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FAD + NAD(P)H
FADH2 + NAD(P)+
FAD + NADH
FADH2 + NAD+
-
-
-
r
FAD + NADH + H+
FADH2 + NAD+
FAD + NADH + H+
reduced FADH2 + NAD+
-
-
-
?
flavin + NADH + H+
reduced flavin + NAD+
FMN + NAD(P)H
FMNH2 + NAD(P)+
-
-
-
-
r
FMN + NADH + H+
FMNH2 + NAD+
FMN + NADPH
FMNH2 + NADP+
-
-
-
-
r
NADH + flavin
NAD+ + reduced flavin
reduced flavin + NAD+
flavin + NADH + H+
riboflavin + NADH
reduced riboflavin + NAD+
-
-
-
r
riboflavin + NADH + H+
reduced riboflavin + NAD+
additional information
?
-
FAD + NAD(P)H
FADH2 + NAD(P)+
-
-
-
-
r
FAD + NAD(P)H
FADH2 + NAD(P)+
-
-
-
-
?
FAD + NADH + H+
FADH2 + NAD+
-
HpaC, the small reductase component of the 4-hydroxyphenylacetate 3-monooxygenase. The reductase (HpaC) and the oxygenase component (HpaB) of the monooxygenase are encoded by two different genes. The reductase component uses NADH to catalyze the reduction of a flavin that diffuses to the oxygenase component for oxidation of the substrate by molecular oxygen. HpaC that is recombinantly overproduced in Escherichia coli K12 catalyzes the reduction of free flavins by NADH in preference to NADPH
-
-
?
FAD + NADH + H+
FADH2 + NAD+
although the HpaC enzyme can also use NADPH as a substrate, its specific activities on FMN, FAD, and riboflavin are more than 2 orders of magnitude lower than those observed in the presence of NADH. Vmax/Km is 37% compared to the value for the reaction of FMN + NADH
-
-
?
FAD + NADH + H+
FADH2 + NAD+
-
-
-
r
FAD + NADH + H+
FADH2 + NAD+
-
-
-
r
FAD + NADH + H+
FADH2 + NAD+
-
-
-
r
FAD + NADH + H+
FADH2 + NAD+
-
-
-
r
FAD + NADH + H+
FADH2 + NAD+
-
the relative activity with FAD is approximately 31% of that of FMN as the acceptor
-
-
?
FAD + NADH + H+
FADH2 + NAD+
-
the relative activity with FAD is approximately 31% of that of FMN as the acceptor
-
-
?
FAD + NADH + H+
FADH2 + NAD+
-
-
-
r
FAD + NADH + H+
FADH2 + NAD+
-
-
-
r
FAD + NADH + H+
FADH2 + NAD+
-
-
-
-
?
FAD + NADH + H+
FADH2 + NAD+
-
-
-
-
?
FAD + NADH + H+
FADH2 + NAD+
AbeF binds FAD with higher affinity than FADH2
-
-
?
FAD + NADH + H+
FADH2 + NAD+
BorF binds FAD with higher affinity than FADH2
-
-
?
FAD + NADH + H+
FADH2 + NAD+
-
-
-
?
flavin + NADH + H+
reduced flavin + NAD+
-
-
-
?
flavin + NADH + H+
reduced flavin + NAD+
-
-
-
?
flavin + NADH + H+
reduced flavin + NAD+
-
-
-
?
FMN + NADH
FMNH2 + NAD+
-
-
-
r
FMN + NADH
FMNH2 + NAD+
-
-
-
-
r
FMN + NADH
FMNH2 + NAD+
-
-
-
-
?
FMN + NADH
FMNH2 + NAD+
-
-
-
-
?
FMN + NADH + H+
FMNH2 + NAD+
-
HpaC, the small reductase component of the 4-hydroxyphenylacetate 3-monooxygenase. The reductase (HpaC) and the oxygenase component (HpaB) of the monooxygenase are encoded by two different genes. The reductase component uses NADH to catalyze the reduction of a flavin that diffuses to the oxygenase component for oxidation of the substrate by molecular oxygen. HpaC that is recombinantly overproduced in Escherichia coli K12 catalyzes the reduction of free flavins by NADH in preference to NADPH
-
-
?
