Information on EC 1.5.1.42 - FMN reductase (NADH)

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.5.1.42
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RECOMMENDED NAME
GeneOntology No.
FMN reductase (NADH)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
FMNH2 + NAD+ = FMN + NADH + H+
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
bacterial bioluminescence
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Riboflavin metabolism
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
FMNH2:NAD+ oxidoreductase
The enzyme often forms a two-component system with monooxygenases. Unlike EC 1.5.1.38, FMN reductase (NADPH), and EC 1.5.1.39, FMN reductase [NAD(P)H], this enzyme has a strong preference for NADH over NADPH, although some activity with the latter is observed [1,2]. While FMN is the preferred substrate, FAD can also be used with much lower activity [1,3].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
i.e. Chelatobacter heintzii
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-
Manually annotated by BRENDA team
Rhodococcus erythropolis IGTS8 / ATCC 53968
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-
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
FAD + NAD+ + H+
FADH2 + NAD+
show the reaction diagram
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activity with FADH2 and NAD+ is 5% of the activity with FMNH2 and NAD+
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-
?
FAD + NADH + H+
FADH2 + NAD+
show the reaction diagram
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activity is 75% of that with FMN
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-
?
FMN + NADH + H+
FMNH2 + NAD+
show the reaction diagram
FMN + NADPH + H+
FMNH2 + NADP+
show the reaction diagram
FMNH2 + NAD+
FMN + NADH + H+
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
FMN + NADH + H+
FMNH2 + NAD+
show the reaction diagram
FMN + NADPH + H+
FMNH2 + NADP+
show the reaction diagram
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-
-
-
?
FMNH2 + NAD+
FMN + NADH + H+
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
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0.005 M, 52% inhibition
5,5'-dithiobis(2-nitrobenzoic acid)
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0.001 M, 38% inhibition
AMP
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0.01 M, 36% inhibition
antimycin A
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0.05 mM, 50% inhibition
N-ethylmaleimide
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0.001 M, 38% inhibition
p-hydroxymercuribenzoate
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0.001 M, 49% inhibition
rotenone
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0.0004 M, 20% inhibition
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.001 - 0.0013
FMN
0.012 - 0.25
NADH
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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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
15.5
NADPH
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pH 7.0, 23C
additional information
additional information
LuxG releases FMNH- with a rate constant of 4.5-6/s. The anaerobic reaction of LuxG with NADH involves half-sites reactivity, with the first flavin being reduced at a rate of 68/s and the second at a rate of 2.8/s
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.05
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pH 6.8, 23C
31
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pH 7.0, 23C
additional information
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purity was too low to permit estimation of specific activity
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2
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gelatin-immobilized enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 10
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bimodal, pH 5: 90% of maximal activity, pH 6.5: about 50% of maximal activity, pH 10: about 70% of maximal activity
5 - 8.6
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the pH curve is bimodal, with maximal activity exhibited at pH 8.6, a minimum at pH 6.0. and a second maximum at pH 5.0
6.8 - 8.1
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over 50% of maximal activity within this range
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23
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assay at
additional information
stopped-flow kinetic experiments are performed at 4C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
lyophilized enzyme
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
19000
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gel filtration
22000
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x * 22000, SDS-PAGE
23000
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gel filtration
26483
x * 26483, calculated from sequence
30000
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gel filtration
31000
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sucrose density gradient centrifugation
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10 - 43
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effective rate constants of the first and second thermal inactivation stages of coupled enzymes NADH:FMN-oxidoreductase and luciferase in the presence of 1% gelatin, 5% gelatin, or buffer solution (control) at different temperatures, overview
55
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5 min, 60% loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
immobilization in starch and gelatin gels increases the stability of of the enzme to the effects of external conditions
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, considerable loss of activity of reductase preparations
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-70C, in presence of 2 mM dithiothreitol, stable over several months
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4C, considerable loss of activity of reductase preparations
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3)pLysS cells
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gene luxG encoding LuxG, the flavin reductase, is encoded in the same operon as its counterpart LuxAB
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
T62A
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the mutant shows 7fold increase in activity compared to the wild type enzyme
T62N
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the mutant shows 5fold increase in activity compared to the wild type enzyme
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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