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Information on EC 1.14.16.1 - phenylalanine 4-monooxygenase and Organism(s) Chromobacterium violaceum and UniProt Accession P30967

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IUBMB Comments
The active centre contains mononuclear iron(II). The reaction involves an arene oxide that rearranges to give the phenolic hydroxy group. This results in the hydrogen at C-4 migrating to C-3 and in part being retained. This process is known as the NIH-shift. The 4a-hydroxytetrahydropteridine formed can dehydrate to 6,7-dihydropteridine, both spontaneously and by the action of EC 4.2.1.96, 4a-hydroxytetrahydrobiopterin dehydratase. The 6,7-dihydropteridine must be enzymically reduced back to tetrahydropteridine, by EC 1.5.1.34, 6,7-dihydropteridine reductase, before it slowly rearranges into the more stable but inactive compound 7,8-dihydropteridine.
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Chromobacterium violaceum
UNIPROT: P30967
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Word Map
The taxonomic range for the selected organisms is: Chromobacterium violaceum
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
phenylalanine hydroxylase, phenylalanine 4-monooxygenase, pheoh, phenylalanine 4-hydroxylase, phenylalanine monooxygenase, dicpah, cepah, l-phenylalanine 4-hydroxylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
L-phenylalanine 4-hydroxylase
-
oxygenase, phenylalanine 4-mono-
-
-
-
-
phenylalaninase
-
-
-
-
phenylalanine 4-hydroxylase
-
-
-
-
phenylalanine hydroxylase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-phenylalanine + a 5,6,7,8-tetrahydropteridine + O2 = L-tyrosine + a 4a-hydroxy-5,6,7,8-tetrahydropteridine
show the reaction diagram
sequential ter-bi mechansim, L-phenylalanine is the middle substrate in order of binding
L-phenylalanine + a 5,6,7,8-tetrahydropteridine + O2 = L-tyrosine + a 4a-hydroxy-5,6,7,8-tetrahydropteridine
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
L-phenylalanine,tetrahydrobiopterin:oxygen oxidoreductase (4-hydroxylating)
The active centre contains mononuclear iron(II). The reaction involves an arene oxide that rearranges to give the phenolic hydroxy group. This results in the hydrogen at C-4 migrating to C-3 and in part being retained. This process is known as the NIH-shift. The 4a-hydroxytetrahydropteridine formed can dehydrate to 6,7-dihydropteridine, both spontaneously and by the action of EC 4.2.1.96, 4a-hydroxytetrahydrobiopterin dehydratase. The 6,7-dihydropteridine must be enzymically reduced back to tetrahydropteridine, by EC 1.5.1.34, 6,7-dihydropteridine reductase, before it slowly rearranges into the more stable but inactive compound 7,8-dihydropteridine.
CAS REGISTRY NUMBER
COMMENTARY hide
9029-73-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-phenylalanine + 5,6,7,8-tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
show the reaction diagram
-
-
-
?
L-phenylalanine + 6,7-dimethyl-5,6,7,8-tetrahydrobiopterin + O2
L-tyrosine + 7,8-dimethyl-6,7-dihydrobiopterin + H2O
show the reaction diagram
-
-
-
?
L-phenylalanine + 6,7-dimethyl-5,6,7,8-tetrahydropterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
show the reaction diagram
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
show the reaction diagram
L-tryptophan + 5,6,7,8-tetrahydrobiopterin + O2
5-hydroxy-L-tryptophan + 4a-hydroxytetrahydrobiopterin
show the reaction diagram
the activity for L-tryptophan is extremely low compared to L-phenylalanine activity levels
-
-
?
3-phenylserine + tetrahydrobiopterin + O2
?
show the reaction diagram
-
-
-
-
?
4-methyl-L-phenylalanine + 5,6,7,8-tetrahydrobiopterin + O2
?
show the reaction diagram
-
-
-
-
?
4-methylphenylalanine + 6,7-dimethyl-tetrahydropterin + O2
4-(hydroxymethyl)phenylalanine + 3-methyltyrosine + H2O + 6,7-dimethyl-dihydropterin
show the reaction diagram
-
-
74% methyl-hydroxylation, 26% para-hydroxylation, shift of para-substituent by NIH shift mechanism
?
L-cyclohexylalanine + 6,7-dimethyl-tetrahydropterin + O2
4-hydroxy-L-cyclohexylalanine + H2O + 6,7-dimethyl-dihydropterin
show the reaction diagram
-
4times slower reaction than with L-phenylalanine
-
?
