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3-hydroxyphenylacetate + FMNH2 + O2
3,4-hydroxyphenylacetate + FMN + H2O
-
hydroxylation rate constant is 16 per s and the product conversion ratio is 90%
-
?
4-aminophenylacetate + FMNH2 + O2
4-amino-3,5-dihydroxyphenylacetate + FMN + H2O
-
-
-
?
4-hydroxyphenylacetate + FMNH + O2
3,4-dihydroxyphenylacetate + FMN + H2O
-
-
-
?
4-hydroxyphenylacetate + NADH + H+ + O2
3,4-dihydroxyphenylacetate + NAD+ + H2O
4-hydroxyphenylacetate + NADH + O2
3,4-dihydroxyphenylacetate + NAD+ + H2O
octopamine + FMNH + O2
norepinephrine + FMN + H2O
no substrate of wild-type or mutant R263E, R263D, R263A, but substrate of mutant R263D/Y398D
-
-
?
tyramine + FMNH + O2
dopamine + FMN + H2O
no substrate of wild-type or mutant R263E, but substrate of mutants R263D and R263A
-
-
?
3-hydroxyphenylacetate + NAD(P)H + O2
3,4-hydroxyphenylacetate + NAD(P)+ + H2O
-
98% of 4-hydroxyphenylacetate activity
-
-
?
4-hydroxyphenylacetate + FADH2 + O2
3,4-dihydroxyphenylacetate + FAD + H2O
-
-
-
-
?
4-hydroxyphenylacetate + FMNH2 + O2
3,4-dihydroxyphenylacetate + FMN + H2O
-
-
-
-
?
4-hydroxyphenylacetate + NADH + H+ + O2
3,4-dihydroxyphenylacetate + NAD+ + H2O
4-hydroxyphenylacetate + NADH + O2
3,4-dihydroxyphenylacetate + NAD+ + H2O
phenylacetic acid + ?
?
-
97% of 4-hydroxyphenylacetate activity
-
-
?
additional information
?
-
4-hydroxyphenylacetate + NADH + H+ + O2
3,4-dihydroxyphenylacetate + NAD+ + H2O
-
-
-
?
4-hydroxyphenylacetate + NADH + H+ + O2
3,4-dihydroxyphenylacetate + NAD+ + H2O
substrate binding, catalytic mechanism and structure-function relationship, overview
-
-
?
4-hydroxyphenylacetate + NADH + O2
3,4-dihydroxyphenylacetate + NAD+ + H2O
-
-
-
?
4-hydroxyphenylacetate + NADH + O2
3,4-dihydroxyphenylacetate + NAD+ + H2O
-
-
-
?
4-hydroxyphenylacetate + NADH + H+ + O2
3,4-dihydroxyphenylacetate + NAD+ + H2O
-
-
-
-
?
4-hydroxyphenylacetate + NADH + H+ + O2
3,4-dihydroxyphenylacetate + NAD+ + H2O
-
HPAH is composed of two proteins: a FMN reductase C1 and an oxygenase C2, C1 catalyzes the reduction of FMN by NADH to generate reduced FMN, FMNH2, for use by C2 in the hydroxylation reaction, C1 is unique among the flavin reductases in that the substrate 4-hydroxyphenylacetate stimulates the rates of both the reduction of FMN and release of FMNH2 from the enzyme, the dissociation of FMNH2 from C1 is rate-limiting in the intermolecular transfer of FMNH2 from C1 to C2, and this process is regulated by the presence of 4-hydroxyphenylacetate , overview
-
-
?
4-hydroxyphenylacetate + NADH + H+ + O2
3,4-dihydroxyphenylacetate + NAD+ + H2O
via C2-FMNH-, and C4a-hydroperoxy-FMN and C4a-hydroxy-FMN
-
-
?
4-hydroxyphenylacetate + NADH + O2
3,4-dihydroxyphenylacetate + NAD+ + H2O
-
-
-
?
4-hydroxyphenylacetate + NADH + O2
3,4-dihydroxyphenylacetate + NAD+ + H2O
-
-
-
?
