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
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biodesulfurization
- erythropolis
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photobacterium
- dibenzothiophene
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fossil
-
instantly
- p-hydroxyphenylacetate
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cost-competitive
- baumannii
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sigma54-dependent
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petroleum
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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
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Substrates Products
Substrates Products on EC 1.5.1.42 - FMN reductase (NADH)
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REACTION DIAGRAM
FADH2 + NAD+
FMN and FAD are both substrates for the reductase. FMN is the favored substrate with a 2fold-higher rate constant and affinity that is about 5times higher compared to that of FAD. With regard to electron donors, only NADH is effective whereas NADPH at a similar concentration acts as a very poor cosubstrate
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?
FAD + NADH + H+
FADH2 + NAD+
FMN and FAD are both substrates for the reductase. FMN is the favored substrate with a 2fold-higher rate constant and affinity that is about 5times higher compared to that of FAD. With regard to electron donors, only NADH is effective whereas NADPH at a similar concentration acts as a very poor cosubstrate
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-
?
FAD + NADH + H+
FADH2 + NAD+
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activity with FADH2 and NAD+ is 5% of the activity with FMNH2 and NAD+
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-
?
FMN + NADH + H+
FMNH2 + NAD+
FMN is obtained by conversion of FAD to FMN using snake venom from Crotalus adamanteus
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?
FMN + NADH + H+
FMNH2 + NAD+
FMN is obtained by conversion of FAD to FMN using snake venom from Crotalus adamanteus
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?
FMN + NADH + H+
FMNH2 + NAD+
FMN and FAD are both substrates for the reductase. FMN is the favored substrate with a 2fold-higher rate constant and affinity that is about 5times higher compared to that of FAD. With regard to electron donors, only NADH is effective whereas NADPH at a similar concentration acts as a very poor cosubstrate
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-
?
FMN + NADH + H+
FMNH2 + NAD+
FMN and FAD are both substrates for the reductase. FMN is the favored substrate with a 2fold-higher rate constant and affinity that is about 5times higher compared to that of FAD. With regard to electron donors, only NADH is effective whereas NADPH at a similar concentration acts as a very poor cosubstrate
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?
FMN + NADH + H+
FMNH2 + NAD+
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activity with NADP+ and FMNH2 is only 10% of the activity with FMNH2 and NAD+
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?
FMN + NADH + H+
FMNH2 + NAD+
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the affinity of the NADH-specific reductase is about 60 times greater for NADH than for NADPH
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?
FMN + NADH + H+
FMNH2 + NAD+
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the NADH specific FMN reductase does dehydrogenate NADPH with a maximal velocity one-tenth of that for NADH
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FMN + NADPH + H+
FMNH2 + NADP+
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activity with NADP+ and FMNH2 is only 10% of the activity with FMNH2 and NAD+
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FMN + NADPH + H+
FMNH2 + NADP+
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the NADH specific FMN reductase does dehydrogenate NADPH with a maximal velocity one-tenth of that for NADH
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HcbA3 is an NADH:FMN oxidoreductase. Successful reconstitution of the oxidative dehalogenase reaction in vitro, which consists of HcbA1, HcbA3, FMN, and NADH, suggesting that HcbA3 may also be the partner reductase component for HcbA1 in Nocardioides sp. PD653. The optimal molar ratio of HcbA1 and HcbA3 is 7:1
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additional information
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a transfer of reduced flavin mononucleotide from enzyme LuxG oxidoreductase to luciferase occurs via free diffusion
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additional information
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a transfer of reduced flavin mononucleotide from enzyme LuxG oxidoreductase to luciferase occurs via free diffusion
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?
additional information
?
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analysis of mode of transfer of FMNH- between enzyme LuxG from Photobacterium leiognathi TH1 and enzyme complexes LuxAB from both Photobacterium leiognathi TH1 and Vibrio campbellii, PlLuxAB and VcLuxAB, respectively, using single-mixing and double-mixing stopped-flow spectrophotometry. The oxygenase component of p-hydroxyphenylacetate hydroxylase (C2) from Acinetobacter baumannii, which has no structural similarity to LuxAB, is used to measure the kinetics of release of FMNH- from LuxG. With all FMNH- acceptors used (C2, PlLuxAB, and VcLuxAB), the kinetics of FMN reduction on LuxG are the same. The kinetics of the overall reactions and the individual rate constants correlate well with a free diffusion model for the transfer of FMNH- from LuxG to either LuxAB
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?
additional information
?
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analysis of mode of transfer of FMNH- between enzyme LuxG from Photobacterium leiognathi TH1 and enzyme complexes LuxAB from both Photobacterium leiognathi TH1 and Vibrio campbellii, PlLuxAB and VcLuxAB, respectively, using single-mixing and double-mixing stopped-flow spectrophotometry. The oxygenase component of p-hydroxyphenylacetate hydroxylase (C2) from Acinetobacter baumannii, which has no structural similarity to LuxAB, is used to measure the kinetics of release of FMNH- from LuxG. With all FMNH- acceptors used (C2, PlLuxAB, and VcLuxAB), the kinetics of FMN reduction on LuxG are the same. The kinetics of the overall reactions and the individual rate constants correlate well with a free diffusion model for the transfer of FMNH- from LuxG to either LuxAB
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?
additional information
?
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establishment of a coupled pure enzyme bioluminescent system and usage for quantitative detection, method evaluation
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additional information
?
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a transfer of reduced flavin mononucleotide from enzyme LuxG oxidoreductase to luciferase occurs via free diffusion
-
-
?
additional information
?
-
-
a transfer of reduced flavin mononucleotide from enzyme LuxG oxidoreductase to luciferase occurs via free diffusion
-
-
?
additional information
?
-
analysis of mode of transfer of FMNH- between enzyme LuxG from Photobacterium leiognathi TH1 and enzyme complexes LuxAB from both Photobacterium leiognathi TH1 and Vibrio campbellii, PlLuxAB and VcLuxAB, respectively, using single-mixing and double-mixing stopped-flow spectrophotometry. The oxygenase component of p-hydroxyphenylacetate hydroxylase (C2) from Acinetobacter baumannii, which has no structural similarity to LuxAB, is used to measure the kinetics of release of FMNH- from LuxG. With all FMNH- acceptors used (C2, PlLuxAB, and VcLuxAB), the kinetics of FMN reduction on LuxG are the same. The kinetics of the overall reactions and the individual rate constants correlate well with a free diffusion model for the transfer of FMNH- from LuxG to either LuxAB
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-
?
additional information
?
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-
analysis of mode of transfer of FMNH- between enzyme LuxG from Photobacterium leiognathi TH1 and enzyme complexes LuxAB from both Photobacterium leiognathi TH1 and Vibrio campbellii, PlLuxAB and VcLuxAB, respectively, using single-mixing and double-mixing stopped-flow spectrophotometry. The oxygenase component of p-hydroxyphenylacetate hydroxylase (C2) from Acinetobacter baumannii, which has no structural similarity to LuxAB, is used to measure the kinetics of release of FMNH- from LuxG. With all FMNH- acceptors used (C2, PlLuxAB, and VcLuxAB), the kinetics of FMN reduction on LuxG are the same. The kinetics of the overall reactions and the individual rate constants correlate well with a free diffusion model for the transfer of FMNH- from LuxG to either LuxAB
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-
?
additional information
?
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establishment of a coupled pure enzyme bioluminescent system and usage for quantitative detection, method evaluation
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-
-
additional information
?
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activity with FAD and NADPH is 0.5% of the activity with FMNH2 and NAD+
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?