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reduced riboflavin + NADP+ = riboflavin + NADPH + H+
reduced riboflavin + NADP+ = riboflavin + NADPH + H+
-
-
-
-
reduced riboflavin + NADP+ = riboflavin + NADPH + H+
ping-pong mechanism
-
reduced riboflavin + NADP+ = riboflavin + NADPH + H+
ping-pong mechanism
-
reduced riboflavin + NADP+ = riboflavin + NADPH + H+
catalytic mechanism
-
reduced riboflavin + NADP+ = riboflavin + NADPH + H+
bi-bi ternary mechanism, i.e. both FMN and NADPH must bind to the active site before catalysis can occur
-
reduced riboflavin + NADP+ = riboflavin + NADPH + H+
binding of FMN by apoenzyme is noncooperative, exothermic and primarily enthalpy driven with significant conformational changes in enzyme upon binding. The kinetically deduced ping-pong mechanism is supported by measurement of binding affinities of the oxidized and reduced FMN cofoactors
-
reduced riboflavin + NADP+ = riboflavin + NADPH + H+
FRP:luciferase coupled reaction can utilize reduced flavin by both free diffusion and direct transfer
-
reduced riboflavin + NADP+ = riboflavin + NADPH + H+
single-enzyme kinetic assay, SsuE follows ordered sequential mechanism with NADPH as the first substrate to bind and NADP+ as the last product to leave. In presence of monooxygenase SsuD and octanesulfonate mechanism is altered to rapid equilibrium ordered mechanism, and Km-value for FMN increases 10fold
-
reduced riboflavin + NADP+ = riboflavin + NADPH + H+
the nicotinamide of NAD+ stacks the isoalloxazine ring of FMN so that NADH can directly transfer hydride. The bound NADP+ also has a compact conformation but is bound in a reverse direction, which is not suitable for hydride transfer
-
reduced riboflavin + NADP+ = riboflavin + NADPH + H+
the enzyme catalysis obeys the ping-pong Bi-Bi kinetic mechanism with substrate FMN as well as substrate nitrofurazone, but upon coupling with the bioluminescent reaction of luciferase, it changes to the sequential mechanism
-
reduced riboflavin + NADP+ = riboflavin + NADPH + H+
the nicotinamide of NAD+ stacks the isoalloxazine ring of FMN so that NADH can directly transfer hydride. The bound NADP+ also has a compact conformation but is bound in a reverse direction, which is not suitable for hydride transfer
-
-
reduced riboflavin + NADP+ = riboflavin + NADPH + H+
the enzyme catalysis obeys the ping-pong Bi-Bi kinetic mechanism with substrate FMN as well as substrate nitrofurazone, but upon coupling with the bioluminescent reaction of luciferase, it changes to the sequential mechanism
-
-
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1,3-dinitrobenzene + NADH + H+
? + NAD+
-
10.6% activity compared to FMN
-
-
?
1,4-benzoquinone + NADH + H+
1,4-benzoquinol + NAD+
-
18.6% activity compared to FMN
-
-
?
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
3-nitrophenol + NADH + H+
? + NAD+
-
8.95% activity compared to FMN
-
-
?
4-nitroacetophenone + NADH + H+
? + NAD+
-
17.9% activity compared to FMN
-
-
?
4-nitroaniline + NADH + H+
? + NAD+
-
4.91% activity compared to FMN
-
-
?
4-nitrobenzoate + NADH + H+
? + NAD+
-
21.2% activity compared to FMN
-
-
?
4-nitrophenol + NADH + H+
? + NAD+
-
8.07% activity compared to FMN
-
-
?
4-nitrotoluene + NADH + H+
? + NAD+
-
8.83% activity compared to FMN
-
-
?
FAD + NAD(P)H
FADH2 + NAD(P)+
FAD + NADH + H+
FADH2 + NAD+
-
58.1% activity compared to FMN
-
-
?
FAD + NADPH
FADH2 + NADP+
FAD + NADPH + H+
FADH2 + NADP+
FAD + NADPH + H+
reduced FAD + NADP+
FMN + NAD(P)H
FMNH2 + NAD(P)+
FMN + NADH
FMNH2 + NADP+
-
preference for NADPH over NADH, rate of reduction is 80 times faster with NADPH
-
-
?