L-phenylalanine + 2-amino-4-hydroxy-6,7-dimethyltetrahydropteridine
?
show the reaction diagram
-
-
-
-
r
L-phenylalanine + 5,6,7,8-tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
show the reaction diagram
-
-
-
-
?
L-phenylalanine + 6,7-dimethyl-tetrahydrobiopterin + O2
L-tyrosine + 6,7-dimethyl-4a-hydroxy-tetrahydrobiopterin
show the reaction diagram
-
-
-
-
?
L-phenylalanine + 6,7-dimethyltetrahydropterin + O2
4-(hydroxymethyl)phenylalanine + 3-methyltyrosine + H2O + 6,7-dimethyl-dihydropterin
show the reaction diagram
-
-
-
-
?
L-phenylalanine + 6-methyltetrahydropterin + O2
L-tyrosine + 2-amino-4a-hydroxy-7-methyl-5,6,7,8-tetrahydropteridin-4(4aH)-one
show the reaction diagram
-
-
-
-
?
L-phenylalanine + 6-methyltetrahydropterin + O2
L-tyrosine + 4a-hydroxy-6-methyltetrahydropterin
show the reaction diagram
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxy-tetrahydrobiopterin
show the reaction diagram
-
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + dihydrobiopterin + H2O
show the reaction diagram
L-tryptophan + tetrahydrobiopterin + O2
?
show the reaction diagram
-
0.4% of activity with L-phenylalanine
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
show the reaction diagram
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxy-tetrahydrobiopterin
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5,6,7,8-tetrahydro-L-biopterin
-
6,7-dimethyl-5,6,7,8-tetrahydrobiopterin
-
tetrahydrobiopterin
-
5,6,7,8-tetrahydro-L-biopterin
-
-
tetrahydrobiopterin
tetrahydrofolate
additional information
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
can substitute for Fe2+, but is less efficient at higher temperature, determination of binding affinity
Zn2+
can substitute for Fe2+, but is less efficient at higher temperature, determination of binding affinity
Ca2+
-
substoichiometric amounts after removal of copper with dithiothreitol
copper
Zn2+
-
substoichiometric amounts after removal of copper with dithiothreitol
additional information
-
enzyme does not contain iron
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Bathocuproine
-
-
Co2+
-
replaced Fe2+ at the active site
diethyldithiocarbamate
-
-
o-phenanthroline
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dithiothreitol
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.035 - 0.14
5,6,7,8-tetrahydrobiopterin
0.044
6,7-dimethyl-5,6,7,8-tetrahydrobiopterin
-
0.152 - 0.262
6,7-dimethyl-5,6,7,8-tetrahydropterin
0.033 - 0.6872
L-phenylalanine
1 - 4.06
L-tryptophan
0.054
2-amino-4-hydroxy-6,7-dimethyltetrahydropteridine
-
-
0.0024
L-cyclohexylalanine
-
-
0.14
L-phenylalanine
-
-
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.2 - 0.6
5,6,7,8-tetrahydrobiopterin
3 - 6
6,7-dimethyl-5,6,7,8-tetrahydrobiopterin
-
0.18 - 21.5
L-phenylalanine
0.4 - 2.08
L-tryptophan
0.9 - 1.4
6,7-dimethyltetrahydropterin
1.6
6-methyltetrahydropterin
-
wild type enzyme, at 25°C with 50 mM HEPES (pH 7.2), 5 mM dithiothreitol
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.8 - 130
6,7-dimethyl-5,6,7,8-tetrahydropterin
0.59 - 48
L-phenylalanine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.307
mutant enzyme W180F, at 30°C, using L-phenylalanine as substrate
0.342
mutant enzyme W180F, at 30°C, using 5,6,7,8-tetrahydrobiopterin as substrate
0.347
wild type enzyme, at 30°C, using 5,6,7,8-tetrahydrobiopterin as substrate
0.69
wild type enzyme, at 30°C, using L-tryptophan as substrate
0.893
mutant enzyme W180F, at 30°C, using L-tryptophan as substrate
1.05
mutant enzyme L101Y/W180F, at 30°C, using 5,6,7,8-tetrahydrobiopterin as substrate
1.77
mutant enzyme L101Y, at 30°C, using L-tryptophan as substrate
10.16
mutant enzyme L101Y, at 30°C, using L-phenylalanine as substrate
3.37
wild type enzyme, at 30°C, using L-phenylalanine as substrate
3.62
mutant enzyme L101Y/W180F, at 30°C, using L-tryptophan as substrate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
between 7°C and 40°C, maximum activity increases exponentially with temperature, below 20°C, KM-value increases and doubles in value at 7°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
31000 - 32400
33000
-
1 * 33000, SDS-PAGE
33613
-
1 * 33613, deduced from nucleotide sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method
hanging drop vapor diffusion method, using 0.1 M Na-HEPES, pH 7.0, 0.01 M magnesium chloride hexahydrate, 0.005 M nickel(II) chloride hexahydrate, and 15% (w/v) PEG 3350, or sitting drop vapor diffusion method, using 0.1 M Na-HEPES pH 7.0, 0.01 M magnesium chloride hexahydrate, and 15% (w/v) PEG
