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
-
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
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KM Value
KM Value on EC 1.5.1.42 - FMN reductase (NADH)
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KM VALUE [mM] 
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
additional information
additional information
the kinetics of binding of FMNH- to PlLuxAB and VcLuxAB and the subsequent reactions with oxygen are the same with either free FMNH- or FMNH- generated in situ by LuxG. No complexes between LuxG and the various species are necessary to transfer FMNH- to the acceptors. Single-mixing and double-mixing stopped-flow spectrophotometry. Anaerobic transient reaction kinetic analysis, overview
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additional information
additional information
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the kinetics of binding of FMNH- to PlLuxAB and VcLuxAB and the subsequent reactions with oxygen are the same with either free FMNH- or FMNH- generated in situ by LuxG. No complexes between LuxG and the various species are necessary to transfer FMNH- to the acceptors. Single-mixing and double-mixing stopped-flow spectrophotometry. Anaerobic transient reaction kinetic analysis, overview
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additional information
additional information
Gibbs activation and reaction free energies obtained for the hydride transfer by wild-type enzyme
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additional information
additional information
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Gibbs activation and reaction free energies obtained for the hydride transfer by wild-type enzyme
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additional information
additional information
steady-state kinetic analysis, the initial rates of NADH oxidation follow typical Michaelis-Menten kinetics, and Lineweaver-Burk plots show parallel patterns for a ping-pong mechanism
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