4-hydroxyphenylacetate + NADH + O2
3,4-dihydroxyphenylacetate + NAD+ + H2O
-
high substrate specificity
-
-
?
4-hydroxyphenylacetate + NADH + O2
3,4-dihydroxyphenylacetate + NAD+ + H2O
-
biodegradation of aromatic compounds
-
?
4-hydroxyphenylacetate + NADH + O2
3,4-dihydroxyphenylacetate + NAD+ + H2O
-
high substrate specificity, reduction of enzyme reductase component C1 by NADH occurs in two phases, while in the presence of HPA, the reduction of C1 by NADH occurs in a single phase requiring complex formation of C1 and 4-hydroxyphenylacetate prior to binding of NADH, C1 is specifically reduced by the pro-(S)-hydride, the reaction of reduced C1 with oxygen, the reoxidation reaction is also biphasic, consistent with reduced C1 being a mixture of fast and slow reacting species, rate constants for both phases are the same in the absence and presence of HPA, but in the presence of HPA, the equilibrium shifts toward the faster reacting species
-
-
?
4-hydroxyphenylacetate + NADH + O2
3,4-dihydroxyphenylacetate + NAD+ + H2O
-
hydroxylation occurs from the ternary complex forming the C2-C(4a)-hydroxy-FMN-3,4-dihydroxyphenylacetate complex
-
-
?
additional information
?
-
the enzyme is a two-component system consisting of a NADH-dependent FMN reductase and a monooxygenase C2, that uses reduced FMN as substrate, structure-function relationship, overview
-
-
?
additional information
?
-
-
the enzyme is a two-component system consisting of a NADH-dependent FMN reductase and a monooxygenase C2, that uses reduced FMN as substrate, structure-function relationship, overview
-
-
?
additional information
?
-
-
in the absence of 4-hydroxyphenylacetate, the rate constant for the formation of C4a-hydroperoxy-FMN is unaffected at pH 6.2-9.9. The rate constant for the following H2O2 elimination step increases with higher pH, consistent with a pKa above 9.4. In the presence of 4-hydroxyphenylacetate, the rate constants for the formation of C4a-hydroperoxy-FMN and the ensuing hydroxylation step are not significantly affected by the pH. In contrast, the following steps of C4a-hydroxy-FMN dehydration to form oxidized FMN occur through two pathways that are dependent on the pH of the reaction. One pathway, dominant at low pH, allows the detection of a C4a-hydroxy-FMN intermediate, whereas the pathway dominant at high pH produces oxidized FMN without an apparent accumulation of the intermediate. Both pathways efficiently catalyze hydroxylation without generating significant amounts of wasteful H2O2 at pH 6.2-9.9
-
-
?
additional information
?
-
in the absence of 4-hydroxyphenylacetate, the rate constant for the formation of C4a-hydroperoxy-FMN is unaffected at pH 6.2-9.9. The rate constant for the following H2O2 elimination step increases with higher pH, consistent with a pKa above 9.4. In the presence of 4-hydroxyphenylacetate, the rate constants for the formation of C4a-hydroperoxy-FMN and the ensuing hydroxylation step are not significantly affected by the pH. In contrast, the following steps of C4a-hydroxy-FMN dehydration to form oxidized FMN occur through two pathways that are dependent on the pH of the reaction. One pathway, dominant at low pH, allows the detection of a C4a-hydroxy-FMN intermediate, whereas the pathway dominant at high pH produces oxidized FMN without an apparent accumulation of the intermediate. Both pathways efficiently catalyze hydroxylation without generating significant amounts of wasteful H2O2 at pH 6.2-9.9
-
-
?
additional information
?
-
proton transfer is not the rate-limiting step in the formation of the C4a-(hydro)peroxyflavin intermediate. Residue His396 may act as an instantaneous proton provider for the proton-coupled electron transfer that occurs before the transition state of C4a-(hydro)peroxyflavin formation
-
-
?
additional information
?