FMN + NADH + H+
FMNH2 + NAD+
FMN + NADPH
FMNH2 + NADP+
FMN + NADPH
FMNH2 + NADP+ + H+
-
-
-
-
?
FMN + NADPH + H+
FMNH2 + NADP+
FMN + NADPH + H+
reduced FMN + NADP+
FMNH2 + NADP+
FMN + NADPH + H+
galactoflavin + NADPH
reduced galactoflavin + NADP+
lumiflavin + NADH + H+
reduced lumiflavin + NAD+
-
14.1% activity compared to FMN
-
-
?
lumiflavin + NADPH + H+
reduced lumiflavin + NADP+
menadione + NADH + H+
menadiol + NAD+
-
19.0% activity compared to FMN
-
-
?
methyl-4-nitrobenzoate + NADH + H+
? + NAD+
-
10.7% activity compared to FMN
-
-
?
methylene blue + NADH + H+
reduced methylene blue + NAD+
-
29.0% activity compared to FMN
-
-
?
NADH + H+ + oxidized 2,6-dichlorophenolindophenol
NAD+ + reduced 2,6-dichlorophenolindophenol
nitrofurantoin + NADH + H+
? + NAD+
-
10.1% activity compared to FMN
-
-
?
nitrofurazone + NADH + H+
reduced nitrofurazone + NAD+
-
13.5% activity compared to FMN
-
-
?
nitrofurazone + NADPH + 4 H+
5-(hydroxyamino)furan-2-carbaldehyde semicarbazone + NADP+ + H2O
oxidized 2,6-dichlorophenolindophenol + NADPH + H+
reduced 2,6-dichlorophenolindophenol + NADP+
-
-
-
-
?
oxidized methylene blue + NADPH + H+
reduced methylene blue + NADP+
-
-
-
-
?
oxidized riboflavin + NADPH + H+
reduced riboflavin + NADP+
reduced 2-thioFMN + NAD+
?
-
-
-
-
r
riboflavin + NAD(P)H
reduced riboflavin + NAD(P)+
-
-
-
-
r
riboflavin + NAD(P)H
reduced riboflavin + NADP+
-
redox potential of the irreversible reductive half-reaction
-
-
?
riboflavin + NADH + H+
reduced riboflavin + NAD+
-
29.0% activity compared to FMN
-
-
?
riboflavin + NADPH
reduced riboflavin + NADP+
riboflavin + NADPH + H+
reduced riboflavin + NADP+
riboflavin-5-phosphate + NADH + H+
reduced FMN + NAD+
additional information
?
-
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
-
15.4% activity compared to FMN
-
-
?
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
-
15.4% activity compared to FMN
-
-
?
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
-
8.48% activity compared to FMN
-
-
?
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
-
8.48% activity compared to FMN
-
-
?
FAD + NAD(P)H
FADH2 + NAD(P)+
-
-
-
-
r
FAD + NAD(P)H
FADH2 + NAD(P)+
-
-
-
-
r
FAD + NADPH
FADH2 + NADP+
-
-
-
-
?
FAD + NADPH
FADH2 + NADP+
-
-
-
-
r
FAD + NADPH
FADH2 + NADP+
-
-
-
-
r
FAD + NADPH
FADH2 + NADP+
-
-
-
-
?
FAD + NADPH
FADH2 + NADP+
-
-
-
-
?
FAD + NADPH
FADH2 + NADP+
-
-
-
-
?
FAD + NADPH
FADH2 + NADP+
-
-
-
-
?
FAD + NADPH + H+
FADH2 + NADP+
-
-
-
?
FAD + NADPH + H+
FADH2 + NADP+
-
-
-
-
?
FAD + NADPH + H+
FADH2 + NADP+
-
specific activity for the reduction of oxidized riboflavin, FMN and FAD is similar
-
-
?
FAD + NADPH + H+
FADH2 + NADP+
the enzyme (BLVRB) binds its coenzyme NADPH 500fold more tightly than its substrate FAD
-
-
?
FAD + NADPH + H+
FADH2 + NADP+
XP_020138941.1
-
-
-
?
FAD + NADPH + H+
FADH2 + NADP+
-
-
-
?
FAD + NADPH + H+
FADH2 + NADP+
-
-
-
r
FAD + NADPH + H+
FADH2 + NADP+
-
-
-
?
FAD + NADPH + H+
reduced FAD + NADP+
-
-
-
-
?
