneum--438789 2D-image
2.3-4-FluorophenolTrichosporon cutaneum--438789 2D-image
0.5-azideTrichosporon cutaneum--438781 2D-image
12.5-catecholTrichosporon cutaneum--438789 2D-image
8.6-Cl-Trichosporon cutaneum--438781 2D-image
0.17-PhenolTrichosporon cutaneum--438786 2D-image
0.72-PhenolTrichosporon cutaneum--438789 2D-image
1.305-PhenolTrichosporon cutaneum--438793 2D-image
1.99-PhenolPseudomonas fluorescens-strain F P69685427 2D-image
2.52-PhenolPseudomonas fluorescens-strain B PC18685427 2D-image
3.44-PhenolPseudomonas fluorescens-strain F PC20685427 2D-image
3.56-PhenolPseudomonas fluorescens-strain F PC17685427 2D-image
3.84-PhenolPseudomonas putida-strain B PC16685427 2D-image
4.31-PhenolPseudomonas fluorescens-strain C PC31685427 2D-image
4.4-PhenolPseudomonas putida-strain B PC30685427 2D-image
7.44-PhenolPseudomonas fluorescens-strain C PC24685427 2D-image
7.57-PhenolPseudomonas putida-strain EST1412685427 2D-image
9.41-PhenolPseudomonas mendocina-strain PC1685427 2D-image
1.8-resorcinolTrichosporon cutaneum--438789 2D-image

IC50 VALUE [mM]IC50 VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

SPECIFIC ACTIVITY [µmol/min/mg] SPECIFIC ACTIVITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
0.083-Candida albicans-cells grown at 30°C on phenol as sole carbon source672664
0.087-Candida albicans-cells grown at 25°C on phenol as sole carbon source672664
0.32-Geobacillus thermoglucosidasius-specific activity of PheA1 in presence of PheA2659279
0.333-Trametes versicolor--704952
0.781.4Pseudomonas sp.--438790
0.84-Trichosporon cutaneum-tetrameric form438799
1.5-Trichosporon cutaneum-reconstituted tetrameric form438799
2.3-Trichosporon cutaneum-dimeric form438799
2.6-Trichosporon cutaneum-reconstituted dimeric form438799
3.4-Trichosporon cutaneum--438784
5-Trichosporon cutaneum--438795
5.4-Trichosporon cutaneum--438798
5.5-Trichosporon cutaneum--438786
6-Trichosporon cutaneum--438796
7-Trichosporon cutaneum--438798
8.3-Trichosporon cutaneum--438777
411.7-Rhodococcus erythropolisA7LCL0, A7LCL1-701875
429.5-Acinetobacter radioresistens--438797

pH OPTIMUMpH MAXIMUMORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
6.5-Trametes versicolor-complete utilization of 0.5 g/l phenol in 6 days704952
6.8-Rhodococcus erythropolisA7LCL0, A7LCL1-701875
7-Pseudomonas sp.-assay at711022
7.27.6Trichosporon cutaneum-in phosphate buffer438777
7.4-Pseudomonas sp.-assay at671532
7.5-Brevibacterium fuscum--438778
7.5-Acinetobacter radioresistens-oxygenase component PHO658619
7.68Candida tropicalis--394993
7.6-Trichosporon cutaneum--438785
7.6-Candida albicans-assay at672664
7.6-Trichosporon cutaneum-assay at690215
7.9-Rhodococcus sp.--438788
8.2-Trichosporon cutaneum-in Tris-Cl buffer438777
additional information-Trichosporon cutaneum-effect of pH on oxidative half-reaction438782
additional information-Geobacillus thermoglucosidasius-the pH-optimum of the NADH:FAD reductase activity of PheA2 is pH 6.7659279

pH RANGEpH RANGE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
6.58.5Acinetobacter radioresistens-pH 6.5: about 45% of maximal activity, pH 8.5: about 30% of maximal activity, oxygenase component PHO658619
6.87Alcaligenes faecalisA5HMH6, A5HMH7, A5HMH8, A5HMH9, A5HMI0, A5HMI1, Q6V9W5; ; ; ; ; ; assay at701413
78.7Candida tropicalis-about 50% of activity maximum at pH 7.0 and 8.7394993

TEMPERATURE OPTIMUMTEMPERATURE OPTIMUM MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
20-Rhodococcus sp.--438788
22-Pseudomonas sp.-assay at room temperature671532
24-Acinetobacter radioresistens-and a second smaller peak at 32°C658619
25-Pseudomonas stutzeri-assay at671421
25-Candida albicans-in vitro assay at672664
25-Pseudomonas sp.-assay at711022
28-Alcaligenes faecalisA5HMH6, A5HMH7, A5HMH8, A5HMH9, A5HMI0, A5HMI1, Q6V9W5; ; ; ; ; ; assay at701413
30-Candida tropicalis-enzyme from resorcinol grown cells394993
30-Candida albicans-in vivo assay at672664
40-Candida tropicalis-enzyme from phenol-induced cells394993
40-Rhodococcus erythropolisA7LCL0, A7LCL1-701875
55-Geobacillus thermoglucosidasius-phenol hydroxylase system659279