-
the protonation of dioxygen by residue His396 of hte oxygenase component via a proton-coupled electron transfer mechanism is the key step in the formation of the triplet diradical complex of flavin semiquinone and the hydroperoxide radical. The complex undergoes intersystem crossing to form the open-shell singlet diradical complex before it forms the closed-shell singlet C4a-hydroperoxyflavin intermediate. The formation of C4a-hydroperoxyflavin is nearly barrierless. The enthalpy of activation for the formation of C4a-hydroperoxyflavin is only 1.4 kcal/mol and the formation is fast. Ser171 is the key residue that stabilizes C4a-hydroperoxyflavin by accepting a hydrogen bond from the H(N5) of the isoalloxazine ring. Both Ser171 and Trp112 facilitate H2O2 elimination by donating hydrogen bonds to the proximal oxygen of the hydroperoxide moiety during the proton transfer
-
-
?
additional information
?
-
wild-type shows a hydroxylation rate constant (kOH) for 4-aminophenylacetate of 0.028 per s compared to 17 per s for 4-hydroxyphenylacetate. Mutant S146A shows hydroxylation rate constants of 2.6 per s for 4-aminophenylacetate compared to 2.5 per s for 4-hydroxyphenylacetate
-
-
?
additional information
?
-
-
wild-type shows a hydroxylation rate constant (kOH) for 4-aminophenylacetate of 0.028 per s compared to 17 per s for 4-hydroxyphenylacetate. Mutant S146A shows hydroxylation rate constants of 2.6 per s for 4-aminophenylacetate compared to 2.5 per s for 4-hydroxyphenylacetate
-
-
?
additional information
?
-
-
a variety of aromatic compounds that contain a hydroxyl group in para-position can be hydroxylated. 4-hydroxyphenylacetate hydroxylase is an effector for C1 and substrate for C2
-
-
?
additional information
?
-
-
the enzyme is a two-protein system consisting of a smaller FMN reductase component C1 and a larger oxygenase component C2, C1 exists as a mixture of isoforms
-
-
?
additional information
?
-
-
the enzyme is a two-protein system consisting of a smaller FMN reductase component C1 and a larger oxygenase component C2, C1 exists as a mixture of isoforms
-
-
?
additional information
?
-
-
the enzyme is a flavin-dependent two-component monooxygenase that consists of a reductase component and an oxygenase component C2. C2 catalyzes the hydroxylation of HPA using oxygen and reduced FMN as co-substrates. All flavin-dependent monooxygenases perform oxygenation through the participation of a reactive intermediate, C4a-hydroperoxy-flavin
-
-
?
additional information
?
-
the enzyme is a flavin-dependent two-component monooxygenase that consists of a reductase component and an oxygenase component C2. C2 catalyzes the hydroxylation of HPA using oxygen and reduced FMN as co-substrates. All flavin-dependent monooxygenases perform oxygenation through the participation of a reactive intermediate, C4a-hydroperoxy-flavin
-
-
?
additional information
?
-
-
decreased accumulation of the intermediate at higher pH is due to the greater rates of C4a-hydroxy-FMN decay caused by the abolishment of substrate inhibition in the dehydration step at high pH
-
-
?
additional information
?
-
decreased accumulation of the intermediate at higher pH is due to the greater rates of C4a-hydroxy-FMN decay caused by the abolishment of substrate inhibition in the dehydration step at high pH
-
-
?
additional information
?
-
-
the enzyme utilizes the C-terminal domain of the reductase component as an autoinhibitory domain to suppress both the rate of reduction of FMN and the rate of release of FMNH2 from the reductase component
-
-
?
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4-hydroxyphenylacetate + NADH + H+ + O2
3,4-dihydroxyphenylacetate + NAD+ + H2O
-
-
-
?
4-hydroxyphenylacetate + FADH2 + O2
3,4-dihydroxyphenylacetate + FAD + H2O
-
-
-
-
?
4-hydroxyphenylacetate + FMNH2 + O2
3,4-dihydroxyphenylacetate + FMN + H2O
-
-
-
-
?
4-hydroxyphenylacetate + NADH + H+ + O2
3,4-dihydroxyphenylacetate + NAD+ + H2O
4-hydroxyphenylacetate + NADH + O2
3,4-dihydroxyphenylacetate + NAD+ + H2O
additional information
?
