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L-phenylalanine + 5,6,7,8-tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
-
-
?
L-phenylalanine + 6,7-dimethyl-5,6,7,8-tetrahydrobiopterin + O2
L-tyrosine + 7,8-dimethyl-6,7-dihydrobiopterin + H2O
-
-
-
?
L-phenylalanine + 6,7-dimethyl-5,6,7,8-tetrahydropterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
L-tryptophan + 5,6,7,8-tetrahydrobiopterin + O2
5-hydroxy-L-tryptophan + 4a-hydroxytetrahydrobiopterin
the activity for L-tryptophan is extremely low compared to L-phenylalanine activity levels
-
-
?
3-phenylserine + tetrahydrobiopterin + O2
?
-
-
-
-
?
4-methyl-L-phenylalanine + 5,6,7,8-tetrahydrobiopterin + O2
?
-
-
-
-
?
4-methylphenylalanine + 6,7-dimethyl-tetrahydropterin + O2
4-(hydroxymethyl)phenylalanine + 3-methyltyrosine + H2O + 6,7-dimethyl-dihydropterin
-
-
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
-
4times slower reaction than with L-phenylalanine
-
?
L-phenylalanine + 2-amino-4-hydroxy-6,7-dimethyltetrahydropteridine
?
-
-
-
-
r
L-phenylalanine + 5,6,7,8-tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
-
-
-
?
L-phenylalanine + 6,7-dimethyl-tetrahydrobiopterin + O2
L-tyrosine + 6,7-dimethyl-4a-hydroxy-tetrahydrobiopterin
-
-
-
-
?
L-phenylalanine + 6,7-dimethyltetrahydropterin + O2
4-(hydroxymethyl)phenylalanine + 3-methyltyrosine + H2O + 6,7-dimethyl-dihydropterin
-
-
-
-
?
L-phenylalanine + 6-methyltetrahydropterin + O2
L-tyrosine + 2-amino-4a-hydroxy-7-methyl-5,6,7,8-tetrahydropteridin-4(4aH)-one
-
-
-
-
?
L-phenylalanine + 6-methyltetrahydropterin + O2
L-tyrosine + 4a-hydroxy-6-methyltetrahydropterin
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxy-tetrahydrobiopterin
-
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + dihydrobiopterin + H2O
L-tryptophan + tetrahydrobiopterin + O2
?
-
0.4% of activity with L-phenylalanine
-
-
?
additional information
?
-
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
-
-
-
?
L-phenylalanine + 6-methyltetrahydropterin + O2
L-tyrosine + 4a-hydroxy-6-methyltetrahydropterin
-
-
in the presence of FeSO4 and dithiothreitol
?
L-phenylalanine + 6-methyltetrahydropterin + O2
L-tyrosine + 4a-hydroxy-6-methyltetrahydropterin
-
copper-depleted enzyme, in the absence of Fe2+, 6-methyltetrahydropterin oxidation can be uncoupled from substrate hydroxylation by the exclusion of iron
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + dihydrobiopterin + H2O
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + dihydrobiopterin + H2O
-
additional electron donors: 6-methylpterin, 6,7-dimethyltetrahydropterin
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + dihydrobiopterin + H2O
-
additional electron donors: 6-methylpterin, 6,7-dimethyltetrahydropterin
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + dihydrobiopterin + H2O
-
additional electron donors: 2-amino-4-hydroxy-6,7-dimethyltetrahydropteridine, 2-amino-4-hydroxy-6-methyltetrahydropteridine, tetrahydrofolate, and 6-methyl-5-deazatetrahydropterin
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + dihydrobiopterin + H2O
-
additional electron donors: 2-amino-4-hydroxy-6,7-dimethyltetrahydropteridine, 2-amino-4-hydroxy-6-methyltetrahydropteridine, tetrahydrofolate, and 6-methyl-5-deazatetrahydropterin
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + dihydrobiopterin + H2O
-
additional electron donors: 2-amino-4-hydroxy-6,7-dimethyltetrahydropteridine, 2-amino-4-hydroxy-6-methyltetrahydropteridine, tetrahydrofolate, and 6-methyl-5-deazatetrahydropterin
-
?
additional information
?