TEMPERATURE RANGE TEMPERATURE MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
1035Rhodococcus sp.-10°C: about 80% of activity maximum, 35°C: about 50% of activity maximum438788
2037Acinetobacter radioresistens-20°C: about 70% of maximal activity, 24°C: maximal activity, 30°C: about 40% of maximal activity, 32°C: about 65% of maximal activity, 37°C: about 30% of maximal activity, oxygenase component PHO658619

pI VALUEpI VALUE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
5.16-Rhodococcus erythropolisA7LCL0, A7LCL1-701875
5.2-Geobacillus thermoglucosidasius-PheA1 and PheA2, isoelectric focusing659279
5.75-Rhodococcus erythropolisA7LCL0, A7LCL1-701875
6.7-Acinetobacter radioresistens-oxygenase component PHO658619
additional information-Acinetobacter radioresistens-isoelectric point of the regulatory component PHI is 4.1658615

SOURCE TISSUE ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE SOURCE
culture condition:phenol-grown cellAcinetobacter radioresistens--658615Manually annotated by BRENDA team
culture condition:phenol-grown cellCandida tropicalis-high levels of specific activity when phenol is used as major carbon and energy source660560Manually annotated by BRENDA team
culture condition:phenol-grown cellPseudomonas sp.--671532Manually annotated by BRENDA team
culture condition:phenol-grown cellCandida albicans-optimal growth at 25-30°C672664Manually annotated by BRENDA team
culture condition:phenol-grown cellTrichosporon cutaneum--690215Manually annotated by BRENDA team
additional informationPseudomonas sp.-strain KL28 is a strain that can grow on n-alkylphenols as a carbon and energy source675732Manually annotated by BRENDA team
additional informationAlcaligenes faecalisA5HMH6, A5HMH7, A5HMH8, A5HMH9, A5HMI0, A5HMI1, Q6V9W5isolated from Alcaligenes faecalis strains from activated sludge of an industrial coking wastewater treatment plant; isolated from Alcaligenes faecalis strains from activated sludge of an industrial coking wastewater treatment plant701413Manually annotated by BRENDA team
additional informationuncultured microorganismA5YUW2, A5YUW3, A5YUW6, A5YUY2, A5YUY5, A5YUY6, A5YUY7, A5YUZ3, A5YUZ5, A5YUZ6, A5YUZ7, A5YUZ8, A5YUZ9, A5YV00, A5YV01, A5YV02, A5YV03, A5YV04, A5YV05, A5YV06, A5YV08, A5YV10, A5YV11, A5YV12, A5YV13, A5YV14, A5YV15, A5YV16, A5YV18, A5YV19, A5YV20from bacterial communities from laboratory-scale activated sludge; from bacterial communities from laboratory-scale activated sludge; from bacterial communities from laboratory-scale activated sludge; from bacterial communities from laboratory-scale activated sludge; from bacterial communities from laboratory-scale activated sludge; from bacterial communities from laboratory-scale activated sludge; from bacterial communities from laboratory-scale activated sludge; from bacterial communities from laboratory-scale activated sludge; from bacterial communities from laboratory-scale activated sludge; from bacterial communities from laboratory-scale activated sludge; from bacterial communities from laboratory-scale activated sludge; from bacterial communities from laboratory-scale activated sludge; from bacterial communities from laboratory-scale activated sludge; from bacterial communities from laboratory-scale activated sludge; from bacterial communities from laboratory-scale activated sludge; from bacterial communities from laboratory-scale activated sludge; from bacterial communities from laboratory-scale activated sludge; from bacterial communities from laboratory-scale activated sludge; from bacterial communities from laboratory-scale activated sludge; from bacterial communities from laboratory-scale activated sludge; from bacterial communities from laboratory-scale activated sludge; from bacterial communities from laboratory-scale activated sludge; from bacterial communities from laboratory-scale activated sludge; from bacterial communities from laboratory-scale activated sludge; from bacterial communities from laboratory-scale activated sludge; from bacterial communities from laboratory-scale activated sludge; from bacterial communities from laboratory-scale activated sludge; from bacterial communities from laboratory-scale activated sludge; from bacterial communities from laboratory-scale activated sludge; from bacterial communities from laboratory-scale activated sludge; from bacterial communities from laboratory-scale activated sludge701833Manually annotated by BRENDA team
additional informationuncultured microorganism-microorganisms from impacted wells from an operating gasoline station with dissolved benzene, toluene, ethylbenzene, and xylene concentrations ranging from 3128 to less than 5 microg/l703484Manually annotated by BRENDA team

LOCALIZATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY GeneOntology No. LITERATURE SOURCE
intracellularTrichosporon cutaneum--5622658569Manually annotated by BRENDA team
microsomeCandida tropicalis---658813Manually annotated by BRENDA team

PDBSCOPCATHORGANISM
1hqi, downloadSCOP (1hqi)CATH (1hqi)Pseudomonas sp. (strain CF600)
1foh, downloadSCOP (1foh)CATH (1foh)Trichosporon cutaneum
1pn0, downloadSCOP (1pn0)CATH (1pn0)Trichosporon cutaneum

MOLECULAR WEIGHT MOLECULAR WEIGHT MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
25500-Pseudomonas sp.-PHK accessory protein711022
38800-Acinetobacter radioresistens-gel filtration438797
41000-Acinetobacter radioresistens-SDS-PAGE438797
45000-Rhodococcus erythropolisA7LCL0, A7LCL1gel filtration701875
67000-Trichosporon cutaneum-SDS-PAGE438798
148000-Trichosporon cutaneum-gel filtration438777, 438779
207000-Acinetobacter radioresistens-oxygenase component PHO, gel filtration658619
236000-Rhodococcus erythropolisA7LCL0, A7LCL1gel filtration701875
238000-Rhodococcus erythropolisA7LCL0, A7LCL1non-denaturing-PAGE followed by staining with Coomassie Brilliant Blue701875
302000-Trichosporon cutaneum-gel filtration438799
additional information-Geobacillus thermoglucosidasius-PheA1 has a MW of 120000 Da as determined by gel filtration. PheA2 has a MW of 35000 Da as determined by gel filtration659279

SUBUNITS ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
?Geobacillus stearothermophilus-x * 44200, sequence analysis, monooxygenase subunit of the phenol hydroxylase (PheA1). x * 16900, sequence analysis, flavin reductase subunit of the phenol hydroxylase (PheA2)691504
dimerTrichosporon cutaneum-2 * 76000, SDS-PAGE438779
dimerTrichosporon cutaneum--438786
dimerPseudomonas sp.-SDS-PAGE shows three polypeptides with molecular masses of 13000, 39000 and 60000, gel filtration experiments are consistent with the existence of a dimer438790
dimerTrichosporon cutaneum-homodimer, each subunit consists of 3 domains438791
dimerPseudomonas sp.-2 * 10235.27, PHK accessory protein, mass spectrometry711022
hexamerAcinetobacter radioresistens-(alphabetagamma)2, 2 * 54000 + 2 * 37800 + 2 * 11600, oxygenase component PHO, SDS-PAGE658619
homodimerRhodococcus erythropolisA7LCL0, A7LCL12 * 20350, sequence analysis, 2 * 22000, SDS-PAGE, 2 * 22550, mass spectrometry701875
tetramerTrichosporon cutaneum-4 * 76000, non-denaturing PAGE, after expression in Escherichia coli438799
homotetramerRhodococcus erythropolisA7LCL0, A7LCL14 * 60720, sequence analysis, 4 * 62000, SDS-PAGE, 4 * 62078, mass spectrometry701875
additional informationAcinetobacter radioresistens-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)2658615
additional informationGeobacillus thermoglucosidasius-the oxygenase component PheA1 is a dimer: 2 * 57000, SDS-PAGE. The flavin reductase PheA2 is a dimer: 2 * 18000, SDS-PAGE659279
additional informationPseudomonas stutzeri-the enzyme is a multicomponent monooxygenase671421
additional informationPseudomonas sp.-the regulatory protein component binds in a canyon on one side of the (alpha,beta)2 enzyme dimer, contacting alpha-subunit helices A, E, and F about 12 A above the diiron core672112
additional informationPseudomonas sp.-the phenol hydroxylase complex possesses the PHL, PHN, PHO, PHM, and PHK subunits711022

POSTTRANSLATIONAL MODIFICATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

Crystallization/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
native and SeMet forms of the phenol hydroxylase in complex with its regulatory protein, hanging drop vapor diffusion method, 20°C, 0.035 mM enzyme in 10 mM MES, pH 7.1, and 10% glycerol is mixed with an equal volume of crystallization buffer containing 100 mM Tris, pH 7.0, 150 mM Na2MoO4, 5% glycerol, and 17-20% PEG 8000 (w/w), X-ray diffraction structure determination and analysis at 2.3 Å resolution, molecular replacement, Single-wavelength anomalous dispersion data for the selenomethionine derivativePseudomonas sp.-672112
complexed with FAD and phenol, hanging drop vapour diffusion methodTrichosporon cutaneum-438791
the crystal structure model of phenol hydroxylase corrected for 11 sequence errors and refined against new data to 1.7 A resolutionTrichosporon cutaneum-657449

pH STABILITYpH STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
5-Trichosporon cutaneum-stable for at least 7 days438777