-
4-hydroxyphenylacetate + NADH + H+ + O2
3,4-dihydroxyphenylacetate + NAD+ + H2O
-
-
-
-
?
4-hydroxyphenylacetate + NADH + H+ + O2
3,4-dihydroxyphenylacetate + NAD+ + H2O
via C2-FMNH-, and C4a-hydroperoxy-FMN and C4a-hydroxy-FMN
-
-
?
4-hydroxyphenylacetate + NADH + O2
3,4-dihydroxyphenylacetate + NAD+ + H2O
-
high substrate specificity
-
-
?
4-hydroxyphenylacetate + NADH + O2
3,4-dihydroxyphenylacetate + NAD+ + H2O
-
biodegradation of aromatic compounds
-
?
additional information
?
-
-
the enzyme is a flavin-dependent two-component monooxygenase that consists of a reductase component and an oxygenase component C2. C2 catalyzes the hydroxylation of HPA using oxygen and reduced FMN as co-substrates. All flavin-dependent monooxygenases perform oxygenation through the participation of a reactive intermediate, C4a-hydroperoxy-flavin
-
-
?
additional information
?
-
the enzyme is a flavin-dependent two-component monooxygenase that consists of a reductase component and an oxygenase component C2. C2 catalyzes the hydroxylation of HPA using oxygen and reduced FMN as co-substrates. All flavin-dependent monooxygenases perform oxygenation through the participation of a reactive intermediate, C4a-hydroperoxy-flavin
-
-
?
additional information
?
-
-
the enzyme utilizes the C-terminal domain of the reductase component as an autoinhibitory domain to suppress both the rate of reduction of FMN and the rate of release of FMNH2 from the reductase component
-
-
?
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15 - 26
4-hydroxyphenylacetate
0.014 - 26
4-hydroxyphenylacetate
additional information
additional information
-
15
4-hydroxyphenylacetate
native C1-C2 system or complete enzyme, respectively, pH 7.5, with FAD as cosubstrate
16
4-hydroxyphenylacetate
recombinant C1-C2 system or complete enzyme, respectively, pH 7.5, with FAD as cosubstrate
25
4-hydroxyphenylacetate
native C1-C2 system or complete enzyme, respectively, pH 7.5, with FMN as cosubstrate
26
4-hydroxyphenylacetate
recombinant C1-C2 system or complete enzyme, respectively, pH 7.5, with FMN as cosubstrate
21
NADH
native C1-C2 system or complete enzyme, respectively, pH 7.5, with FMN as cosubstrate
22
NADH
native and recombinant C1-C2 system or complete enzyme, respectively, pH 7.5, with FAD as cosubstrate
28
NADH
recombinant C1-C2 system or complete enzyme, respectively, pH 7.5, with FMN as cosubstrate
0.014
4-hydroxyphenylacetate
-
apparent, with FAD
0.019
4-hydroxyphenylacetate
-
apparent, with FMN
15
4-hydroxyphenylacetate
native C1-C2 system or complete enzyme, respectively, pH 7.5, with FAD as cosubstrate
16
4-hydroxyphenylacetate
recombinant C1-C2 system or complete enzyme, respectively, pH 7.5, with FAD as cosubstrate
25
4-hydroxyphenylacetate
native C1-C2 system or complete enzyme, respectively, pH 7.5, with FMN as cosubstrate
26
4-hydroxyphenylacetate
recombinant C1-C2 system or complete enzyme, respectively, pH 7.5, with FMN as cosubstrate
0.012
NADH
-
apparent, with FMN
0.028
NADH
-
apparent, with FAD
21
NADH
native C1-C2 system or complete enzyme, respectively, pH 7.5, with FMN as cosubstrate
22
NADH
native and recombinant C1-C2 system or complete enzyme, respectively, pH 7.5, with FAD as cosubstrate
28
NADH
recombinant C1-C2 system or complete enzyme, respectively, pH 7.5, with FMN as cosubstrate
additional information
additional information
-
kinetics and thermodynamics, determination of redox potentials of FMN reductase component C1-bound FMN in presence or absence of 4-hydroxyphenylacetate, overview
-
additional information
additional information
-
transient kinetic study, overview
-
additional information
additional information
-
steady-steady kinetics, kinetics of FMN reduction, transfer from C1 to C2 component, and FMNH- release, thermodynamic data, including redox potentials, and Kd values, detailed overview
-
additional information
additional information
-
reaction kinetics of C2-FMNH with oxygen at various pH values investigated by stopped-flow and rapid quenched-flow techniques, detailed overview
-
additional information
additional information
reaction kinetics of C2-FMNH with oxygen at various pH values investigated by stopped-flow and rapid quenched-flow techniques, detailed overview
-
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?
