Information on EC 1.5.1.37 - FAD reductase (NADH)

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.5.1.37
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RECOMMENDED NAME
GeneOntology No.
FAD reductase (NADH)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
FADH2 + NAD+ = FAD + NADH + H+
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Metabolic pathways
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Microbial metabolism in diverse environments
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Riboflavin metabolism
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SYSTEMATIC NAME
IUBMB Comments
FADH2:NAD+ oxidoreductase
The enzyme from Burkholderia phenoliruptrix can reduce either FAD or flavin mononucleotide (FMN) but prefers FAD. Unlike EC 1.5.1.36, flavin reductase (NADH), the enzyme can not reduce riboflavin. The enzyme does not use NADPH as acceptor.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
FAD + NADH + H+
FADH2 + NAD+
show the reaction diagram
FMN + NADH + H+
FMNH2 + NAD+
show the reaction diagram
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FAD is a better substrate than FMN. The enzyme does not use NADPH or riboflavin as substrate
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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
FAD + NADH + H+
FADH2 + NAD+
show the reaction diagram
Q8GME2
the enzyme can adequately supply reduced flavin under saturating substrate conditions to support catalysis of flavin-dependent halogenase SgcC3 and monooxygenase SgcC during biosynthesis of C-1027
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADH
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the enzyme does not use NADPH as substrate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0048 - 0.0082
FAD
0.0103
FMN
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cosubstrate: NADH, pH 7.0, 24°C
0.0401 - 0.164
NADH
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.5 - 16.6
FAD
18.5
FMN
Paraburkholderia phenoliruptrix
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cosubstrate: NADH, pH 7.0, 24°C
3.1 - 30.1
NADH
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3458
FAD
Paraburkholderia phenoliruptrix
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cosubstrate: NADH, pH 7.0, 24°C
20
1796
FMN
Paraburkholderia phenoliruptrix
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cosubstrate: NADH, pH 7.0, 24°C
56
72.5 - 77.3
NADH
8
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
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Na-phosphate buffer
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 7.6
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pH 5.0 (sodium succinate buffer): 52% of maximal activity, pH 7.6: 75% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
assay at room temperature
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23 - 45
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23°C: 85% of maximal activity, 45°C: 70% of maximal activity
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22000
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x * 22000, His-tagged TftC, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 22000, His-tagged TftC, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
apo-form crystals of TftC, TftC-FAD complex and TftC-FAD-NADH complex are grown at 4°C using the hanging drop vapor diffusion method. Crystal structures of dimeric TftC is determined at 2.5 A resolution
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, His-tagged TftC loses about 50% activity after 2 months
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0°C, His-tagged TftC is unstable in the elution buffer containing 140 mM imidazole on ice, losing about 50% activity in 2 h
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli as a C-terminally His-tagged fusion protein
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overexpression in Escherichia coli