FMN + NADH + H+
FMNH2 + NAD+
the most effective substrates are NADH and FMN. When FMN is added in a 200fold molar excess of the HpaC protein, it becomes completely reduced, suggesting that the flavin dissociates from the protein and behaves as a true substrate rather than as a tightly bound cofactor. Although the HpaC enzyme can also use NADPH as a substrate, its specific activities on FMN, FAD, and riboflavin are more than 2 orders of magnitude lower than those observed in the presence of NADH
-
-
?
FMN + NADH + H+
FMNH2 + NAD+
-
-
-
r
FMN + NADH + H+
FMNH2 + NAD+
-
-
-
r
FMN + NADH + H+
FMNH2 + NAD+
-
-
-
r
FMN + NADH + H+
FMNH2 + NAD+
-
-
-
r
FMN + NADH + H+
FMNH2 + NAD+
-
-
-
-
?
FMN + NADH + H+
FMNH2 + NAD+
-
-
-
-
?
FMN + NADH + H+
FMNH2 + NAD+
-
-
-
r
FMN + NADH + H+
FMNH2 + NAD+
-
-
-
r
FMN + NADH + H+
FMNH2 + NAD+
-
-
-
-
?
FMN + NADH + H+
FMNH2 + NAD+
-
-
-
?
FMN + NADH + H+
FMNH2 + NAD+
-
-
-
?
FMN + NADH + H+
FMNH2 + NAD+
-
-
-
?
NADH + flavin
NAD+ + reduced flavin
-
-
-
?
NADH + flavin
NAD+ + reduced flavin
-
-
-
?
reduced flavin + NAD+
flavin + NADH + H+
-
-
-
?
reduced flavin + NAD+
flavin + NADH + H+
-
-
-
-
?
reduced flavin + NAD+
flavin + NADH + H+
-
-
-
?
riboflavin + NADH + H+
reduced riboflavin + NAD+
-
HpaC, the small reductase component of the 4-hydroxyphenylacetate 3-monooxygenase. The reductase (HpaC) and the oxygenase component (HpaB) of the monooxygenase are encoded by two different genes. The reductase component uses NADH to catalyze the reduction of a flavin that diffuses to the oxygenase component for oxidation of the substrate by molecular oxygen. HpaC that is recombinantly overproduced in Escherichia coli K12 catalyzes the reduction of free flavins by NADH in preference to NADPH
-
-
?
riboflavin + NADH + H+
reduced riboflavin + NAD+
although the HpaC enzyme can also use NADPH as a substrate, its specific activities on FMN, FAD, and riboflavin are more than 2 orders of magnitude lower than those observed in the presence of NADH. Vmax/Km is 70% compared to the value for the reaction of FMN + NADH
-
-
?
riboflavin + NADH + H+
reduced riboflavin + NAD+
-
-
-
r
riboflavin + NADH + H+
reduced riboflavin + NAD+
-
-
-
r
riboflavin + NADH + H+
reduced riboflavin + NAD+
-
the relative activity with riboflavin is approximately 5.8% of that of FMN as the acceptor
-
-
?
riboflavin + NADH + H+
reduced riboflavin + NAD+
-
the relative activity with riboflavin is approximately 5.8% of that of FMN as the acceptor
-
-
?
riboflavin + NADH + H+
reduced riboflavin + NAD+
-
-
-
-
?
riboflavin + NADH + H+
reduced riboflavin + NAD+
-
-
-
?
riboflavin + NADH + H+
reduced riboflavin + NAD+
-
-
-
?
riboflavin + NADH + H+
reduced riboflavin + NAD+
-
-
-
?
additional information
?
-
-
the enzyme is also active with FMN and NADPH, cf. EC 1.5.1.30
-
-
?
additional information
?
-
-
the enzyme is also active with FMN and NADPH, cf. EC 1.5.1.30
-
-
?
additional information
?
-
-
the enzyme supplies reduced FADH2 for other enzymes, e.g. the 4-hydroxylphenylacetate 3-monooxygenase HpaB, which contains bound FADH2 and which protects FADH2 from being oxidized by O2, HpaC binds to HpaB without substrate channeling
-
-
?
additional information
?
-
no activity with NADPH
-
-
?
additional information
?
-
no activity with NADPH
-
-
?
additional information
?
-
-
no activity with NADPH
-
-
?
additional information
?
-
no activity with NADPH
-
-
?
additional information
?