vapor-diffusion hanging drop method at 4°C, reservoir solution contains 1 ml of 1.65-1.9 M ammonium sulfate, 40-100 mM NaCl and 20 mM HEPES pH 7.5, hanging drops are made using equal volumes of enzyme, 20 mg/ml, and reservoir solution, crystals grow in about one week, crystal structures of Fe-free apoenzyme, Fe3+-bound enzyme and Fe3+ plus 7,8-dihydro-L-biopterin-bound enzyme at 1.7 A, 2.0 A and 1.4 A resolution respectively
vapour diffusion, 1 mg enzyme dissolved in 0.1 ml 35% ammonium sulfate, 50 mM acetate, pH 6.0, 1 mM dithiothreitol, reservoir contains 60% ammonium sulfate, crystals appear after 3-4 d at 4°C
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D139A
the catalytic efficiency for L-phenylalanine is 81fold lower than that of the wild type enzyme
D139E
the catalytic efficiency for L-phenylalanine is 7fold lower than that of the wild type enzyme
D139N
the catalytic efficiency for L-phenylalanine is 17fold lower than that of the wild type enzyme
F258A
the mutant shows decreased activity and a marked decrease in the affinity for L-phenylalanine
G221A
the half-life of the mutant at 50°C is 16.8 min, which is increased by 0.9-times compared to the wild type enzyme
K94R
the half-life of the mutant at 50°C is 26.2 min, which is increased by 1.9-times compared to the wild type enzyme
K94R/G221A
the residual activity of the mutant is improved to 65.6% after keeping at 50°C for 1 h, which is 6.6 time higher than the wild type enzyme
L101A
the mutant shows 26% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
L101C
the mutant shows 47% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
L101D
the mutant shows 5% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
L101E
the mutant shows 9% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
L101F
the mutant shows 133% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
L101G
the mutant shows 20% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
L101H
the mutant shows 16% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
L101I
the mutant shows 51% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
L101K
the mutant shows 29% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
L101M
the mutant shows 102% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
L101N
the mutant shows 15% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
L101P
the mutant shows 9% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
L101Q
the mutant shows 30% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
L101R
the mutant shows 29% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
L101S
the mutant shows 28% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
L101T
the mutant shows 26% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
L101V
the mutant shows 26% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
L101W
the mutant shows 55% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
L101Y
the mutant shows 153% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
L101Y/W180F
the double mutant displays higher L-tryptophan hydroxylation activity than the wild type enzyme with a 5.2fold increase in kcat
S230P
the mutant shows strongly decreased activity and a marked decrease in the affinity for L-phenylalanine
T254A
the mutant shows decreased activity and a marked decrease in the affinity for L-phenylalanine
W180A
the mutant shows 66% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
W180C
the mutant shows 119% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
W180D
the mutant shows 3% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
W180E
the mutant shows 6% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
W180F
the mutant shows 204% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
W180G
the mutant shows 8% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
W180H
the mutant shows 73% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
W180I
the mutant shows 113% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
W180K
the mutant shows 4% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
W180L
the mutant shows 174% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
W180M
the mutant shows 166% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
W180N
the mutant shows 49% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
W180P
the mutant shows 15% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
W180Q
the mutant shows 17% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
W180R
the mutant shows 85% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
W180S
the mutant shows 46% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
W180T
