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EC Tree
IUBMB Comments 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 , but isoforms specific for FMN also exist .
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
fmn hydrolase, atcpfhy1, fmn phosphohydrolase,
more
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At4g21470
gene name, bifunctional riboflavin kinase/FMN phosphatase
At4g21470
gene name, bifunctional riboflavin kinase/FMN phosphatase
-
AtFMN/FHy
bifunctional riboflavin kinase/FMN phosphatase
AtFMN/FHy
bifunctional riboflavin kinase/FMN phosphatase
-
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FMN + H2O = riboflavin + phosphate
-
-
-
-
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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].
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4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
alpha-D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
25% of the activity with 4-nitrophenyl phosphate
-
-
?
AMP + H2O
adenosine + phosphate
-
47% of the activity with 4-nitrophenyl phosphate
-
-
?
FMN + H2O
riboflavin + phosphate
FMN + H2O
riboflavin + phosphate
-
-
-
?
FMN + H2O
riboflavin + phosphate
-
-
-
?
FMN + H2O
riboflavin + phosphate
high specificity for FMN. The enzyme does not hydrolyze the following substrates: ADP, AMP, ATP, CTP, GTP, IMP, UTP, xanthosine 5'-monophosphate, dATP, glucose 1-phosphate, glucose 6-phosphate, glucose 1,6-bisphosphate, and fructose 1,6-bisphosphate, pyridoxal 5'-phosphate and NADP+
-
-
?
FMN + H2O
riboflavin + phosphate
-
-
-
?
FMN + H2O
riboflavin + phosphate
-
most important physiological substrate, 87% of the activity with 4-nitrophenyl phosphate
-
-
?
FMN + H2O
riboflavin + phosphate
-
-
-
-
?
FMN + H2O
riboflavin + phosphate
Pisum sativum cv. Bohatyr
-
-
-
-
?
FMN + H2O
riboflavin + phosphate
-
-
-
-
?
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FMN + H2O
riboflavin + phosphate
FMN + H2O
riboflavin + phosphate
-
-
-
?
FMN + H2O
riboflavin + phosphate
Pisum sativum cv. Bohatyr
-
-
-
-
?
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Mg2+
required
Mg2+
the FMN hydrolase activity of the bifunctional riboflavin kinase/FMN phosphatase greatly decreases when EDTA replaced Mg2+ in the assays
Mg2+
Pisum sativum cv. Bohatyr
-
required
Mg2+
-
Mg2+ has no effect at pH 5.0, but shows 50% stimulation at pH 8.5
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4-chloromercuribenzoate
-
2 mM, 100% inhibition
5,5'-dithiobis-2-nitrobenzoic acid
-
3 mM, 100% inhibition
AlCl3
-
5 mM, 82% inhibition
Ca2+
-
5 mM, 27% inhibition, 2 mM, 40% inhibition
Cd2+
-
5 mM, 92% inhibition
FeCl3
-
5 mM, 100% inhibition
L-phenylalanine
-
2.5 mM, 10% inhibition
N-ethylmaleimide
-
10 mM, 57% inhibition
sodium dodecylsulfate
-
0.3%, 100% inhibition
Zn2+
-
5 mM, 67% inhibition
EDTA
the FMN hydrolase activity of the bifunctional riboflavin kinase/FMN phosphatase greatly decreases when EDTA replaced Mg2+ in the assays
EDTA
-
10 mM, 100% inhibition
phosphate
the FMN hydrolase activity of the bifunctional riboflavin kinase/FMN phosphatase is inhibited
phosphate
-
10 mM, 54% inhibition
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Tween 20
enzyme activity increases and temperature optimum shifts to 510°C higher temperature in the presence of Tween 20
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0.0008
FMN
pH 7.5, 30°C
1
FMN
-
pH and temperature not specified in the publication, enzyme YigB
2.3
FMN
-
pH and temperature not specified in the publication, enzyme YbjI
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0.59
FMN
pH 8.0, 30°C
6.5
FMN
-
pH and temperature not specified in the publication, enzyme YbjI
9.4
FMN
-
pH and temperature not specified in the publication, enzyme YigB
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2.8
FMN
-
pH and temperature not specified in the publication, enzyme YbjI
9.4
FMN
-
pH and temperature not specified in the publication, enzyme YigB
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0.00752
Pisum sativum cv. Bohatyr
-
pH 8.0, 30°C
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5
-
-
8
assay at
8
Pisum sativum cv. Bohatyr
-
assay at
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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
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30
assay at
30
Pisum sativum cv. Bohatyr
-
assay at
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30 - 50
30°C: about 65% of maximal activity, 50°C: about 55% of maximal activity
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bifunctional riboflavin kinase/FMN phosphatase