TEMPERATURE STABILITYTEMPERATURE STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
4-Candida tropicalis-stable for some hours394993
60-Geobacillus thermoglucosidasius-PheA1, stable for 2 h659279
65-Geobacillus thermoglucosidasius-2 h, more than 65% of the NADH:FAD reductase activity of PheA2 is maintained659279
70-Geobacillus thermoglucosidasius-complete inactivation of Phea1 after 10 min659279
88-Geobacillus thermoglucosidasius-2 h, 15-20% of the NADH:FAD reductase activity of PheA2 is maintained659279

GENERAL STABILITYORGANISM UNIPROT ACCESSION NO.LITERATURE
dilution causes considerable loss of activity and cannot be prevented by addition of proteins such as egg or serum albumin or substances of high molecular weight such as Carbowax-4000 or polyvinylpyrrolidoneBrevibacterium fuscum-438778
partially purified enzyme loses considerable activity upon dialysis or aging, addition of boiled extract prepared from crude extract fully restores activityBrevibacterium fuscum-438778
longer exposure to ultrasound drastically reduces enzyme activityCandida tropicalis-394993
chloride destabilizesTrichosporon cutaneum-438777
phosphate stabilizesTrichosporon cutaneum-438777

ORGANIC SOLVENT ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

OXIDATION STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

STORAGE STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-70°C, no significant loss of activity of the flavin reductase component PheA2 after 4 monthsGeobacillus thermoglucosidasius-659279
-20°C, 4-6 weeks stableTrichosporon cutaneum-438777
-70°C, 6 months stableTrichosporon cutaneum-438786
anion exchanger-immobilized enzyme is stable for several months at 4°C in 0.01 M buffers at pH 7.6Trichosporon cutaneum-438780

Purification/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-Acinetobacter radioresistens-438797
oxygenase component PHOAcinetobacter radioresistens-658619
partialBrevibacterium fuscum-438778
PheA1 and PheA2 expressed in recombinant Escherichia coli BL21 pLysS cellsGeobacillus thermoglucosidasius-659279
purification of the oxygenase componentPseudomonas sp.-438790
recombinant PHK, the accessory component of the phenol hydroxylase, from Escherichia coliPseudomonas sp.-711022
on a Ni2+ column, to electrophoretic homogeneity; on a Ni2+ column, to electrophoretic homogeneityRhodococcus erythropolisA7LCL0, A7LCL1701875
-Trichosporon cutaneum-438780, 438786, 438791, 438798, 438799, 438800, 438801
90% pureTrichosporon cutaneum-438795, 438796
homogeneityTrichosporon cutaneum-438777

Cloned/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
oxygenase component PHOAcinetobacter radioresistens-658619
a 7.6 kb SalI fragment of pZC1115 containing LmPH gene subcloned to pUC19 vector, resulting in recombinant plasmid pME08. Expressed in Escherichia coli DH5alpha; a 7.6 kb SalI fragment of pZC1115 containing LmPH gene subcloned to pUC19 vector, resulting in recombinant plasmid pME08. Expressed in Escherichia coli DH5alpha; expression in Escherichia coli LE392; expression in Escherichia coli LE392; expression in Escherichia coli LE392; expression in Escherichia coli LE392; expression in Escherichia coli LE392; expression in Escherichia coli LE392Alcaligenes faecalisA5HMH6, A5HMH7, A5HMH8, A5HMH9, A5HMI0, A5HMI1, Q6V9W5701413
expression in Pseudomonas aeruginosa PAO1cComamonas testosteroni-662875
-Cupriavidus necator-438792
PheA1 and PheA2 are separately expressed in recombinant Escherichia coli BL21 pLysS cellsGeobacillus thermoglucosidasius-659279
gene pheBA, DNA and amino acid sequence determination and analysis, expression analysisPseudomonas fluorescens-685427
DNA and amino acid sequence determination and analysis, expression analysisPseudomonas mendocina-685427
gene pheBA, DNA and amino acid sequence determination and analysis, expression analysisPseudomonas putida-685427
-Pseudomonas sp.-659881
co-expression of phenol hydroxylase with the regulatory protein in Escherichia coli JM109, expression of selenomethionine-enzyme in Escherichia coli strain BL21(DE3)Pseudomonas sp.-672112
DNA and amino acid sequence determination and analysis of diverse strains and their genes encoding the enzyme, phylogenetic analysis, sequence comparisons, overviewPseudomonas sp.-671645
expression of enzyme from strain KL33 and KL28 in Escherichia coliPseudomonas sp.-675732
expression of the phenol hydroxylase gene cluster in Escherichia coli strain JM109 in the absence or presence of the phk genePseudomonas sp.-711022
co-expression with wild-type or E103 mutant toluene o-xylene monooxygenases in Escherichia coli strain JM109Pseudomonas stutzeri-671422
the enzyme is encoded in the ph operon, expression in Escherichia coli strain JM109Pseudomonas stutzeri-671421
plasmid pQE30A2 expressing His6PheA2 protein transformed into Escherichia coli M15; plasmid pQE9A1 expressing His6PheA1 protein transformed into Escherichia coli M15Rhodococcus erythropolisA7LCL0, A7LCL1701875
-Trichosporon cutaneum-438791, 438793, 438798, 438799, 438800, 438801
gene phyA, DNA and amino acid sequence determinations from different strains and analysis, expression analysis, expression of the enzymes from strains R57 and ATCC 46490 in Saccharomyces cerevisiaeTrichosporon cutaneum-690216