the mutant shows 44% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
W180V
the mutant shows 155% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
W180Y
the mutant shows 115% relative L-tryptophan hydroxylation activity compared to the wild type enzyme
Y155A
the mutant shows decreased activity and a marked decrease in the affinity for L-phenylalanine
I234D
-
mutant shows decreased kcat value for 6,7-dimethyltetrahydropterin compared to the wild type enzyme
Y179A
-
stability and metal binding comparable to wild-type, kcat-value one order of magnitude lower than wild-type, KM-value of L-phenylalanine increases by 10-fold
Y179F
-
stability and metal binding comparable to wild-type, kcat-value one order of magnitude lower than wild-type
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
44 - 76
pH 7.4, kinetics of thermal unfolding of apo- and holo-enzymes within the temperature range and with different metal cofactors: native Fe2+, or artificial Zn2+ or Co2+, unfolding profiles, transition-state analysis shows a common mechanism for all enzyme variants, at higher temperatures the unfolding rates of Zn- and Co-PAH are affected significantly by entropy, while the unfolding rates of apo- and Fe-PAH are dominated by enthalpy even at higher temperatures, overview
50
the residual activity of the enzyme is 8.6% and the half-life is 9 min when incubated at 50°C for 1 h
47
-
50% residual activity after 66 min, presence of Fe(II), after 8 min in presence of EDTA
53
-
melting temperature of enzyme, presence of EDTA
63
-
melting temperature of enzyme, presence of Fe(II)
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 50 mM acetate, pH 6.0, 3 months, 20% loss of activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
glutathione-Sepharose column chromatography and Superdex S75 gel filtration
Ni-TED 2000 column chromatography, gel filtration
recombinant enzyme from Escherichia coli by anion exchange chromatography and gel filtration
ammonium sulfate precipitation and DEAE-Sephacel gel filtration
-
metal-free enzyme by extraction of copper with dithiothreitol
-
protamine, DEAE-Sephadex, acid, DEAE-cellulose, Ultrogel, hydroxylapatite, Blue dextran-phenyl-butylamine-Sepharose
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3)pLysS cells
gene pah, expression in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
-
expression in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fujisawa, H.; Nakata, H.
Phenylalanine 4-monooxygenase from Chromobacterium violaceum
Methods Enzymol.
142
44-49
1987
Chromobacterium violaceum
Manually annotated by BRENDA team
Pember, S.O.; Villafranca, J.J.; Benkovic, S.J.
Chromobacterium violaceum phenylalanine 4-monooxygenase
Methods Enzymol.
142
50-56
1987
Chromobacterium violaceum
Manually annotated by BRENDA team
Pember, S.O.; Villafranca, J.J.; Benkovic, S.J.
Phenylalanine hydroxylase from Chromobacterium violaceum is a copper-containing monooxygenase. Kinetics of the reductive activation of the enzyme
Biochemistry
25
6611-6619
1986
Chromobacterium violaceum
Manually annotated by BRENDA team
Nakata, H.; Yamauchi, T.; Fujisawa, H.
Phenylalanine hydroxylase from Chromobacterium violaceum. Purification and characterization
J. Biol. Chem.
254
1829-1833
1979
Chromobacterium violaceum
Manually annotated by BRENDA team
Carr, R.T.; Balasubramanian, S.; Hawkins, P.C.D.; Benkovic, S.J.
Mechanism of metal-independent hydroxylation by Chromobacterium violaceum phenylalanine hydroxylase
Biochemistry
34
7525-7532
1995
Chromobacterium violaceum, Rattus norvegicus
Manually annotated by BRENDA team
Chen, D.; Frey, P.A.
Phenylalanine hydroxylase from Chromobacterium violaceum. Uncoupled oxidation of tetrahydropterin and the role of iron in hydroxylation
J. Biol. Chem.
273
25594-25601
1998
Chromobacterium violaceum
Manually annotated by BRENDA team
Erlandsen, H.; Kim, J.Y.; Patch, M.G.; Han, A.; Volner, A.; Abu-Omar, M.M.; Stevens, R.C.
Structural comparison of bacterial and human iron-dependent phenylalanine hydroxylases: similar fold, different stability and reaction rates
J. Mol. Biol.
320
645-661
2002
Homo sapiens (P00439), Homo sapiens, Chromobacterium violaceum (P30967), Chromobacterium violaceum
Manually annotated by BRENDA team
Volner, A.; Zoidakis, J.; Abu-Omar, M.M.
Order of substrate binding in bacterial phenylalanine hydroxylase and its mechanistic implication for pterin-dependent oxygenases
J. Biol. Inorg. Chem.
8
121-128
2003
Chromobacterium violaceum (P30967), Chromobacterium violaceum
Manually annotated by BRENDA team
Zoidakis, J.; Sam, M.; Volner, A.; Han, A.; Vu, K.; Abu-Omar, M.M.