-
no activity with NADPH
-
-
?
additional information
?
-
the reductase activity requires FMN, flavin adenine dinucleotide (FAD), or riboflavin, that give a similar activity, and is specific for NADH and not NADPH
-
-
?
additional information
?
-
-
the reductase activity requires FMN, flavin adenine dinucleotide (FAD), or riboflavin, that give a similar activity, and is specific for NADH and not NADPH
-
-
?
additional information
?
-
the reductase activity requires FMN, flavin adenine dinucleotide (FAD), or riboflavin, that give a similar activity, and is specific for NADH and not NADPH
-
-
?
additional information
?
-
-
the reductase activity requires FMN, flavin adenine dinucleotide (FAD), or riboflavin, that give a similar activity, and is specific for NADH and not NADPH
-
-
?
additional information
?
-
-
less than 0.3% of enzyme activity remains when NADPH is used as the electron donor instead of NADH
-
-
?
additional information
?
-
-
less than 0.3% of enzyme activity remains when NADPH is used as the electron donor instead of NADH
-
-
?
additional information
?
-
enzyme FerA binds FMN and FAD with comparable affinity in an enthalpically driven, entropically opposed process. The reduced flavin is bound more loosely than the oxidized one, enzyme FerA follows a random-ordered sequence of substrate, NADH and FMN, binding. The primary kinetic isotope effects from stereospecif-ically deuterated nicotinamide nucleotides demonstrate that hydride transfer occurs from the pro-S position and contributes to rate limitation for the overall reaction. Only minor structural changes around Arg106 take place upon FMN binding, role of Arg106 and His146 in binding offlavin and NADH, respectively. Riboflavin (dephosphorylated FMN) also binds to the enzyme
-
-
?
additional information
?
-
-
enzyme FerA binds FMN and FAD with comparable affinity in an enthalpically driven, entropically opposed process. The reduced flavin is bound more loosely than the oxidized one, enzyme FerA follows a random-ordered sequence of substrate, NADH and FMN, binding. The primary kinetic isotope effects from stereospecif-ically deuterated nicotinamide nucleotides demonstrate that hydride transfer occurs from the pro-S position and contributes to rate limitation for the overall reaction. Only minor structural changes around Arg106 take place upon FMN binding, role of Arg106 and His146 in binding offlavin and NADH, respectively. Riboflavin (dephosphorylated FMN) also binds to the enzyme
-
-
?
additional information
?
-
enzyme FerA binds FMN and FAD with comparable affinity in an enthalpically driven, entropically opposed process. The reduced flavin is bound more loosely than the oxidized one, enzyme FerA follows a random-ordered sequence of substrate, NADH and FMN, binding. The primary kinetic isotope effects from stereospecif-ically deuterated nicotinamide nucleotides demonstrate that hydride transfer occurs from the pro-S position and contributes to rate limitation for the overall reaction. Only minor structural changes around Arg106 take place upon FMN binding, role of Arg106 and His146 in binding offlavin and NADH, respectively. Riboflavin (dephosphorylated FMN) also binds to the enzyme
-
-
?
additional information
?
-
-
the enzyme has no measureable activity with NADPH
-
-
?
additional information
?
-
-
AbeF can reduce FAD, FMN, and riboflavin in vitro and is selective for NADH over NADPH
-
-
-
additional information
?
-
AbeF can reduce FAD, FMN, and riboflavin in vitro and is selective for NADH over NADPH
-
-
-
additional information
?
-
-
AbeF can reduce FAD, FMN, and riboflavin in vitro and is selective for NADH over NADPH. BorF proceeds by a sequential ordered kinetic mechanism in which FAD binds first. NADH does not bind BorF in the absence of FAD
-
-
-
additional information
?