EXPRESSION ORGANISM UNIPROT ACCESSION NO. LITERATURE
expression of mphN encoding the largest subunit of multi-component phenol hydroxylase is reduced 70fold in the presence of both phenol and benzoate. Repression of mphN transcription is specifically released in the presence of benzoateAcinetobacter calcoaceticus-703338

ENGINEERINGORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
D54NTrichosporon cutaneum-slower reaction than wild type enzyme, higher dissociation constant for binding of phenol than wild type enzyme438800
P364STrichosporon cutaneum-only 13% of the FAD is utilized to hydroxylate the substrate phenol, when resorcinol is used as substrate, the reaction is not significantly different from the reaction of the wild type enzyme438801
R281MTrichosporon cutaneum-slower reaction than wild type enzyme, binds the FAD cofactor more weakly than wild type enzyme438800
Y298FTrichosporon cutaneum-binds phenol more weakly than wild type enzyme438800
additional informationPseudomonas stutzeri-production ToMO mutants with modified regioselectivity compared with the regioselectivity of the wild-type protein in order to alter the ability of the recombinant upper pathway to produce methylcatechol isomers from toluene and to produce 3,4-dimethylcatechol from o-xylene, the combination of ToMO mutant E103G and phenol oxidase increases the production of 4-methylcatechol from toluene and the formation of 3,4-dimethylcatechol from o-xylene, overview671422

Renatured/COMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

APPLICATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
environmental protectionCandida albicans-the enzyme is useful in degradation of industrial pollutants672664
degradationPseudomonas fluorescens, Pseudomonas mendocina, Pseudomonas putida-phenol degradation, among kinetic parameters of growth, the maximum specific growth rate significantly affects the rate of contaminant degradation and is therefore an important parameter to characterise microbes in biological reatment systems685427
additional informationAcinetobacter sp. PND-4A5Z0R4potential application of LmPH as a molecular marker for the phylogenetic analysis of phenol-degrading strains704033
additional informationAcinetobacter sp. PND-5A5Z0R5potential application of LmPH as a molecular marker for the phylogenetic analysis of phenol-degrading strains704033
industryCandida albicans-the enzyme is useful in degradation of industrial pollutants672664
additional informationComamonas sp. PND-3A7L9S9potential application of LmPH as a molecular marker for the phylogenetic analysis of phenol-degrading strains704033
additional informationCupriavidus sp. PND-6A7L9T0potential application of LmPH as a molecular marker for the phylogenetic analysis of phenol-degrading strains704033
synthesisPseudomonas sp.-the multicomponent phenol hydroxylases can be used as biocatalysts for producing dyes, e.g. indigo, and hydroxyindoles such as 7-hydroxyindole from indole and its derivatives, overview, multicomponent phenol hydroxylases may serve as potential agents for organic syntheses as well as bioremediation675732
additional informationPseudomonas sp. PND-1A7L9S7potential application of LmPH as a molecular marker for the phylogenetic analysis of phenol-degrading strains704033
additional informationPseudomonas sp. PND-2A7L9S8potential application of LmPH as a molecular marker for the phylogenetic analysis of phenol-degrading strains704033