UniProt
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
Pisum sativum cv. Bohatyr
-
-
-
brenda
-
-
-
brenda
-
UniProt
brenda
bifunctional riboflavin kinase/FMN phosphatase
UniProt
brenda
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intestinal brush borders
brenda
-
hairy root, epidermis and cortex of the root tip
brenda
-
-
brenda
-
-
brenda
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-
-
brenda
Pisum sativum cv. Bohatyr
-
-
brenda
-
intermembrane space
brenda
-
brenda
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physiological function
-
inhibition of 14C-riboflavin uptake by FMN and FAD in everted rings of rat intestine is directly related to the amount of conversion of these coenzymes to free riboflavin by intestinal enzymes. When FMN and FAD conversion to riboflavin is inhibited by EDTA, competition with 14C-riboflavin for transport is correspondingly decreased, best explained by a sequential process in which hydrolysis of FMN and FAD by enzymes of the intestinal brush border is followed by absorption of free riboflavin
physiological function
-
not only de novo riboflavin synthesis but also the hydrolysis of FMN contributes to riboflavin secretion under conditions of Fe deficiency. Respiration activity is also enhanced after 3 days under Fe deficiency
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FHY1C_ARATH
245
0
27695
Swiss-Prot
Chloroplast (Reliability: 2 )
FHYRK_ARATH
379
0
42110
Swiss-Prot
Secretory Pathway (Reliability: 5 )
A0A3B0M6Y3_9GAMM
185
0
20639
TrEMBL
-
A0A3B1DUA5_9GAMM
237
0
27059
TrEMBL
-
A0A5B6Z361_DAVIN
251
0
27492
TrEMBL
other Location (Reliability: 3 )
A0A5B6Z6C3_DAVIN
253
0
28072
TrEMBL
other Location (Reliability: 3 )
F4HQA8_ARATH
270
0
30619
TrEMBL
-
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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
-
gel filtration
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dimer
Pisum sativum cv. Bohatyr
-
2 * 25000-30000, SDs-PAGE
monomer
1 * 42100, bifunctional riboflavin kinase/FMN phosphatase, SDS-PAGE
monomer
-
1 * 42100, bifunctional riboflavin kinase/FMN phosphatase, SDS-PAGE
-
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56
-
30 min, 50% residual activity
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-
-
-
Pisum sativum cv. Bohatyr
-
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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
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in Fe-deficient root cultures, FMN hydrolase activity is substantially increased after 3 days, when riboflavin secretion becomes detectable
-
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Akiyama, T.; Selhub, J.; Rosenberg, J.H.
FMN phosphatase and FAD pyrophosphatase in rat intestinal brush borders: Role in intestinal absorption of dietary riboflavin
J. Nutr.
112
263-268
1982
Rattus norvegicus
brenda
Barile, M.; Brizio, C.; de Virgilio, C.; Delfine, S.; Quagliariello, E.; Passarella, S.
Flavin adenine dinucleotide and flavin mononucleotide metabolism in rat liver: The occurrence of FAD pyrophosphatase and FMN phosphohydrolase in isolated mitochondria
Eur. J. Biochem.
249
777-785
1997
Rattus norvegicus
brenda
Sandoval, F.J.; Roje, S.
An FMN hydrolase is fused to a riboflavin kinase homolog in plants
J. Biol. Chem.
280
38337-38345
2005
Arabidopsis thaliana (Q84MD8), Arabidopsis thaliana ecotype Columbia (Q84MD8)
brenda
Higa, A.; Khandakar, J.; Mori, Y.; Kitamura, Y.
Increased de novo riboflavin synthesis and hydrolysis of FMN are involved in riboflavin secretion from Hyoscyamus albus hairy roots under iron deficiency
Plant Physiol. Biochem.
58
166-173
2012
Hyoscyamus albus
brenda
Rawat, R.; Sandoval, F.J.; Wei, Z.; Winkler, R.; Roje, S.
An FMN hydrolase of the haloacid dehalogenase superfamily is active in plant chloroplasts
J. Biol. Chem.
286
42091-42098
2011
Pisum sativum cv. Bohatyr, Arabidopsis thaliana (F4HQA8), Arabidopsis thaliana
brenda
Mallik, S.; Dey, M.; Dutta, M.; Ghosh, A.; Bandyopadhyay, D.
Flavin mononucleotide phosphatase from goat liver: A possible target for divalent heavy metal cations
Int. J. Pharm. Pharm. Sci.
6
708-714
2014
Capra hircus
-
brenda
Kuznetsova, E.; Proudfoot, M.; Gonzalez, C.F.; Brown, G.; Omelchenko, M.V.; Borozan, I.; Carmel, L.; Wolf, Y.I.; Mori, H.; Savchenko, A.V.; Arrowsmith, C.H.; Koonin, E.V.; Edwards, A.M.; Yakunin, A.F.
Genome-wide analysis of substrate specificities of the Escherichia coli haloacid dehalogenase-like phosphatase family
J. Biol. Chem.
281
36149-36161
2006
Escherichia coli
brenda
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