-
no activity against 5-deaza,6-methyltetrahydropterin
-
-
?
additional information
?
-
-
no activity against 5-deaza,6-methyltetrahydropterin
-
-
?
additional information
?
-
-
EPR and UV-Vis studies of enzyme-nitric oxide adducts, increase in NO affinity in the presence of substrate, overview
-
-
?
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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
0.054
2-amino-4-hydroxy-6,7-dimethyltetrahydropteridine
-
-
0.0024
L-cyclohexylalanine
-
-
additional information
additional information
-
0.035
5,6,7,8-tetrahydrobiopterin
mutant enzyme W180F, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)
0.086
5,6,7,8-tetrahydrobiopterin
mutant enzyme L101Y/W180F, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)
0.099
5,6,7,8-tetrahydrobiopterin
mutant enzyme L101Y, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)
0.14
5,6,7,8-tetrahydrobiopterin
wild type enzyme, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)
0.152
6,7-dimethyl-5,6,7,8-tetrahydropterin
wild type enzyme, at pH 7.4 and 20°C
0.236
6,7-dimethyl-5,6,7,8-tetrahydropterin
mutant enzyme D139N, at pH 7.4 and 20°C
0.254
6,7-dimethyl-5,6,7,8-tetrahydropterin
mutant enzyme D139N, at pH 7.4 and 20°C
0.262
6,7-dimethyl-5,6,7,8-tetrahydropterin
mutant enzyme D139N, at pH 7.4 and 20°C
0.033
L-phenylalanine
mutant enzyme W180F, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)
0.111
L-phenylalanine
wild type enzyme, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)
0.1365
L-phenylalanine
mutant enzyme Y155A, in 0.1 M Na-HEPES (pH 7.4) at 30°C
0.137
L-phenylalanine
mutant enzyme D139N, at pH 7.4 and 20°C
0.225
L-phenylalanine
mutant enzyme D139N, at pH 7.4 and 20°C
0.244
L-phenylalanine
wild type enzyme, in 0.1 M Na-HEPES (pH 7.4) at 30°C
0.244
L-phenylalanine
wild type enzyme, at pH 7.4 and 20°C
0.253
L-phenylalanine
mutant enzyme L101Y/W180F, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)
0.316
L-phenylalanine
mutant enzyme D139N, at pH 7.4 and 20°C
0.414
L-phenylalanine
mutant enzyme T254A, in 0.1 M Na-HEPES (pH 7.4) at 30°C
0.4675
L-phenylalanine
mutant enzyme F258A, in 0.1 M Na-HEPES (pH 7.4) at 30°C
0.478
L-phenylalanine
mutant enzyme L101Y, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)
0.6872
L-phenylalanine
mutant enzyme S230P, in 0.1 M Na-HEPES (pH 7.4) at 30°C
1
L-tryptophan
mutant enzyme W180F, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)
3.44
L-tryptophan
wild type enzyme, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)
3.54
L-tryptophan
mutant enzyme L101Y, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)
4.06
L-tryptophan
mutant enzyme L101Y/W180F, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)
additional information
additional information
thermodynamics, overview
-
additional information
additional information
-
thermodynamics of iron nitrosyl formation
-
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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
0.9 - 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
0.2
5,6,7,8-tetrahydrobiopterin
mutant enzyme W180F, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)
0.2
5,6,7,8-tetrahydrobiopterin
wild type enzyme, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)
0.57
5,6,7,8-tetrahydrobiopterin
mutant enzyme L101Y, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)
0.6
5,6,7,8-tetrahydrobiopterin
mutant enzyme L101Y/W180F, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)
0.18
L-phenylalanine
mutant enzyme W180F, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)
0.57
L-phenylalanine
mutant enzyme L101Y/W180F, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)