REF. AUTHORS TITLE JOURNAL VOL. PAGES YEAR ORGANISMLINK TO PUBMEDSOURCE
394993Krug, M.; Straube, G.Degradation of phenolic compounds by the yeast Candida tropicalis HP 15. II. Some properties of the first two enzymes of the degradation pathwayJ. Basic Microbiol.26271-2811986Candida tropicalis PubMed
438777Neujahr, H.Y.; Gaal, A.Phenol hydroxylase from yeast. Purification and properties of the enzyme from Trichosporon cutaneumEur. J. Biochem.35386-4001973Trichosporon cutaneum PubMed
438778Nakagawa, H.; Takeda, Y.Phenol hydroxylaseBiochim. Biophys. Acta62423-4261962Brevibacterium fuscum PubMed
438779Neujahr, H.Y.; Gaal, A.Phenol hydroxylase from yeast. Sulfhydryl groups in phenol hydroxylase from Trichosporon cutaneumEur. J. Biochem.58351-3571975Trichosporon cutaneum PubMed
438780Kjellen, K.G.; Neujahr, H.Y.Immobilization of phenol hydroxylaseBiotechnol. Bioeng.21715-7191979Trichosporon cutaneum PubMed
438781Detmer, K.; Massey, V.Effect of monovalent anions on the mechanism of phenol hydroxylaseJ. Biol. Chem.25911265-112721984Trichosporon cutaneum PubMed
438782Detmer, K.; Massey, V.Effect of substrate and pH on the oxidative half-reaction of phenol hydroxylaseJ. Biol. Chem.2605998-60051985Trichosporon cutaneum PubMed
438783Neujahr, H.Y.; Kjellen, K.G.Phenol hydroxylase from yeast. Reaction with phenol derivativesJ. Biol. Chem.2538835-88411978Trichosporon cutaneum PubMed
438784Neujahr, H.Y.Effect of anions, chaotropes, and phenol on the attachment of flavin adenine dinucleotide to phenol hydroxylaseBiochemistry22580-5841983Trichosporon cutaneum PubMed
438785Neujahr, H.Y.; Kjellen, K.G.Phenol hydroxylase from yeast: a lysyl residue essential for binding of reduced nicotinamide adenine dinucleotide phosphateBiochemistry194967-49721980Trichosporon cutaneum PubMed
438786Selitz, T.; Neujahr, H.Y.Phenol hydroxylase from yeast. A model for phenol binding and an improved purification procedureEur. J. Biochem.170343-3491987Trichosporon cutaneum PubMed
438788Straube, G.Phenol hydroxylase from Rhodococcus sp. P 1J. Basic Microbiol.27229-2321987Rhodococcus sp. PubMed
438789Mörtberg, M.; Neujahr, H.Y.In situ and in vitro kinetics of phenol hydroxylaseBiochem. Biophys. Res. Commun.14641-461987Trichosporon cutaneum PubMed
438790Cadieux, E.; Vrajmasu, V.; Achim, C.; Powlowski, J.; Muenck, E.Biochemical, Mossbauer, and EPR studies of the diiron cluster of phenol hydroxylase from Pseudomonas sp. strain CF 600Biochemistry4110680-106912002Pseudomonas sp. PubMed
438791Enroth, C.; Neujahr, H.; Schneider, G.; Lindqvist, Y.The crystal structure of phenol hydroxylase in complex with FAD and phenol provides evidence for a concerted conformational change in the enzyme and its cofactor during catalysisStructure6605-6171998Trichosporon cutaneum PubMed
438792Hino, S.; Watanabe, K.; Takahashi, N.Phenol hydroxylase cloned from Ralstonia eutropha strain E2 exhibits novel kinetic propertiesMicrobiology1441765-17721998Cupriavidus necator-
438793Kaelin, M.; Neujahr, H.Y.; Weissmahr, R.N.; Sejlitz, T.; Joehl, R.; Fiechter, A.; Reiser, J.Phenol hydroxylase from Trichosporon cutaneum: gene cloning, sequence analysis, and functional expression in Escherichia coliJ. Bacteriol.1747112-71201992Trichosporon cutaneum PubMed
438794Maeda-Yorita, K.; Massey, V.On the reaction mechanism of phenol hydroxylase. New information obtained by correlation of fluorescence and absorbance stopped flow studiesJ. Biol. Chem.2684134-41441993Trichosporon cutaneum PubMed
438795Peelen, S.; Rietjens, I.M.C.M.; Boersma, M.G.; Vervoort, J.Conversion of phenol derivatives to hydroxylated products by phenol hydroxylase from Trichosporon cutaneum. A comparison of regioselectivity and rate of conversion with calculated molecular orbital substrate characteristicsEur. J. Biochem.227284-2911995Trichosporon cutaneum PubMed
438796Peelen, S.; Rietjens, I.M.C.M.; van Berkel, W.J.H.; van Workum, W.A.T.; Vervoort, J.Fluorine-19 NMR study on the pH-dependent regioselectivity and rate of the ortho-hydroxylation of 3-fluorophenol by phenol hydroxylase from Trichosporon cutaneum. Implications for the reaction mechanismEur. J. Biochem.218345-3531993Trichosporon cutaneum PubMed
