1.5.1.42: FMN reductase (NADH)
This is an abbreviated version!
For detailed information about FMN reductase (NADH), go to the full flat file.
Word Map on EC 1.5.1.42
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1.5.1.42
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luciferase
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monooxygenase
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desulfurization
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bioluminescent
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rhodococcus
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biodesulfurization
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erythropolis
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photobacterium
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dibenzothiophene
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fossil
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instantly
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p-hydroxyphenylacetate
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cost-competitive
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baumannii
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sigma54-dependent
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petroleum
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fmnh2-dependent
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phosphoreum
- 1.5.1.42
- luciferase
- monooxygenase
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desulfurization
-
bioluminescent
- rhodococcus
-
biodesulfurization
- erythropolis
-
photobacterium
- dibenzothiophene
-
fossil
-
instantly
- p-hydroxyphenylacetate
-
cost-competitive
- baumannii
-
sigma54-dependent
-
petroleum
-
fmnh2-dependent
- phosphoreum
Reaction
Synonyms
DszD, flavin reductase, Fred, HcbA3, hexachlorobenzene oxidative dehalogenase system reductase component, LuxG, LuxG oxidoreductase, NADH specific FMN reductase, NADH-dependent FMN reductase, NADH-FMN oxidoreductase, NADH-FMN reductase, NADH:flavin oxidoreductase, NADH:FMN oxidoreductase, NADH:FMN oxidoreductase (flavin reductase), NADH:FMN-oxidoreductase
ECTree
Advanced search results
Engineering
Engineering on EC 1.5.1.42 - FMN reductase (NADH)
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N33A
site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type
N33C
site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type
N33D
site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type
N33E
site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type
N33F
site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type
N33G
site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type
N33HID
site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type
N33HIE
site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type
N33HIP
site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type
N33I
site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type
N33K
site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type
N33L
site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type
N33M
site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type
N33Q
site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type
N33R
site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type
N33S
site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type
N33T
site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type
N33V
site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type
N33W
site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type
N33Y
site-directed mutagenesis, Gibbs activation and reaction free energies obtained for the hydride transfer compared to wild-type
T62A
T62N
T62A
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the mutant shows 7fold increase in activity compared to the wild type enzyme
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T62N
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the mutant shows 5fold increase in activity compared to the wild type enzyme
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additional information
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the mutant shows 7fold increase in activity compared to the wild type enzyme
T62A
site-directed mutagenesis, the mutant shows 7fold increased activity compared to wild-type
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the mutant shows 5fold increase in activity compared to the wild type enzyme
T62N
site-directed mutagenesis, the mutant shows 5fold increased activity compared to wild-type
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design of a stable immobilizing reagent for bioluminescent analysis using luciferase, EC 1.14.14., from a recombinant Escherichia coli strain and NADH:FMN-oxidoreductase, EC 1.5.1.42. Natural polymers, gelatin and starch, are used to create a viscous, structured microenvironment for the NADH:FMN-oxidoreductase-luciferase system. Evaluation of the stability of the coupled enzyme system, overview. Both gelatin and starch have a stabilizing effect on the enzymes, the enzymes' activity is increased 2fold in the presence of 1% and 5% of gelatin at 20°C and 25°C, respectively. The acceptable pH range of the coupled enzyme system expands into the alkaline region and becomes 6.8-8.1. Stabilization at low ionic strength (0.01-0.06 mol/l) is observed, thermal inactivation rate constants of the enzymes at 25-43°C are unchanged
additional information
establishment of a coupled pure enzyme bioluminescent system and usage for NADH detection
additional information
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establishment of a coupled pure enzyme bioluminescent system and usage for NADH detection
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additional information
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the role played by the critical active site residue threonine residue is analyzed using mutant having an asparagine or alanine substitution at this position. The mutants show that having an alanine residue at this position lowers the activation barrier for this reaction, increasing the reaction rate
additional information
replacement of the wild-type spectator residue of the rate-limiting step of the reduction of FMN to FMNH2 catalysed by DszD and known to play an important role in the reaction energy profile. As replacements, all the naturally occurring amino acids are used, one at a time, using computational methodologies, determination of mutant activities, application of quantum mechanics/molecular mechanics (QM/MM) methods within an ONIOM scheme
additional information
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replacement of the wild-type spectator residue of the rate-limiting step of the reduction of FMN to FMNH2 catalysed by DszD and known to play an important role in the reaction energy profile. As replacements, all the naturally occurring amino acids are used, one at a time, using computational methodologies, determination of mutant activities, application of quantum mechanics/molecular mechanics (QM/MM) methods within an ONIOM scheme
additional information
Rhodococcus erythropolis IGTS8 / ATCC 53968
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the role played by the critical active site residue threonine residue is analyzed using mutant having an asparagine or alanine substitution at this position. The mutants show that having an alanine residue at this position lowers the activation barrier for this reaction, increasing the reaction rate
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