x * 35000, C1 component, SDS-PAGE, x * 47000, C2 component, SDS-PAGE
?
x * 35000, C1 component, SDS-PAGE, x * 47000, C2 component, SDS-PAGE
dimer
-
x * 32000, small component, SDS-PAGE
tetramer
-
homotetramer, 4 * 50000, large component, SDS-PAGE
additional information
enzyme belongs to the two-protein component class of aromatic hydroxylases, component C2 is an oxygenase, the N-terminal half of the C1 reductase has the binding site for flavin and NADH, while the C-terminal half may be responsible for 4-hydroxyphenylacetate-stimulation of NADH oxidation
additional information
enzyme belongs to the two-protein component class of aromatic hydroxylases, component C2 is an oxygenase, the N-terminal half of the C1 reductase has the binding site for flavin and NADH, while the C-terminal half may be responsible for 4-hydroxyphenylacetate-stimulation of NADH oxidation
additional information
-
enzyme belongs to the two-protein component class of aromatic hydroxylases, component C2 is an oxygenase, the N-terminal half of the C1 reductase has the binding site for flavin and NADH, while the C-terminal half may be responsible for 4-hydroxyphenylacetate-stimulation of NADH oxidation
additional information
the enzyme is a two-component system consisting of a NADH-dependent FMN reductase and a monooxygenase C2, that uses reduced FMN as substrate, structure analysis, overview
additional information
-
the enzyme is a two-component system consisting of a NADH-dependent FMN reductase and a monooxygenase C2, that uses reduced FMN as substrate, structure analysis, overview
additional information
enzyme belongs to the two-protein component class of aromatic hydroxylases, component C2 is an oxygenase, the N-terminal half of the C1 reductase has the binding site for flavin and NADH, while the C-terminal half may be responsible for 4-hydroxyphenylacetate-stimulation of NADH oxidation
additional information
enzyme belongs to the two-protein component class of aromatic hydroxylases, component C2 is an oxygenase, the N-terminal half of the C1 reductase has the binding site for flavin and NADH, while the C-terminal half may be responsible for 4-hydroxyphenylacetate-stimulation of NADH oxidation
additional information
-
enzyme belongs to the two-protein component class of aromatic hydroxylases, component C2 is an oxygenase, the N-terminal half of the C1 reductase has the binding site for flavin and NADH, while the C-terminal half may be responsible for 4-hydroxyphenylacetate-stimulation of NADH oxidation
additional information
-
the enzyme is a two-protein system consisting of a smaller FMN reductase component C1 and a larger oxygenase component C2, C1 exists as a mixture of isoforms
additional information
-
the enzyme is a two-protein system consisting of a smaller FMN reductase component C1 and a larger oxygenase component C2, C1 exists as a mixture of isoforms
additional information
-
HPAH is composed of two proteins: a FMN reductase C1 and an oxygenase C2
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H120D
mutant can form C4a-hydroperoxy-FMN, a reactive intermediate necessary for hydroxylation, but cannot hydroxylate 4-hydroxyphenylacetate
H120E
mutant can form C4a-hydroperoxy-FMN, a reactive intermediate necessary for hydroxylation, but cannot hydroxylate 4-hydroxyphenylacetate
H120K
catalyzes hydroxylation with efficiency comparable to that of the wild-type enzyme, the hydroxylation rate constant for H120K is 5.7 per s and the product conversion ratio is 75%, compared to values of 16 s-1 and 90% for the wild-type enzyme