438797Pessione, E.; Divari, S.; Griva, E.; Cavaletto, M.; Rossi, G.L.; Gilardi, G.; Giunta, C.Phenol hydroxylase from Acinetobacter radioresistens is a multicomponent enzyme. Purification and characterization of the reductase moietyEur. J. Biochem.265549-5551999Acinetobacter radioresistens PubMed
438798Waters, S.; Neujahr, H.Y.A fermentor culture for production of recombinant phenol hydroxylaseProtein Expr. Purif.5534-5401994Trichosporon cutaneum PubMed
438799Waters, S.; Neujahr, H.Y.Sources and nature of heterogeneity in recombinant phenol hydroxylase derived from the basidiomycetous soil yeast Trichosporon cutaneumBiotechnol. Appl. Biochem.25235-2421997Trichosporon cutaneum-
438800Xu, D.; Ballou, D.P.; Massey, V.Studies of the mechanism of phenol hydroxylase: mutants Tyr289Phe, Asp54Asn, and Arg281MetBiochemistry4012369-123782001Trichosporon cutaneum PubMed
438801Xu, D.; Enroth, C.; Lindqvist, Y.; Ballou, D.P.; Massey, V.Studies of the mechanism of phenol hydroxylase: Effect of mutation of proline 364 to serineBiochemistry4113627-136362002Trichosporon cutaneum PubMed
657449Enroth, C.High-resolution structure of phenol hydroxylase and correction of sequence errorsActa Crystallogr. Sect. D591597-16022003Trichosporon cutaneum PubMed
657596Cafaro, 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 enzymesAppl. Environ. Microbiol.702211-22192004Pseudomonas stutzeri PubMed
658569Alexievaa, Z.; Gerginova, M.; Zlateva, P.; Peneva, N.Comparison of growth kinetics and phenol metabolizing enzymes of Trichosporon cutaneum R57 and mutants with modified degradation abilitiesEnzyme Microb. Technol.34242-2472004Trichosporon cutaneum-
658615Griva, E.; Pessione, E.; Divari, S.; Valetti, F.; Cavaletto, M.; Rossi, G.L.; Giunta, C.Phenol hydroxylase from Acinetobacter radioresistens S13. Isolation and characterization of the regulatory componentEur. J. Biochem.2701434-14402003Acinetobacter radioresistens PubMed
658619Divari, S.; Valetti, F.; Caposio, P.; Pessione, E.; Cavaletto, M.; Griva, E.; Gribaudo, G.; Gilardi, G.; Giunta, C.The oxygenase component of phenol hydroxylase from Acinetobacter radioresistens S13Eur. J. Biochem.2702244-22532003Acinetobacter radioresistens PubMed
658813Stiborova, M.; Sucha, V.; Miksanova, M.; Paca, J.Jr.; Paca, J.Hydroxylation of phenol to catechol by Candida tropicalis: involvement of cytochrome P450Gen. Physiol. Biophys.22167-1792003Candida tropicalis PubMed
659279Kirchner, U.; Westphal, A.H.; Muller, R.; van Berkel, W.J.Phenol hydroxylase from Bacillus thermoglucosidasius A7, a two-protein component monooxygenase with a dual role for FADJ. Biol. Chem.27847545-475532003Geobacillus thermoglucosidasius PubMed
659881Jeong, J.J.; Kim, J.H.; Kim, C.K.; Hwang, I.; Lee, K.3- and 4-alkylphenol degradation pathway in Pseudomonas sp. strain KL28: genetic organization of the lap gene cluster and substrate specificities of phenol hydroxylase and catechol 2,3-dioxygenaseMicrobiology1493265-32772003Pseudomonas sp. PubMed
660560Ahuatzi-Chacon, D.; Ordorica-Morales, G.; Ruiz-Ordaz, N.; Cristiani-Urbina, E.; Juarez-Ramirez, C.; Galindez-Mayer, J.Kinetic study of phenol hydroxylase and catechol 1,2-dioxygenase biosynthesis by Candida tropicalis cells grown on different phenolic substratesWorld J. Microbiol. Biotechnol.20695-7022004Candida tropicalis-
662875Teramoto, M.; Futamata, H.; Harayama, S.; Watanabe, K.Characterization of a high-affinity phenol hydroxylase from Comamonas testosteroni R5 by gene cloning, and expression in Pseudomonas aeruginosa PAO1cMol. Gen. Genet.262552-5581999Comamonas testosteroni PubMed
671421Cafaro, V.; Notomista, E.; Capasso, P.; Di Donato, A.Regiospecificity of two multicomponent monooxygenases from Pseudomonas stutzeri OX1: molecular basis for catabolic adaptation of this microorganism to methylated aromatic compoundsAppl. Environ. Microbiol.714736-47432005Pseudomonas stutzeri PubMed
671422Cafaro, V.; Notomista, E.; Capasso, P.; Di Donato, A.Mutation of glutamic acid 103 of toluene o-xylene monooxygenase as a means to control the catabolic efficiency of a recombinant upper pathway for degradation of methylated aromatic compoundsAppl. Environ. Microbiol.714744-47502005Pseudomonas stutzeri PubMed
671532Kagle, J.; Hay, A.G.Phenylacetylene reversibly inhibits the phenol hydroxylase of Pseudomonas sp. CF600 at high concentrations but is oxidized at lower concentrationsAppl. Microbiol. Biotechnol.72306-3152006Pseudomonas sp. PubMed
