Information on EC 3.6.1.18 - FAD diphosphatase

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

EC NUMBER
COMMENTARY hide
3.6.1.18
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RECOMMENDED NAME
GeneOntology No.
FAD diphosphatase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
FAD + H2O = AMP + FMN
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphorous acid anhydride hydrolysis
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Metabolic pathways
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Riboflavin metabolism
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SYSTEMATIC NAME
IUBMB Comments
FAD nucleotidohydrolase
The plant enzyme also hydrolyses NAD+ and NADH; the animal enzyme hydrolyses NAD+ and CoA at about half of the rate of hydrolysis of FAD. May be identical with EC 3.6.1.9 nucleotide diphosphatase.
CAS REGISTRY NUMBER
COMMENTARY hide
37289-30-8
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
bifunctional FAD diphosphatase/FAD:protein FMN transferase, activity of EC 2.7.1.180
UniProt
Manually annotated by BRENDA team
bifunctional FAD diphosphatase/FAD:protein FMN transferase, activity of EC 2.7.1.180
UniProt
Manually annotated by BRENDA team
mung bean seedlings
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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
ADP + H2O
AMP + phosphate
show the reaction diagram
ATP + H2O
?
show the reaction diagram
CoA + H2O
?
show the reaction diagram
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-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
FAD + H2O
AMP + FMN
show the reaction diagram
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-
-
-
?
FAD + H2O
FMN + AMP
show the reaction diagram
GDP-Man + H2O
Man-1-phosphate + GMP
show the reaction diagram
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EC 3.6.1.9 activity
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?
NAD+ + H2O
NMN + AMP
show the reaction diagram
NADH + H2O
NMNH + AMP
show the reaction diagram
NDP + H2O
?
show the reaction diagram
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cleaves A, G, C, U dinucleotides
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-
?
NTP + H2O
?
show the reaction diagram
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cleaves A, G, C, U trinucleotides
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?
nucleotide sugars + H2O
?
show the reaction diagram
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EC 3.6.1.9 activity
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?
additional information
?
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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 + H2O
AMP + FMN
show the reaction diagram
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-
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?
FAD + H2O
FMN + AMP
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ag2+
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strong inhibition
Cd2+
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inhibitory at high concentrations
Ni2+
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inhibitory at high concentrations
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
2-mercaptoethanol
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8-hydroxyquinoline
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adenine
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slight inhibition
adenosine
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slight inhibition
CDP-choline
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diphosphate
dithiothreitol
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FMN
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no inhibitory effect
GDP-Man
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inhibits FAD diphosphatase activity
IMP
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slight inhibition
molybdate
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slight inhibition at 1 mM
N-ethylmaleimide
NAD+
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very effective inhibitor
NADP+
NaF
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complete inhibition
phosphate
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e.g. KH2PO4
thiamine diphosphate
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ADP
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reactivates aged enzyme, activating up to 0.01 mM
AMP
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activates at concentrations below 0.01 mM
Ca2+
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may replace Mg2+/Mn2+ but with lower catalytic efficiencies
Mg2+
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or Mn2+, most efficiently support FAD hydrolysis
Mn2+
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or Mg2+, most efficiently support FAD hydrolysis
Ni2+
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may replace Mg2+/Mn2+ but with lower catalytic efficiencies
p-chloromercuribenzoate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.001 - 0.33
FAD
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1
N-ethylmaleimide
Saccharomyces cerevisiae
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pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00003
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at pH 7.5 in chloroplasts, in 0.1 M Tris-HCl, 15 mM MgCl2, 1 mM tris(hydroxypropyl)phosphine and 0.05 mM flavin
0.0000384
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at pH 8.5 in chloroplasts, in 0.1 M Tris-HCl, 15 mM MgCl2, 1 mM tris(hydroxypropyl)phosphine and 0.05 mM flavin
0.000343
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at pH 7.5 in mitochondria, in 0.1 M Tris-HCl, 15 mM MgCl2, 1 mM tris(hydroxypropyl)phosphine and 0.05 mM flavin
0.000482
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at pH 8.5 in mitochondria, in 0.1 M Tris-HCl, 15 mM MgCl2, 1 mM tris(hydroxypropyl)phosphine and 0.05 mM flavin
0.098
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purified enzyme
0.458
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purified enzyme
539
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membrane fraction
250000
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purified enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
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in presence of CdCl2 or EDTA
6.5 - 8.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.6 - 5.6
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55% of maximum activity at pH 3.6, 20% of maximum activity at pH 5.6
4 - 8
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60% of maximum activity at pH 4, 20% of maximum activity at pH 8
7 - 10
7
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no activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32700
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analytical untracentrifugation
36593
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1 * 36593, calculated
44000
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more than one enzyme suggested
60000
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gel filtration
70000
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more than one enzyme suggested
74000
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more than one enzyme suggested
135000
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SDS-PAGE of papain-solubilized enzyme
140000
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SDS-PAGE
220000
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SDS-PAGE of detergent-solubilized enzyme
560000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
tetramer
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4 * 140000, SDS-PAGE, gel filtration
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
apo-enzyme and in complex with FAD, AMP and Mn2+, Mg2+, to 1.45-2.3 A resolution. The enzyme adopts the canonical ApbE superfamily fold and has a unique bimetal Mg2+ catalytic center. Isoform TP0796 is a monomer in the crystalline lattice
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
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no inactivation within 120 min
56
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44% loss of activity within 30 min
65
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inactivates
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 12 h, concentration below 0.2 mg/ml, 60% loss of activity, can be restored by adding ADP
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stable at 0-4°C
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partial purification
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D284A
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mutation eliminates the enzyme's dual activities, thereby underscoring the role of Mg2+ in the enzyme-catalyzed reactions
E244A
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critical catalytic residue, may activate a water molecule for nucleophilic attack
H256A
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critical catalytic residue, may neutralize the charge on the leaving group during attack
K165A
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mutation enhances the FAD diphosphatase activity
K165E
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mutation enhances the FAD diphosphatase activity
N55Y
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complete loss of FAD hydrolyase activity, mutation converts the enzyme from an Mg2+-dependent FAD diphosphatase to an FAD-binding protein
R245A
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critical catalytic residue, may neutralize the charge on the leaving group during attack
S240A
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critical catalytic residue, may activate a water molecule for nucleophilic attack
T288A
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mutation in metal binding residue, abolishes FAD diphosphatase activity
D284A
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mutation eliminates the enzyme's dual activities, thereby underscoring the role of Mg2+ in the enzyme-catalyzed reactions
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H256A
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critical catalytic residue, may neutralize the charge on the leaving group during attack
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K165A
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mutation enhances the FAD diphosphatase activity
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S240A
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critical catalytic residue, may activate a water molecule for nucleophilic attack
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T288A
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mutation in metal binding residue, abolishes FAD diphosphatase activity
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Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
reversible denaturation with urea
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