1.93
L-phenylalanine
wild type enzyme, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)
4.9
L-phenylalanine
mutant enzyme S230P, in 0.1 M Na-HEPES (pH 7.4) at 30°C
5.83
L-phenylalanine
mutant enzyme L101Y, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)
8.81
L-phenylalanine
mutant enzyme Y155A, in 0.1 M Na-HEPES (pH 7.4) at 30°C
10.9
L-phenylalanine
mutant enzyme F258A, in 0.1 M Na-HEPES (pH 7.4) at 30°C
18
L-phenylalanine
wild type enzyme, in 0.1 M Na-HEPES (pH 7.4) at 30°C
21.5
L-phenylalanine
mutant enzyme T254A, in 0.1 M Na-HEPES (pH 7.4) at 30°C
0.4
L-tryptophan
wild type enzyme, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)
0.51
L-tryptophan
mutant enzyme W180F, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)
1.02
L-tryptophan
mutant enzyme L101Y, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)
2.08
L-tryptophan
mutant enzyme L101Y/W180F, at 30°C, in 50 mM HEPES-NaOH buffer (pH 7.5)
0.9
6,7-dimethyltetrahydropterin
-
mutant enzyme I234D, at 25°C with 50 mM HEPES (pH 7.2), 5 mM dithiothreitol
1.4
6,7-dimethyltetrahydropterin
-
wild type enzyme, at 25°C with 50 mM HEPES (pH 7.2), 5 mM dithiothreitol
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0.8 - 130
6,7-dimethyl-5,6,7,8-tetrahydropterin
0.59 - 48
L-phenylalanine
0.8
6,7-dimethyl-5,6,7,8-tetrahydropterin
mutant enzyme D139N, at pH 7.4 and 20°C
5.1
6,7-dimethyl-5,6,7,8-tetrahydropterin
mutant enzyme D139N, at pH 7.4 and 20°C
9.4
6,7-dimethyl-5,6,7,8-tetrahydropterin
mutant enzyme D139N, at pH 7.4 and 20°C
130
6,7-dimethyl-5,6,7,8-tetrahydropterin
wild type enzyme, at pH 7.4 and 20°C
0.59
L-phenylalanine
mutant enzyme D139N, at pH 7.4 and 20°C
2.8
L-phenylalanine
mutant enzyme D139N, at pH 7.4 and 20°C
5.6
L-phenylalanine
mutant enzyme S230P, in 0.1 M Na-HEPES (pH 7.4) at 30°C
7.1
L-phenylalanine
mutant enzyme D139N, at pH 7.4 and 20°C
14
L-phenylalanine
mutant enzyme F258A, in 0.1 M Na-HEPES (pH 7.4) at 30°C
25
L-phenylalanine
mutant enzyme Y155A, in 0.1 M Na-HEPES (pH 7.4) at 30°C
32
L-phenylalanine
mutant enzyme T254A, in 0.1 M Na-HEPES (pH 7.4) at 30°C
48
L-phenylalanine
wild type enzyme, in 0.1 M Na-HEPES (pH 7.4) at 30°C
48
L-phenylalanine
wild type enzyme, at pH 7.4 and 20°C
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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
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Fujisawa, H.; Nakata, H.
Phenylalanine 4-monooxygenase from Chromobacterium violaceum
Methods Enzymol.
142
44-49
1987
Chromobacterium violaceum
brenda
Pember, S.O.; Villafranca, J.J.; Benkovic, S.J.
Chromobacterium violaceum phenylalanine 4-monooxygenase
Methods Enzymol.
142
50-56
1987
Chromobacterium violaceum
brenda
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
brenda
Nakata, H.; Yamauchi, T.; Fujisawa, H.
Phenylalanine hydroxylase from Chromobacterium violaceum. Purification and characterization
J. Biol. Chem.
254
1829-1833
1979
Chromobacterium violaceum
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
-
brenda
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)
brenda
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
brenda
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)
brenda
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)
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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
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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
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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
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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
brenda