671645Merimaa, M.; Heinaru, E.; Liivak, M.; Vedler, E.; Heinaru, A.Grouping of phenol hydroxylase and catechol 2,3-dioxygenase genes among phenol- and p-cresol-degrading Pseudomonas species and biotypesArch. Microbiol.186287-2962006Pseudomonas sp. PubMed
672112Sazinsky, M.H.; Dunten, P.W.; McCormick, M.S.; Didonato, A.; Lippard, S.J.X-ray structure of a hydroxylase-regulatory protein complex from a hydrocarbon-oxidizing multicomponent monooxygenase, Pseudomonas sp. OX1 phenol hydroxylaseBiochemistry4515392-154042006Pseudomonas sp. PubMed
672664Tsai, S.C.; Tsai, L.D.; Li, Y.K.An isolated Candida albicans TL3 capable of degrading phenol at large concentrationBiosci. Biotechnol. Biochem.692358-23672005Candida albicans PubMed
675732Kim, J.Y.; Kim, J.K.; Lee, S.O.; Kim, C.K.; Lee, K.Multicomponent phenol hydroxylase-catalysed formation of hydroxyindoles and dyestuffs from indole and its derivativesLett. Appl. Microbiol.41163-1682005Pseudomonas sp. PubMed
685427Viggor, S.; Heinaru, E.; Kuennapas, A.; Heinaru, A.Evaluation of different phenol hydroxylase-possessing phenol-degrading pseudomonads by kinetic parametersBiodegradation19759-7692008Pseudomonas fluorescens, Pseudomonas mendocina, Pseudomonas putida PubMed
690215Gerginova, M.; Manasiev, J.; Shivarova, N.; Alexieva, Z.Influence of various phenolic compounds on phenol hydroxylase activity of a Trichosporon cutaneum strainZ. Naturforsch. C6283-862007Trichosporon cutaneum-
690216Manasiev, J.; Gerginova, M.; Yemendzhiev, H.; Peneva, N.; Alexieva, Z.Molecular analysis of phenol-degrading microbial strainsZ. Naturforsch. C63133-1382008no activity in Escherichia coli, no activity in Lactobacillus acidophilus, Trichosporon cutaneum-
691504Omokoko, B.; Jaentges, U.K.; Zimmermann, M.; Reiss, M.; Hartmeier, W.Isolation of the phe-operon from G. stearothermophilus comprising the phenol degradative meta-pathway genes and a novel transcriptional regulatorBMC Microbiol.81972008Geobacillus stearothermophilus PubMed
701413Zhu, C.; Zhang, L.; Zhao, L.Molecular cloning, genetic organization of gene cluster encoding phenol hydroxylase and catechol 2,3-dioxygenase in Alcaligenes faecalis IS-46World J. Microbiol. Biotechnol.241687-16952008Alcaligenes faecalis-
701833Basile, L.A.; Erijman, L.Quantitative assessment of phenol hydroxylase diversity in bioreactors using a functional gene analysisAppl. Microbiol. Biotechnol.78863-8722008uncultured microorganism PubMed
701875Saa, L.; Jaureguibeitia, A.; Largo, E.; Llama, M.J.; Serra, J.L.Cloning, purification and characterization of two components of phenol hydroxylase from Rhodococcus erythropolis UPV-1Appl. Microbiol. Biotechnol.86201-2112009Rhodococcus erythropolis PubMed
703338Zhan, Y.; Yu, H.; Yan, Y.; Ping, S.; Lu, W.; Zhang, W.; Chen, M.; Lin, M.Benzoate catabolite repression of the phenol degradation in Acinetobacter calcoaceticus PHEA-2Curr. Microbiol.59368-3732009Acinetobacter calcoaceticus PubMed
703484Nebe, J.; Baldwin, B.; Kassab, R.; Nies, L.; Nakatsu, C.Quantification of aromatic oxygenase genes to evaluate enhanced bioremediation by oxygen releasing materials at a gasoline-contaminated siteEnviron. Sci. Technol.432029-20342009uncultured microorganism PubMed
704033Dong, X.; Hong, Q.; He, L.; Jiang, X.; Li, S.Characterization of phenol-degrading bacterial strains isolated from natural soilInt. Biodeter. Biodegrad.62257-2622008Acinetobacter sp. PND-4, Acinetobacter sp. PND-5, Comamonas sp. PND-3, Cupriavidus sp. PND-6, Pseudomonas sp. PND-1, Pseudomonas sp. PND-2-
704952Yemendzhiev, H.; Gerginova, M.; Krastanov, A.; Stoilova, I.; Alexieva, Z.Growth of Trametes versicolor on phenolJ. Ind. Microbiol. Biotechnol.351309-13122008Trametes versicolor PubMed
711022Izzo, V.; Leo, G.; Scognamiglio, R.; Troncone, L.; Birolo, L.; Di Donato, A.PHK from phenol hydroxylase of Pseudomonas sp. OX1. Insight into the role of an accessory protein in bacterial multicomponent monooxygenasesArch. Biochem. Biophys.50548-592011Pseudomonas sp. PubMed

LINKS TO OTHER DATABASES (specific for EC-Number 1.14.13.7)
ExplorEnz
ExPASy
KEGG
MetaCyc
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)