H120N
mutant can form C4a-hydroperoxy-FMN, a reactive intermediate necessary for hydroxylation, but cannot hydroxylate 4-hydroxyphenylacetate
H120Q
mutant can form C4a-hydroperoxy-FMN, a reactive intermediate necessary for hydroxylation, but cannot hydroxylate 4-hydroxyphenylacetate
H120R
mutant is able to catalyze hydroxylation
H120Y
mutant can form C4a-hydroperoxy-FMN, a reactive intermediate necessary for hydroxylation, but cannot hydroxylate 4-hydroxyphenylacetate
H396A
mutation of oxygenase component, decrease in hydroxylation efficiency. pKa value is 7.1 compared to 9.8 for wild-type
H396N
mutation of oxygenase component, decrease in hydroxylation efficiency. pKa value is 9.3 compared to 9.8 for wild-type
H396V
mutation of oxygenase component, decrease in hydroxylation efficiency. pKa value is 7.3 compared to 9.8 for wild-type
R263A
mutation of oxygenase component, 72% hydroxylation efficiency of phydroxyphenylacetate, 7% hydroxylation of tyramine
R263D
mutation of oxygenase component, variant can catalyze hydroxylation of tyramine to form dopamine with the highest yield (57%) while maintaining 86% hydroxylation efficiency of phydroxyphenylacetate
R263E
mutation of oxygenase component, 73% hydroxylation efficiency of phydroxyphenylacetate, no hydroxylation of tyramine
S146C
product formation decreases from about 65% at pH 6.0 to 27% at pH 10.0
S146A
product formation is pH-independent and constant at about 70% over a pH range of 6-10
S146A
mutation in oxygenase component C2, mutant is more effective than the wild-type in catalyzing the hydroxylation of 4-aminophenylacetate. Both variants first hydroxylate to give 3-hydroxy-4-aminophenylacetate, which is further hydroxylated to give 3,5-dihydroxy-4-aminophenylacetate
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Chaiyen, P.; Suadee, C.; Wilairat, P.
A novel two-protein component flavoprotein hydroxylase. p-Hydroxyphenylacetate hydroxylase from Acinetobacter baumannii
Eur. J. Biochem.
268
5550-5561
2001
Acinetobacter baumannii, Escherichia coli, Pseudomonas putida
brenda
Thotsaporn, K.; Sucharitakul, J.; Wongratana, J.; Suadee, C.; Chaiyen, P.
Cloning and expression of p-hydroxyphenylacetate 3-hydroxylase from Acinetobacter baumannii: evidence of the divergence of enzymes in the class of two-protein component aromatic hydroxylases
Biochim. Biophys. Acta
1680
60-66
2004
Acinetobacter baumannii (Q6Q271), Acinetobacter baumannii (Q6Q272), Acinetobacter baumannii
brenda
Sucharitakul, J.; Chaiyen, P.; Entsch, B.; Ballou, D.P.
The reductase of p-hydroxyphenylacetate 3-hydroxylase from Acinetobacter baumannii requires p-hydroxyphenylacetate for effective catalysis
Biochemistry
44
10434-10442
2005
Acinetobacter baumannii
brenda
Sucharitakul, J.; Chaiyen, P.; Entsch, B.; Ballou, D.P.
Kinetic mechanisms of the oxygenase from a two-component enzyme, p-hydroxyphenylacetate 3-hydroxylase from Acinetobacter baumannii
J. Biol. Chem.
281
17044-17053
2006
Acinetobacter baumannii
brenda
Sucharitakul, J.; Phongsak, T.; Entsch, B.; Svasti, J.; Chaiyen, P.; Ballou, D.P.
Kinetics of a two-component p-hydroxyphenylacetate hydroxylase explain how reduced flavin is transferred from the reductase to the oxygenase
Biochemistry
46
8611-8623
2007
Acinetobacter baumannii
brenda
Alfieri, A.; Fersini, F.; Ruangchan, N.; Prongjit, M.; Chaiyen, P.; Mattevi, A.