-
AbeF can reduce FAD, FMN, and riboflavin in vitro and is selective for NADH over NADPH. BorF proceeds by a sequential ordered kinetic mechanism in which FAD binds first. NADH does not bind BorF in the absence of FAD
-
-
-
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0.0026 - 0.011
riboflavin
additional information
additional information
-
0.0008
FAD
-
recombinant enzyme Fre, pH 7.0, 37°C
0.003
FAD
-
recombinant enzyme HpaC, pH 7.0, 30°C
0.0031
FAD
-
pH and temperature not specified in the publication
0.0031
FAD
pH 7.8, 22°C, the value is obtained with NADH as the electron donor
0.0044
FAD
pH 7.5, 25°C, recombinant enzyme, with NADH
0.0021
FMN
-
pH and temperature not specified in the publication
0.0021
FMN
pH 7.8, 22°C, the value is obtained with NADH as the electron donor
0.0027
FMN
-
at 4°C in 50 mM Tris-Cl buffer, pH 8.0
0.0055
FMN
pH 7.5, 25°C, recombinant enzyme, with NADH
0.0066
FMN
-
purified enzyme, at pH 7.0 and 55°C
0.008
NADH
-
pH 7.2, 37°C
0.0084
NADH
-
with FMN, pH 7.5, 30°C, recombinant enzyme
0.0141
NADH
-
with FAD, pH 7.5, 30°C, recombinant enzyme
0.015
NADH
-
at 4°C in 50 mM Tris-Cl buffer, pH 8.0
0.024
NADH
pH 7.5, 25°C, recombinant enzyme, with FAD
0.04
NADH
-
pH and temperature not specified in the publication
0.04
NADH
pH 7.8, 22°C, the value is obtained with FMN as electron acceptor
0.076
NADH
-
recombinant enzyme HpaC, pH 7.0, 30°C
0.0779
NADH
-
purified enzyme, at pH 7.0 and 55°C
0.183
NADH
-
recombinant enzyme Fre, pH 7.0, 37°C
0.0026
riboflavin
-
pH and temperature not specified in the publication
0.0026
riboflavin
pH 7.8, 22°C, the value is obtained with NADH as the electron donor
0.011
riboflavin
pH 7.5, 25°C, recombinant enzyme, with NADH
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
kinetics, binding studies of HpaC and HpaB
-
additional information
additional information
bi-substrate kinetic analysis, stopped-flow kinetic measurements, detailed overview
-
additional information
additional information
-
bi-substrate kinetic analysis, stopped-flow kinetic measurements, detailed overview
-
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evolution
SMOB-ADP1 belongs to the flavin reductases of the HpaC-like subfamily. NAD(P)H:flavin oxidoreductase structure comparisons, overview
evolution
in many luminous species (i.e. Aliivibrio fischeri, Photorhabdus luminescens, and others) not only LuxG, but also Fre-like oxidoreductases are found. Probably, they are not involved in the regulation of bioluminescence in vivo except for in Photorhabdus species which lack luxG gene and apparently compensate oxidoreductase activity by Fre. Phylogenetic analysis, sequence comparisons, and reconstruction of phylogenetic tree. The enzyme belongs to the FNR superfamily. The determined specific residues can play a significant role in the division of oxidoreductases into Fre and LuxG subfamily and the mechanisms of their functioning
evolution
in many luminous species (i.e. Aliivibrio fischeri, Photorhabdus luminescens, and others) not only LuxG, but also Fre-like oxidoreductases are found. Probably, they are not involved in the regulation of bioluminescence in vivo except for in Photorhabdus species which lack luxG gene and apparently compensate oxidoreductase activity by Fre. Phylogenetic analysis, sequence comparisons, and reconstruction of phylogenetic tree. The enzyme belongs to the FNR superfamily. The determined specific residues can play a significant role in the division of oxidoreductases into Fre and LuxG subfamily and the mechanisms of their functioning
malfunction
deletion of the encoding genes genes nfr1 and nfr2 in Lactobacillus johnsonii leads to a 40fold reduction of hydrogen peroxide formation. H2O2 production in this mutant can only be restored by in trans complementation of both genes
malfunction
inhibition of Nox causes a noticeable decrease in the microsclerotium yields. Silencing of Nox decreases the microsclerotium yield by 98.5%, H2O2 and virulence decrease it by 38% and 21.5%, respectively
malfunction
-
inhibition of Nox causes a noticeable decrease in the microsclerotium yields. Silencing of Nox decreases the microsclerotium yield by 98.5%, H2O2 and virulence decrease it by 38% and 21.5%, respectively
-
malfunction
-
deletion of the encoding genes genes nfr1 and nfr2 in Lactobacillus johnsonii leads to a 40fold reduction of hydrogen peroxide formation. H2O2 production in this mutant can only be restored by in trans complementation of both genes
-
metabolism
