Information on EC 1.5.1.41 - riboflavin reductase [NAD(P)H]

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The expected taxonomic range for this enzyme is: Bacteria, Archaea

EC NUMBER
COMMENTARY hide
1.5.1.41
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RECOMMENDED NAME
GeneOntology No.
riboflavin reductase [NAD(P)H]
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
reduced riboflavin + NAD(P)+ = riboflavin + NAD(P)H + H+
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Metabolic pathways
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Riboflavin metabolism
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flavin biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
riboflavin:NAD(P)+ oxidoreductase
Catalyses the reduction of soluble flavins by reduced pyridine nucleotides. Highest activity with riboflavin. When NADH is used as acceptor, the enzyme can also utilize FMN and FAD as substrates, with lower activity than riboflavin. When NADPH is used as acceptor, the enzyme has a very low activity with FMN and no activity with FAD [1].
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
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in Escherichia coli NAD(P)H:flavin oxidoreductase is part of a multienzyme system that reduces the Fe(III) center of ribonucleotide reductase to Fe(II) and thereby sets the stage for the generation by dioxygen of a free tyrosyl radical required for enzyme activity
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
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no activity with FAD + NADPH
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-
?
FMN + NADH + H+
FMNH2 + NAD+
show the reaction diagram
FMN + NADPH + H+
FMNH2 + NADP+
show the reaction diagram
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very low activity
-
-
?
riboflavin + NADH + H+
reduced riboflavin + NAD+
show the reaction diagram
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-
-
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?
riboflavin + NADPH + H+
reduced riboflavin + NADP+
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FMN
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the purified refolded enzyme does not contain FMN, unlike the same enzyme expressed as a soluble protein. After the addition of FMN to the protein solution, the refolded enzyme shows a higher activity than the enzyme expressed as the soluble protein
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
iodoacetate
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N-ethylmaleimide
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additional information
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no inhibition by EDTA, desferal or dicoumarol
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0008
FAD
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second substrate: NADH, pH 7.5, 23°C
0.0008 - 0.002
FMN
0.025
NADH
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second substrate riboflavin, pH 7.5, 23°C
0.043
NADPH
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second substrate riboflavin, pH 7.5, 23°C
0.0006 - 0.0016
riboflavin
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.36
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pH 7.5, 23°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23
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assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.9
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isoelectric focusing
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
26212
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x * 26212, calculated from sequence
28000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 26212, calculated from sequence
monomer
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1 * 28000-29000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
vapor diffusion method
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crystals of the refolded enzyme are obtained by adding FMN, FAD, or riboflavin to the protein solution and without the addition of flavin compound
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
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stable at pH 7.4, except at low protein concentrations
392190
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dilute solutions can be stabilized by the addition of bovine serum albumin (0.1 mg/ml) and/or by glycerol
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
construction of a bacterial strain that overproduces the enzyme approximately 100fold
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expressed of N-terminally His-tagged HpaCSt protein in Escherichia coli
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