Structure of the monooxygenase component of a two-component flavoprotein monooxygenase
Proc. Natl. Acad. Sci. USA
104
1177-1182
2007
Acinetobacter baumannii (Q6Q272), Acinetobacter baumannii
brenda
Chosrowjan, H.; Taniguchi, S.; Mataga, N.; Phongsak, T.; Sucharitakul, J.; Chaiyen, P.; Tanaka, F.
Ultrafast solvation dynamics of flavin mononucleotide in the reductase component of p-hydroxyphenylacetate hydroxylase
J. Phys. Chem. B
113
8439-8442
2009
Acinetobacter baumannii
brenda
Ruangchan, N.; Tongsook, C.; Sucharitakul, J.; Chaiyen, P.
pH-Dependent studies reveal an efficient hydroxylation mechanism of the oxygenase component of p-hydroxyphenylacetate 3-hydroxylase
J. Biol. Chem.
286
223-233
2011
Acinetobacter baumannii, Acinetobacter baumannii (Q6Q272)
brenda
Tongsook, C.; Sucharitakul, J.; Thotsaporn, K.; Chaiyen, P.
Interactions with the substrate phenolic group are essential for hydroxylation by the oxygenase component of p-hydroxyphenylacetate 3-hydroxylase
J. Biol. Chem.
286
44491-44502
2011
Acinetobacter baumannii (Q6Q272)
brenda
Oonanant, W.; Sucharitakul, J.; Chaiyen, P.; Yuvaniyama, J.
Crystallization and preliminary X-ray analysis of the reductase component of p-hydroxyphenylacetate 3-hydroxylase from Acinetobacter baumannii
Acta Crystallogr. Sect. F
68
720-723
2012
Acinetobacter baumannii
brenda
Phongsak, T.; Sucharitakul, J.; Thotsaporn, K.; Oonanant, W.; Yuvaniyama, J.; Svasti, J.; Ballou, D.P.; Chaiyen, P.
The C-terminal domain of 4-hydroxyphenylacetate 3-hydroxylase from Acinetobacter baumannii is an autoinhibitory domain
J. Biol. Chem.
287
26213-26222
2012
Acinetobacter baumannii
brenda
Dhammaraj, T.; Pinthong, C.; Visitsatthawong, S.; Tongsook, C.; Surawatanawong, P.; Chaiyen, P.
A single-site mutation at Ser146 expands the reactivity of the oxygenase component of p-hydroxyphenylacetate 3-hydroxylase
ACS Chem. Biol.
11
2889-2896
2016
Acinetobacter baumannii (Q6Q272), Acinetobacter baumannii
brenda
Chenprakhon, P.; Dhammaraj, T.; Chantiwas, R.; Chaiyen, P.
Hydroxylation of 4-hydroxyphenylethylamine derivatives by R263 variants of the oxygenase component of p-hydroxyphenylacetate-3-hydroxylase
Arch. Biochem. Biophys.
620
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2017
Acinetobacter baumannii (Q6Q272), Acinetobacter baumannii
brenda
Chenprakhon, P.; Trisrivirat, D.; Thotsaporn, K.; Sucharitakul, J.; Chaiyen, P.
Control of C4a-hydroperoxyflavin protonation in the oxygenase component of p-hydroxyphenylacetate-3-hydroxylase
Biochemistry
53
4084-4086
2014
Acinetobacter baumannii (Q6Q272)
brenda
Pietra, F.
Unveiling the pathways of dioxygen through the C2 component of the environmentally relevant monooxygenase p-hydroxyphenylacetate hydroxylase from Acinetobacter baumannii A molecular dynamics investigation
Chem. Biodivers.
13
954-960
2016
Acinetobacter baumannii (Q6Q272), Acinetobacter baumannii
brenda
Visitsatthawong, S.; Chenprakhon, P.; Chaiyen, P.; Surawatanawong, P.
Mechanism of oxygen activation in a flavin-dependent monooxygenase A nearly barrierless formation of C4a-hydroperoxyflavin via proton-coupled electron transfer
J. Am. Chem. Soc.
137
9363-9374
2015
Acinetobacter baumannii (Q6Q272)
brenda