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FAD + NAD(P)H
FADH2 + NAD(P)+
FAD + NADH
FADH2 + NAD+
-
-
-
r
FAD + NADH + H+
FADH2 + 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+
-
-
-
-
?
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+
-
-
-
-
?
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+
-
-
-
-
?
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
-
-
?
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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
0.056
FAD
-
pH 7.2, 37°C
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
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
-
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
-
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 * 18000, SDS-PAGE
?
-
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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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
-
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli Rosetta(DE3) cells
-
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)
-
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
-
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
-
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

-
expressed in Escherichia coli BL21(DE3) cells
-
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Prieto, M.A.; Garcia, J.L.
Molecular characterization of 4-hydroxyphenylacetate 3-hydroxylase of Escherichia coli. A two-protein component enzyme
J. Biol. Chem.
269
22823-22829
1994
Escherichia coli W (Q57501)
brenda
Galan, B.; Diaz, E.; Prieto, M.A.; Garcia, J.L.
Functional analysis of the small component of the 4-hydroxyphenylacetate 3-monooxygenase of Escherichia coli W: a prototype of a new flavin:NAD(P)H reductase subfamily
J. Bacteriol.
182
627-636
2000
Escherichia coli, Escherichia coli W (Q57501)
brenda
Louie, T.M.; Xie, X.S.; Xun, L.
Coordinated production and utilization of FADH2 by NAD(P)H-flavin oxidoreductase and 4-hydroxyphenylacetate 3-monooxygenase
Biochemistry
42
7509-7517
2003
Escherichia coli
brenda
Chakraborty, S.; Ortiz-Maldonado, M.; Entsch, B.; Ballou, D.P.
Studies on the mechanism of p-hydroxyphenylacetate 3-hydroxylase from Pseudomonas aeruginosa: a system composed of a small flavin reductase and a large flavin-dependent oxygenase
Biochemistry
49
372-385
2010
Pseudomonas aeruginosa
brenda
Yeo, Y.J.; Shin, S.; Lee, S.G.; Park, S.; Jeong, Y.J.
Production, purification, and characterization of soluble NADH-flavin Oxidoreductase (StyB) from Pseudomonas putida SN1
J. Microbiol. Biotechnol.
19
362-367
2009
Pseudomonas putida
brenda
Okai, M.; Ohtsuka, J.; Asano, A.; Guo, L.; Miyakawa, T.; Miyazono, K.; Nakamura, A.; Okada, A.; Zheng, H.; Kimura, K.; Nagata, K.; Tanokura, M.
High pressure refolding, purification, and crystallization of flavin reductase from Sulfolobus tokodaii strain 7
Protein Expr. Purif.
84
214-218
2012
Sulfurisphaera tokodaii, Sulfurisphaera tokodaii 7
brenda
Nijvipakul, S.; Ballou, D.P.; Chaiyen, P.
Reduction kinetics of a flavin oxidoreductase LuxG from Photobacterium leiognathi (TH1): half-sites reactivity
Biochemistry
49
9241-9248
2010
Photobacterium leiognathi
brenda
Li, Q.; Feng, J.; Gao, C.; Li, F.; Yu, C.; Meng, L.; Zhang, Z.; Ma, C.; Gu, L.; Wu, G.; Xu, P.
Purification and characterization of a flavin reductase from the biodesulfurizing bacterium Mycobacterium goodii X7B
Process Biochem.
47
1144-1149
2012
Mycolicibacterium goodii, Mycolicibacterium goodii X7B
-
brenda
Hertzberger, R.; Arents, J.; Dekker, H.L.; Pridmore, R.D.; Gysler, C.; Kleerebezem, M.; de Mattos, M.J.
H(2)O(2) production in species of the Lactobacillus acidophilus group a central role for a novel NADH-dependent flavin reductase
Appl. Environ. Microbiol.
80
2229-2239
2014
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