in many luminous species (i.e. Aliivibrio fischeri, Photorhabdus luminescens, and others) not only LuxG, but also Fre-like oxidoreductases are found. LuxG enzymes are able to reduce FMN, FAD, and riboflavin with comparable efficiency, whereas for Fre oxidoreductases FAD is a preferred substrate
metabolism
in many luminous species (i.e. Aliivibrio fischeri, Photorhabdus luminescens, and others) not only LuxG, but also Fre-like oxidoreductases are found. LuxG enzymes are able to reduce FMN, FAD, and riboflavin with comparable efficiency, whereas for Fre oxidoreductases FAD is a preferred substrate
physiological function
the 4-hydroxyphenylacetate 3-monooxygenase from Escherichia coli W is a two-component enzyme encoded by the hpaB and hpaC genes and catalyzes the initial reaction in the degradation of 4-hydroxyphenylacetate, i.e., the introduction of a second hydroxyl group into the benzene nucleus at a position ortho to the existing hydroxyl group, giving rise to 3,4-dihydroxyphenylacetate
physiological function
the conserved NADH-dependent flavin reductase is prominently involved in H2O2 production in Lactobacillus johnsonii, overview
physiological function
the enzyme Nox is required for microsclerotium differentiation through regulation of intracellular H2O2 concentration. Additionally Nox has a great impact on the virulence in Nomuraea rileyi in cabbage caterpillar
physiological function
-
the enzyme Nox is required for microsclerotium differentiation through regulation of intracellular H2O2 concentration. Additionally Nox has a great impact on the virulence in Nomuraea rileyi in cabbage caterpillar
-
physiological function
-
the conserved NADH-dependent flavin reductase is prominently involved in H2O2 production in Lactobacillus johnsonii, overview
-
additional information
stabilizing effect of another Paracoccus denitrificans protein, the NAD(P)H:acceptor oxidoreducase FerB, against spontaneous oxidation of the FerA-produced dihydroflavin. The turnover rate for NADH oxidation initiated by the addition of FMN is comparable to that for the native, untagged FerA, indicating that the His tag does not interfere with catalysis. Enzyme active ite structure analysis, overview
additional information
-
stabilizing effect of another Paracoccus denitrificans protein, the NAD(P)H:acceptor oxidoreducase FerB, against spontaneous oxidation of the FerA-produced dihydroflavin. The turnover rate for NADH oxidation initiated by the addition of FMN is comparable to that for the native, untagged FerA, indicating that the His tag does not interfere with catalysis. Enzyme active ite structure analysis, overview
additional information
enzyme structure modelling and structure comparisons. The difference in affinity to flavins could be partly attributed to the absence of the Arg46 in the structure of LuxG. This residue forms a conserved Arg46-Pro47-Phe48-Ser49 segment characteristic to all Fre oxidoreductases as well as to the members of FNR family, but not to LuxG oxidoreductases
additional information
enzyme structure modelling and structure comparisons. The difference in affinity to flavins could be partly attributed to the absence of the Arg46 in the structure of LuxG. This residue forms a conserved Arg46-Pro47-Phe48-Ser49 segment characteristic to all Fre oxidoreductases as well as to the members of FNR family, but not to LuxG oxidoreductases
additional information
enzyme structure modelling and structure comparisons. The difference in affinity to flavins could be partly attributed to the absence of the Arg46 in the structure of LuxG. This residue forms a conserved Arg46-Pro47-Phe48-Ser49 segment characteristic to all Fre oxidoreductases as well as to the members of FNR family, but not to LuxG oxidoreductases
additional information
-
His160 and Arg38 contribute to the catalytic activity and the pH dependence
additional information
His160 and Arg38 contribute to the catalytic activity and the pH dependence
additional information
-
stabilizing effect of another Paracoccus denitrificans protein, the NAD(P)H:acceptor oxidoreducase FerB, against spontaneous oxidation of the FerA-produced dihydroflavin. The turnover rate for NADH oxidation initiated by the addition of FMN is comparable to that for the native, untagged FerA, indicating that the His tag does not interfere with catalysis. Enzyme active ite structure analysis, overview
-
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?
x * 58500, SDS-PAGE, recombinant protein
?
-
x * 58500, SDS-PAGE, recombinant protein
-
?
-
x * 18000, SDS-PAGE
-
?
x * 44810, sequence calculation
?
