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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Metabolic pathways
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Riboflavin metabolism
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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
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
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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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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?
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
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
15.5
NADPH
Vibrio harveyi
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pH 7.0, 23C
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
6.8
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assay at
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
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assay at
23
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assay at
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
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5 min, 60% loss of activity
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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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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