Role of the second coordination sphere residue tyrosine 179 in substrate affinity and catalytic activity of phenylalanine hydroxylase
J. Biol. Inorg. Chem.
9
289-296
2004
Chromobacterium violaceum
Manually annotated by BRENDA team
Zoidakis, J.; Loaiza, A.; Vu, K.; Abu-Omar, M.M.
Effect of temperature, pH, and metals on the stability and activity of phenylalanine hydroxylase from Chromobacterium violaceum
J. Inorg. Biochem.
99
771-775
2005
Chromobacterium violaceum
Manually annotated by BRENDA team
Han, A.Y.; Lee, A.Q.; Abu-Omar, M.M.
EPR and UV-Vis studies of the nitric oxide adducts of bacterial phenylalanine hydroxylase: effects of cofactor and substrate on the iron environment
Inorg. Chem.
45
4277-4283
2006
Chromobacterium violaceum
Manually annotated by BRENDA team
Teigen, K.; Jensen, V.R.; Martinez, A.
The reaction mechanism of phenylalanine hydroxylase. - A question of coordination
Pteridines
16
27-34
2005
Chromobacterium violaceum, Homo sapiens, Rattus norvegicus
-
Manually annotated by BRENDA team
Loaiza, A.; Armstrong, K.M.; Baker, B.M.; Abu-Omar, M.M.
Kinetics of thermal unfolding of phenylalanine hydroxylase variants containing different metal cofactors (FeII, CoII, and ZnII) and their isokinetic relationship
Inorg. Chem.
47
4877-4883
2008
Chromobacterium violaceum (P30967)
Manually annotated by BRENDA team
Panay, A.J.; Fitzpatrick, P.F.
Kinetic isotope effects on aromatic and benzylic hydroxylation by Chromobacterium violaceum phenylalanine hydroxylase as probes of chemical mechanism and reactivity
Biochemistry
47
11118-11124
2008
Chromobacterium violaceum
Manually annotated by BRENDA team
Kino, K.; Hara, R.; Nozawa, A.
Enhancement of L-tryptophan 5-hydroxylation activity by structure-based modification of L-phenylalanine 4-hydroxylase from Chromobacterium violaceum
J. Biosci. Bioeng.
108
184-189
2009
Chromobacterium violaceum (P30967), Chromobacterium violaceum, Chromobacterium violaceum NBRC 12614 (P30967)
Manually annotated by BRENDA team
Ronau, J.A.; Paul, L.N.; Fuchs, J.E.; Corn, I.R.; Wagner, K.T.; Liedl, K.R.; Abu-Omar, M.M.; Das, C.
An additional substrate binding site in a bacterial phenylalanine hydroxylase
Eur. Biophys. J.
42
691-708
2013
Chromobacterium violaceum (P30967), Chromobacterium violaceum, Chromobacterium violaceum ATCC 12472 (P30967)
Manually annotated by BRENDA team
Flydal, M.I.; Martinez, A.
Phenylalanine hydroxylase: function, structure, and regulation
IUBMB Life
65
341-349
2013
Caenorhabditis elegans, Legionella pneumophila, Homo sapiens (P00439), Homo sapiens, Rattus norvegicus (P04176), Chromobacterium violaceum (P30967), Colwellia psychrerythraea (Q47XN7), Legionella pneumophila 130b
Manually annotated by BRENDA team
Ronau, J.A.; Paul, L.N.; Fuchs, J.E.; Liedl, K.R.; Abu-Omar, M.M.; Das, C.
A conserved acidic residue in phenylalanine hydroxylase contributes to cofactor affinity and catalysis
Biochemistry
53
6834-6848
2014
Chromobacterium violaceum (P30967), Chromobacterium violaceum
Manually annotated by BRENDA team
Subedi, B.P.; Fitzpatrick, P.F.
Kinetic mechanism and intrinsic rate constants for the reaction of a bacterial phenylalanine hydroxylase
Biochemistry
55
6848-6857
2016
Chromobacterium violaceum (P30967), Chromobacterium violaceum
Manually annotated by BRENDA team
Ye, S.; Zhou, L.; Zhou, Z.
Thermal stability improvement for phenylalanine hydroxylase by site-directed mutagenesis
Chin. J. Biotechnol.
32
1243-1254
2016
Chromobacterium violaceum (P30967), Chromobacterium violaceum
Manually annotated by BRENDA team