-
x * 44810, sequence calculation
-
?
x * 19936.4, recombinant enzyme, mass spectrometry, x * 20000, recombinant enzyme, SDS-PAGE, x * 20080.8, sequence calculation
?
-
x * 19936.4, recombinant enzyme, mass spectrometry, x * 20000, recombinant enzyme, SDS-PAGE, x * 20080.8, sequence calculation
-
?
-
x * 19400, calculated from amino acid sequence
dimer
-
2 * 18600, HpaC, the recombinant small component of the 4-hydroxyphenylacetate 3-monooxygenase is a homodimer, calculated from sequence
dimer
-
2 * 20000, HpaC, the recombinant small component of the 4-hydroxyphenylacetate 3-monooxygenase is a homodimer, SDS-PAGE
dimer
2 * 18679, calculated from sequence
dimer
2 * 20000, SDS-PAGE
dimer
-
2 * 20000, SDS-PAGE
-
homodimer
2 * 22665, His10-tagged enzyme, sequence calculation, 2 * 20000-25000, recombinant His10-tagged enzyme, SDS-PAGE, 2 * 18679, native enzyme, sequence calculation
homodimer
2 * 20000, SDS-PAGE
homodimer
2 * 18522, small component of the 4-hydroxyphenylacetate 3-monooxygenase, calculated from sequence
homodimer
-
2 * 17000, SDS-PAGE
homodimer
-
2 * 16989, calculated from amino acid sequence
homodimer
-
2 * 17000, SDS-PAGE
-
homodimer
-
2 * 16989, calculated from amino acid sequence
-
homotrimer
3 * 71400
homotrimer
3 * 72000, SDS-PAGE
homotrimer
-
3 * 72000, SDS-PAGE
-
homotrimer
-
3 * 72000, SDS-PAGE
-
additional information
overproduction of the small HpaC component in Escherichia coli K-12 cells facilitates the purification of the protein, which is a homodimer that catalyzes the reduction of free flavins by NADH in preference to NADPH
additional information
the two 20-kDa subunit proteins contain flavin mononucleotide (FMN) reductase conserved domains
additional information
-
the two 20-kDa subunit proteins contain flavin mononucleotide (FMN) reductase conserved domains
additional information
-
the two 20-kDa subunit proteins contain flavin mononucleotide (FMN) reductase conserved domains
-
additional information
crystal structure of FerA reveals a twisted seven-stranded antiparallel beta-barrel, enzyme structure modeling, overview
additional information
-
crystal structure of FerA reveals a twisted seven-stranded antiparallel beta-barrel, enzyme structure modeling, overview
additional information
-
crystal structure of FerA reveals a twisted seven-stranded antiparallel beta-barrel, enzyme structure modeling, overview
-
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E248A
residue of the of the recognition helix of the MarR domain, activation by 4-hydroxyphenylacetic acid similarly to wild-type, high constitutive NADH oxidation activity without auto-inhibition
E251A
residue of the of the recognition helix of the MarR domain, activation by 4-hydroxyphenylacetic acid similarly to wild-type, high constitutive NADH oxidation activity without auto-inhibition
F216A
high constitutive NADH oxidation activity without auto-inhibition
H170A
putative residue of the 4-hydroxyphenylacetic acid binding site, activation by 4-hydroxyphenylacetic acid similarly to wild-type
N174A
putative residue of the 4-hydroxyphenylacetic acid binding site, activation by 4-hydroxyphenylacetic acid similarly to wild-type
R20A
residue of flavin reductase domain, activation by 4-hydroxyphenylacetic acid similarly to wild-type
S172A
putative residue of the 4-hydroxyphenylacetic acid binding site, activation by 4-hydroxyphenylacetic acid similarly to wild-type
Y207A
putative residue of the 4-hydroxyphenylacetic acid binding site, no activation by 4-hydroxyphenylacetic acid along with low NADH oxidation rate
synthesis
construction of biosynthetic pathways for the production of tyrosol acetate and hydroxytyrosol acetate in Escherichia coli. Escherichia coli YeaE is the best aldehyde reductase for tyrosol accumulation. Tyrosol acetate production is achieved by overexpression of alcohol acetyltransferase ATF1 from Saccharomyces cerevisiae, and hydroxytyrosol acetate production by overexpression of 4-hydroxyphenylacetate 3-hydroxylase genes HpaBC
synthesis
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construction of biosynthetic pathways for the production of tyrosol acetate and hydroxytyrosol acetate in Escherichia coli. Escherichia coli YeaE is the best aldehyde reductase for tyrosol accumulation. Tyrosol acetate production is achieved by overexpression of alcohol acetyltransferase ATF1 from Saccharomyces cerevisiae, and hydroxytyrosol acetate production by overexpression of 4-hydroxyphenylacetate 3-hydroxylase genes HpaBC
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additional information
