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Information on EC 1.5.1.36 - flavin reductase (NADH)
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1.5.1.36 flavin reductase (NADH)IUBMB Comments
The enzyme from Escherichia coli W catalyses the reduction of free flavins by NADH. The enzyme has similar affinity to FAD, FMN and riboflavin. Activity with NADPH is more than 2 orders of magnitude lower than activity with NADH.
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Word Map
- 1.5.1.36
-
nadph:flavin
- fmnh2
-
alkanesulfonate
-
oxygen-insensitive
-
beneckea
-
desulfonation
- nitroreductases
-
fmnh2-dependent
The enzyme appears in viruses and cellular organisms
Synonyms
fmn reductase, nad(p)h:flavin oxidoreductase, nadh:flavin oxidoreductase, nadh:fmn oxidoreductase, nad(p)h-flavin oxidoreductase, nadh-dependent flavin reductase, fad reductase, flavin mononucleotide reductase, smob-adp1, c1-hpah, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
BaiH
DszD
FerA
flavin mononucleotide reductase
flavin reductase
flavin:NADH oxidoreductase
FMN reductase
Frd188
fre
HpaC
LJ0548
LJ0549
LuxG
NAD(P)H-dependent H2O2-forming flavin reductase
NAD(P)H:flavin-oxidoreductase
NADH-dependent flavin reductase
NADH: flavin oxidoreductase
NADH: flavinoxidore ductase/NADH oxidase
NADH:flavin oxidoreductase
nfr1
nfr2
NOX
Pden2689
additional information
HpaC
small component of the 4-hydroxyphenylacetate 3-monooxygenase in Escherichia coli K-12 cells
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
reduced flavin + NAD+ = flavin + NADH + H+
-
-
-
-
reduced flavin + NAD+ = flavin + NADH + H+
FAD reduction by recombinant His10-tagged SMOB-ADP1 follows a random sequential mechanism
reduced flavin + NAD+ = flavin + NADH + H+
AbeF follows a random-ordered sequence of substrate binding
reduced flavin + NAD+ = flavin + NADH + H+
BorF proceeds by a sequential ordered kinetic mechanism in which FAD binds first
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
flavin:NAD+ oxidoreductase
The enzyme from Escherichia coli W catalyses the reduction of free flavins by NADH. The enzyme has similar affinity to FAD, FMN and riboflavin. Activity with NADPH is more than 2 orders of magnitude lower than activity with NADH.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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+
-
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+
AbeF binds FAD with higher affinity than FADH2
-
-
?
FAD + NADH + H+
FADH2 + NAD+
BorF binds FAD with higher affinity than FADH2
-
-
?
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
-
-
?
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
-
-
?
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
?
-
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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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
?
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
-
-
?
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+
-
-
-
r
riboflavin + NADH + H+
reduced riboflavin + NAD+
-
-
-
r
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
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADH
-
HpaC, the small component of the 4-hydroxyphenylacetate 3-monooxygenase, is recombinantly overproduced in Escherichia coli K12 and catalyzes the reduction of free flavins by NADH in preference to NADPH
NADH
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
NADPH
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
additional information
-
the enzyme is selectively for NADH over NADPH
-
additional information
the enzyme is selectively for NADH over NADPH
-
additional information
the nicotinamide ribose phosphate part of NAD(P)H plays a major role in binding to Fre, whereas the impact of adenosine phosphate part is negligible
-
additional information
the nicotinamide ribose phosphate part of NAD(P)H plays a major role in binding to Fre, whereas the impact of adenosine phosphate part is negligible
-
additional information
the nicotinamide ribose phosphate part of NAD(P)H plays a major role in binding to Fre, whereas the impact of adenosine phosphate part is negligible
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
no effect on enzyme activity by Cl- and NaN3
additional information
-
the enzyme is not susceptible to Ca2+, Mg2+, Mn2+ and Co2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
AMP
mixed noncompetitive versus FMN, and competitive versus NADH
Fe2+
complete inactivation at 0.1 mM, 38% activity remains in presence of 10 mM EDTA
HpaB
-
presence and binding of HpaB reduced the enzyme activity of HpaC due to stabilization and reduced oxidation by O2 of FADH2
-