FAD + NADPH + H+
reduced FAD + NADP+
-
-
-
-
?
FMN + NAD(P)H
FMNH2 + NAD(P)+
-
-
-
-
r
FMN + NAD(P)H
FMNH2 + NAD(P)+
-
-
-
-
r
FMN + NAD(P)H
FMNH2 + NAD(P)+
-
-
-
-
r
FMN + NADH
FMNH2 + NAD+
-
-
-
-
?
FMN + NADH
FMNH2 + NAD+
-
-
-
-
?
FMN + NADH + H+
FMNH2 + NAD+
-
-
-
-
?
FMN + NADH + H+
FMNH2 + NAD+
-
-
-
-
?
FMN + NADH + H+
FMNH2 + NAD+
-
-
-
-
?
FMN + NADPH
FMNH2 + NADP+
-
-
-
-
?
FMN + NADPH
FMNH2 + NADP+
-
-
-
-
?
FMN + NADPH
FMNH2 + NADP+
-
preference for NADPH over NADH, rate of reduction is 80 times faster with NADPH
-
-
?
FMN + NADPH
FMNH2 + NADP+
-
-
-
-
?
FMN + NADPH
FMNH2 + NADP+
-
-
-
-
?
FMN + NADPH
FMNH2 + NADP+
-
-
-
-
?
FMN + NADPH
FMNH2 + NADP+
-
-
-
-
?
FMN + NADPH
FMNH2 + NADP+
-
-
-
-
?
FMN + NADPH
FMNH2 + NADP+
-
-
-
-
?
FMN + NADPH
FMNH2 + NADP+
-
-
-
-
?
FMN + NADPH
FMNH2 + NADP+
-
-
-
-
?
FMN + NADPH
FMNH2 + NADP+
-
-
-
-
r
FMN + NADPH
FMNH2 + NADP+
-
-
-
-
?
FMN + NADPH
FMNH2 + NADP+
-
-
-
-
?
FMN + NADPH
FMNH2 + NADP+
-
-
-
-
r
FMN + NADPH
FMNH2 + NADP+
-
reaction may be coupled with luciferase for bioluminescence
-
-
?
FMN + NADPH
FMNH2 + NADP+
-
-
-
-
?
FMN + NADPH + H+
FMNH2 + NADP+
-
203% activity compared to NAD+
-
-
?
FMN + NADPH + H+
FMNH2 + NADP+
-
203% activity compared to NAD+
-
-
?
FMN + NADPH + H+
FMNH2 + NADP+
-
-
-
-
?
FMN + NADPH + H+
FMNH2 + NADP+
-
-
-
-
?
FMN + NADPH + H+
FMNH2 + NADP+
-
-
-
?
FMN + NADPH + H+
FMNH2 + NADP+
-
specific activity for the reduction of oxidized riboflavin, FMN and FAD is similar
-
-
?
FMN + NADPH + H+
FMNH2 + NADP+
-
-
-
?
FMN + NADPH + H+
FMNH2 + NADP+
-
-
-
-
?
FMN + NADPH + H+
FMNH2 + NADP+
-
-
-
?
FMN + NADPH + H+
reduced FMN + NADP+
-
-
-
-
?
FMN + NADPH + H+
reduced FMN + NADP+
-
-
-
-
?
FMNH2 + NADP+
FMN + NADPH + H+
-
-
-
r
FMNH2 + NADP+
FMN + NADPH + H+
-
-
-
r
galactoflavin + NADPH
reduced galactoflavin + NADP+
-
-
-
-
?
galactoflavin + NADPH
reduced galactoflavin + NADP+
-
-
-
-
?
lumiflavin + NADPH + H+
reduced lumiflavin + NADP+
-
-
-
-
?
lumiflavin + NADPH + H+
reduced lumiflavin + NADP+
-
-
-
-
?
NADH + H+ + oxidized 2,6-dichlorophenolindophenol
NAD+ + reduced 2,6-dichlorophenolindophenol
-
23.0% activity compared to FMN
-
-
?