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improvement of the intracellular environment for enhancing L-arginine production of Corynebacterium glutamicum by inactivation of H2O2-forming flavin reductases and optimization of ATP supply. Construction of mutants of gene frd2, strain 5-5(frd2) and deletion strains 5-5DELTAfrd2 and 5-5DELTAfrd12. The extracellular H2O2 concentrations of mutant 5-5DELTAfrd12 are lower than that of the wild-type strain SYPA5-5, and the extracellular H2O2 concentrations of mutant 5-5(frd2) is increased compared to the wild-type. Flavin reductase activities in frd1 and frd2 overexpression and deletion strains with NADH and FAD, overview
additional information
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improvement of the intracellular environment for enhancing L-arginine production of Corynebacterium glutamicum by inactivation of H2O2-forming flavin reductases and optimization of ATP supply. Construction of mutants of gene frd2, strain 5-5(frd2) and deletion strains 5-5DELTAfrd2 and 5-5DELTAfrd12. The extracellular H2O2 concentrations of mutant 5-5DELTAfrd12 are lower than that of the wild-type strain SYPA5-5, and the extracellular H2O2 concentrations of mutant 5-5(frd2) is increased compared to the wild-type. Flavin reductase activities in frd1 and frd2 overexpression and deletion strains with NADH and FAD, overview
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additional information
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construction of an HpaC inactivation mutant strain W-KO
additional information
silencing of Nox by RNAi
additional information
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silencing of Nox by RNAi
additional information
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silencing of Nox by RNAi
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additional information
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site-directed mutagenesis of BorF implicates His160 and Arg38 as contributing to the catalytic activity and the pH dependence
additional information
site-directed mutagenesis of BorF implicates His160 and Arg38 as contributing to the catalytic activity and the pH dependence
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Escherichia coli strain BL21(DE3)pLysS effectively produces an active and soluble form of StyB as about 9% of the total protein content, when cultivated at 20°C with 0.5 mM IPTG
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expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli Rosetta(DE3) cells
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expression in Escherichia coli
expression in Saccharomyces cerevisiae
gene abeF, recombinant overexpression in Escherichia coli
gene borF, recombinant overexpression in Escherichia coli
gene frd2, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant overexpression of N-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3)
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gene Nox, DNA and amino acid sequence determination and analysis, phylogenetic tree, quantitative real-time PCR enzyme expresison analysis
gene Pden_2689, recombinant overexpression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)pLysS
overexpression in Escherichia coli
overproduction of the small HpaC component in Escherichia coli K-12
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overproduction of the small HpaC component of the 4-hydroxyphenylacetate 3-monooxygenase in Escherichia coli K-12 cells
recombinant overexpression of His-tagged wild-type enzymes HpaC and Fre in strain BL21(DE3), complementation of the inactivation mutant by transient expression of different gene hpaC variants, overview
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sequence comparisons and phylogenetic analysis, cloning in Escherichia coli strain DH5alpha, recombinant expression in Escherichia coli strain BL21(DE3) (pLysS) in inclusion bodies
subcloned into an IPTG-inducible expression vector, pBaiH2.2. Escherichia coli DH5a cells transformed with pBaiH2.2 express 10fold higher levels of NADH:FOR upon induction with IPTG than did Eubacterium sp. VPI 12708 cells induced with cholic acid
the NADH-dependent flavin reductase is encoded by two highly similar genes, LJ_0548 and LJ_0549, or ,nfr1 and nfr2, encoding the subunits 1 and 2 of the enzyme, DNA and amino acid sequence determination and analysis, a plasmid with the promoter region of the LJ_0045 lactate dehydrogenase gene and a bidirectional terminator is used for overexpression of the LJ_0548 and LJ_0549 genes
expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(DE3) cells
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