1.5.1.36: flavin reductase (NADH)
This is an abbreviated version!
For detailed information about flavin reductase (NADH), go to the full flat file.
Word Map on EC 1.5.1.36
-
1.5.1.36
-
nadph:flavin
-
fmnh2
-
alkanesulfonate
-
oxygen-insensitive
-
beneckea
-
desulfonation
-
nitroreductases
-
fmnh2-dependent
- 1.5.1.36
-
nadph:flavin
- fmnh2
-
alkanesulfonate
-
oxygen-insensitive
-
beneckea
-
desulfonation
- nitroreductases
-
fmnh2-dependent
Reaction
Synonyms
AbeF, BaiH, BorF, C1-HpaH, DszD, FAD reductase, FerA, flavin mononucleotide reductase, flavin reductase, flavin:NADH oxidoreductase, FMN reductase, Frd188, frd2, fre, HpaC, LJ0548, LJ0549, LJ_0548, LJ_0549, LuxG, More, NAD(P)H-dependent H2O2-forming flavin reductase, NAD(P)H-flavin oxidoreductase, NAD(P)H:flavin oxidoreductase, NAD(P)H:flavin-oxidoreductase, NADH-dependent flavin reductase, NADH-flavin oxidoreductase, NADH: flavin oxidoreductase, NADH: flavinoxidore ductase/NADH oxidase, NADH:flavin oxidoreductase, NADH:FMN oxidoreductase, nfr1, nfr2, NOX, Pden2689, SMOB-ADP1
ECTree
1.5.1.36 flavin reductase (NADH)Advanced search results
results (
results (Substrates Products
Substrates Products on EC 1.5.1.36 - flavin reductase (NADH)
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
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
-
-
-
