Information on EC 3.1.3.102 - FMN hydrolase

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

EC NUMBER
COMMENTARY hide
3.1.3.102
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RECOMMENDED NAME
GeneOntology No.
FMN hydrolase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
FMN + H2O = riboflavin + phosphate
show the reaction diagram
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Riboflavin metabolism
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
FMN phosphohydrolase
Requires Mg2+. The enzyme, found in many isoforms purified from both bacteria and plants, is a member of the haloacid dehalogenase superfamily. Most of the isoforms have a wide substrate specificity [2], but isoforms specific for FMN also exist [3].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional riboflavin kinase/FMN phosphatase
UniProt
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
-
-
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Manually annotated by BRENDA team
Pisum sativum cv. Bohatyr
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-
-
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
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
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-
-
-
?
alpha-D-glucose 6-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
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25% of the activity with 4-nitrophenyl phosphate
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-
?
AMP + H2O
adenosine + phosphate
show the reaction diagram
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47% of the activity with 4-nitrophenyl phosphate
-
-
?
FMN + H2O
riboflavin + phosphate
show the reaction diagram
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 + H2O
riboflavin + phosphate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-chloromercuribenzoate
-
2 mM, 100% inhibition
5,5'-dithiobis-2-nitrobenzoic acid
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3 mM, 100% inhibition
AlCl3
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5 mM, 82% inhibition
AMP
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competitive
Ca2+
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5 mM, 27% inhibition, 2 mM, 40% inhibition
Cd2+
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5 mM, 92% inhibition
FeCl3
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5 mM, 100% inhibition
L-phenylalanine
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2.5 mM, 10% inhibition
N-ethylmaleimide
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10 mM, 57% inhibition
phosphate
sodium dodecylsulfate
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0.3%, 100% inhibition
Zn2+
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5 mM, 67% inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Tween 20
enzyme activity increases and temperature optimum shifts to 5–10°C higher temperature in the presence of Tween 20
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0008 - 2.3
FMN
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.59 - 9.4
FMN
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.8 - 1028
FMN
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.55
AMP
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pH 5.0, 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00752
Pisum sativum cv. Bohatyr
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pH 8.0, 30°C
1.1
pH 8.0, 30°C
22750
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pH 5.0, 50°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 8
pH 5.0: about 90% of maximal activity, pH 8.0: about 60% of maximal activity
6 - 8.5
pH 6.0: about 90% of maximal activity, pH 8.5: about 45% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 50
30°C: about 65% of maximal activity, 50°C: about 55% of maximal activity
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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intestinal brush borders
Manually annotated by BRENDA team
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hairy root, epidermis and cortex of the root tip
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
Pisum sativum cv. Bohatyr
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-
Manually annotated by BRENDA team
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intermembrane space
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25700
FMN hydrolase domains of the bifunctional riboflavin kinase/FMN phosphatase, SDS-PAGE
43600
bifunctional riboflavin kinase/FMN phosphatase, gel filtration
59400
Pisum sativum cv. Bohatyr
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
Pisum sativum cv. Bohatyr
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2 * 25000-30000, SDs-PAGE
monomer
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
56
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30 min, 50% residual activity
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
functional overexpression of the individual domains in Escherichia coli establishes that the riboflavin kinase and FMN hydrolase activities reside, respectively, in the C-terminal (AtFMN) and N-terminal (AtFHy) domains of the bifunctional riboflavin kinase/FMN phosphatase (AtFMN/FHy). Riboflavin kinase and FMN hydrolase domains of AtFMN/FHy can be physically separated, with little change in their kinetic properties
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
in Fe-deficient root cultures, FMN hydrolase activity is substantially increased after 3 days, when riboflavin secretion becomes detectable
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