NADH + H+ + oxidized 2,6-dichlorophenolindophenol
NAD+ + reduced 2,6-dichlorophenolindophenol
-
23.0% activity compared to FMN
-
-
?
nitrofurazone + NADPH + 4 H+
5-(hydroxyamino)furan-2-carbaldehyde semicarbazone + NADP+ + H2O
-
-
-
-
?
nitrofurazone + NADPH + 4 H+
5-(hydroxyamino)furan-2-carbaldehyde semicarbazone + NADP+ + H2O
-
-
-
-
?
oxidized riboflavin + NADPH + H+
reduced riboflavin + NADP+
-
-
-
?
oxidized riboflavin + NADPH + H+
reduced riboflavin + NADP+
-
specific activity for the reduction of oxidized riboflavin, FMN and FAD is similar
-
-
?
riboflavin + NADPH
reduced riboflavin + NADP+
-
-
-
-
?
riboflavin + NADPH
reduced riboflavin + NADP+
-
-
-
-
?
riboflavin + NADPH
reduced riboflavin + NADP+
-
-
-
-
?
riboflavin + NADPH
reduced riboflavin + NADP+
-
-
-
-
?
riboflavin + NADPH
reduced riboflavin + NADP+
-
-
-
-
?
riboflavin + NADPH
reduced riboflavin + NADP+
-
-
-
-
r
riboflavin + NADPH
reduced riboflavin + NADP+
-
i.e. FMN
i.e. FMNH2
-
?
riboflavin + NADPH
reduced riboflavin + NADP+
-
redox potential and equilibria in the reversible reductive half-reaction
-
-
?
riboflavin + NADPH + H+
reduced riboflavin + NADP+
-
-
-
-
?
riboflavin + NADPH + H+
reduced riboflavin + NADP+
-
-
-
-
?
riboflavin + NADPH + H+
reduced riboflavin + NADP+
-
-
-
-
?
riboflavin + NADPH + H+
reduced riboflavin + NADP+
-
-
-
?
riboflavin + NADPH + H+
reduced riboflavin + NADP+
-
-
-
?
riboflavin-5-phosphate + NADH + H+
reduced FMN + NAD+
-
-
-
-
r
riboflavin-5-phosphate + NADH + H+
reduced FMN + NAD+
-
-
-
-
r
additional information
?
-
-
enzyme additionally has azoreductase activity cleaving the -N=N- bond in azo dyes
-
-
?
additional information
?
-
-
the enzyme reduces both nitrofurazone and FMN effectively, it is bifunctional as flavin reductase and nitroreductase. Two different FMN molecules are involved in the FMN reduction process: FMN tightly associated to the enzyme as prosthetic group and FMN as a substrate. The enzyme is also active with FAD, riboflavin, and lumiflavin, the two latter give the highest activity
-
-
?
additional information
?
-
-
the enzyme reduces both nitrofurazone and FMN effectively, it is bifunctional as flavin reductase and nitroreductase. Two different FMN molecules are involved in the FMN reduction process: FMN tightly associated to the enzyme as prosthetic group and FMN as a substrate. The enzyme is also active with FAD, riboflavin, and lumiflavin, the two latter give the highest activity
-
-
?
additional information
?
-
-
bifunctional enzyme flavin reductase (NADPH)/biliverdin-IXbeta reductase
-
-
?
additional information
?
-
-
prefers NADPH over NADH
-
-
?
additional information
?
-
-
prefers NADPH over NADH
-
-
?
additional information
?
-
-
the enzyme is also active with FMN and NADH, cf. EC 1.5.1.36
-
-
?
additional information
?
-
-
the enzyme is also active with FMN and NADH, cf. EC 1.5.1.36
-
-
?
additional information
?
-
-
no catalytic activity is detected with NADH
-
-
?
additional information
?
-
significant reduction of NADP+ by rFlaR refolded in the presence Fe2+. Fe2+ is the electron donor in the rFlaR-NADP+ reductase activity
-
-
-
additional information
?
-
FR is a relevant source of hydrogen peroxide but superoxide radical anions are a minor by-product of the reaction
-
-
?
additional information
?
-
-
FR is a relevant source of hydrogen peroxide but superoxide radical anions are a minor by-product of the reaction
-
-
?
additional information
?
-
FR is a relevant source of hydrogen peroxide but superoxide radical anions are a minor by-product of the reaction
-
-
?
additional information
?
-
-
enzyme transfers reduced riboflavin 5'-phosphate to luciferase by direct channeling in vitro and in vivo, formation of donor-acceptor enzyme complex
-
-
?
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1.5.1.30 flavin reductase (NADPH)
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