Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
atropine + NADPH + H+ + O2
atropine N-oxide + NADP+ + H2O
-
Substrates: -
Products: -
?
atropine + NADPH + O2
atropine N-oxide + NADP+ + H2O
Substrates: 21% of the activity with monocrotaline
Products: -
?
axillaridine + NADPH + H+ + O2
axillaridine N-oxide + NADP+ + H2O
-
Substrates: -
Products: -
?
axillaridine + NADPH + O2
axillaridine N-oxide + NADP+ + H2O
axillarine + NADPH + H+ + O2
axillarine N-oxide + NADP+ + H2O
-
Substrates: -
Products: -
?
axillarine + NADPH + O2
axillarine N-oxide + NADP+ + H2O
cysteamine + NADPH + H+ + O2
cysteamine N-oxide + NADP+ + H2O
-
Substrates: -
Products: -
?
heliotrine + NADPH + H+ + O2
heliotrine N-oxide + NADP+ + H2O
-
Substrates: -
Products: -
?
heliotrine + NADPH + O2
heliotrine N-oxide + NADP+ + H2O
indicine + NADPH + H+ + O2
indicine N-oxide + NADP+ + H2O
-
Substrates: -
Products: -
?
indicine + NADPH + O2
indicine N-oxide + NADP+ + H2O
lycopsamine + NADPH + O2
lycopsamine N-oxide + NADP+ + H2O
monocrotaline + NADPH + H+ + O2
monocrotaline N-oxide + NADP+ + H2O
-
Substrates: -
Products: -
?
monocrotaline + NADPH + O2
monocrotaline N-oxide + NADP+ + H2O
nicotine + NADPH + H+ + O2
nicotine N-oxide + NADP+ + H2O
-
Substrates: -
Products: -
?
phalaenopsine + NADPH + H+ + O2
phalaenopsine N-oxide + NADP+ + H2O
-
Substrates: -
Products: -
?
phalaenopsine + NADPH + O2
phalaenopsine N-oxide + NADP+ + H2O
Substrates: 19% of the activity with monocrotaline
Products: -
?
retronecine + NADPH + H+ + O2
retronecine N-oxide + NADP+ + H2O
-
Substrates: -
Products: -
?
retrorsine + NADPH + H+ + O2
retrorsine N-oxide + NADP+ + H2O
-
Substrates: -
Products: -
?
retrorsine + NADPH + O2
retrorsine N-oxide + NADP+ + H2O
rinderine + NADPH + H+ + O2
rinderine N-oxide + NADP+ + H2O
-
Substrates: -
Products: -
?
rinderine + NADPH + O2
rinderine N-oxide + NADP+ + H2O
sarracine + NADPH + H+ + O2
sarracine N-oxide + NADP+ + H2O
-
Substrates: -
Products: -
?
senecionine + NADPH + H+ + O2
senecionine N-oxide + NADP+ + H2O
senecionine + NADPH + O2
senecionine N-oxide + NADP+ + H2O
seneciphylline + NADPH + H+ + O2
seneciphylline N-oxide + NADP+ + H2O
-
Substrates: second best substrate
Products: -
?
seneciphylline + NADPH + O2
seneciphylline N-oxide + NADP+ + H2O
senecivernine + NADPH + H+ + O2
senecivernine N-oxide + NADP+ + H2O
-
Substrates: -
Products: -
?
senecivernine + NADPH + O2
senecivernine N-oxide + NADP+ + H2O
triangularine + NADPH + O2
triangularine N-oxide + NADP+ + H2O
-
Substrates: 60% of the activity with senecionine
Products: -
?
additional information
?
-
axillaridine + NADPH + O2
axillaridine N-oxide + NADP+ + H2O
-
Substrates: 79% of the activity with senecionine
Products: -
?
axillaridine + NADPH + O2
axillaridine N-oxide + NADP+ + H2O
-
Substrates: 93% of the activity with senecionine
Products: -
?
axillaridine + NADPH + O2
axillaridine N-oxide + NADP+ + H2O
-
Substrates: 76% of the activity with senecionine
Products: -
?
axillarine + NADPH + O2
axillarine N-oxide + NADP+ + H2O
Substrates: 69% of the activity with monocrotaline
Products: -
?
axillarine + NADPH + O2
axillarine N-oxide + NADP+ + H2O
-
Substrates: 55% of the activity with senecionine
Products: -
?
axillarine + NADPH + O2
axillarine N-oxide + NADP+ + H2O
-
Substrates: 38% of the activity with senecionine
Products: -
?
axillarine + NADPH + O2
axillarine N-oxide + NADP+ + H2O
-
Substrates: 74% of the activity with senecionine
Products: -
?
axillarine + NADPH + O2
axillarine N-oxide + NADP+ + H2O
Substrates: 74% of the activity with senecionine, native enzyme. 83% of the activity with senecionine, recombinant enzyme
Products: -
?
heliotrine + NADPH + O2
heliotrine N-oxide + NADP+ + H2O
Substrates: 49% of the activity with monocrotaline
Products: -
?
heliotrine + NADPH + O2
heliotrine N-oxide + NADP+ + H2O
-
Substrates: 86% of the activity with senecionine
Products: -
?
heliotrine + NADPH + O2
heliotrine N-oxide + NADP+ + H2O
-
Substrates: 115% of the activity with senecionine
Products: -
?
heliotrine + NADPH + O2
heliotrine N-oxide + NADP+ + H2O
-
Substrates: -
Products: -
?
heliotrine + NADPH + O2
heliotrine N-oxide + NADP+ + H2O
-
Substrates: 25% of the activity with senecionine
Products: -
?
heliotrine + NADPH + O2
heliotrine N-oxide + NADP+ + H2O
Substrates: 25% of the activity with senecionine, native enzyme. 49% of the activity with senecionine, recombinant enzyme
Products: -
?
indicine + NADPH + O2
indicine N-oxide + NADP+ + H2O
-
Substrates: 90% of the activity with senecionine
Products: -
?
indicine + NADPH + O2
indicine N-oxide + NADP+ + H2O
-
Substrates: 78% of the activity with senecionine
Products: -
?
indicine + NADPH + O2
indicine N-oxide + NADP+ + H2O
-
Substrates: 35% of the activity with senecionine
Products: -
?
lycopsamine + NADPH + O2
lycopsamine N-oxide + NADP+ + H2O
-
Substrates: 93% of the activity with senecionine
Products: -
?
lycopsamine + NADPH + O2
lycopsamine N-oxide + NADP+ + H2O
-
Substrates: 75% of the activity with senecionine
Products: -
?
lycopsamine + NADPH + O2
lycopsamine N-oxide + NADP+ + H2O
-
Substrates: 20% of the activity with senecionine
Products: -
?
monocrotaline + NADPH + O2
monocrotaline N-oxide + NADP+ + H2O
Substrates: -
Products: -
?
monocrotaline + NADPH + O2
monocrotaline N-oxide + NADP+ + H2O
-
Substrates: 103% of the activity with senecionine
Products: -
?
monocrotaline + NADPH + O2
monocrotaline N-oxide + NADP+ + H2O
-
Substrates: 110% of the activity with senecionine
Products: -
?
monocrotaline + NADPH + O2
monocrotaline N-oxide + NADP+ + H2O
-
Substrates: -
Products: -
?
monocrotaline + NADPH + O2
monocrotaline N-oxide + NADP+ + H2O
-
Substrates: 92% of the activity with senecionine
Products: -
?
monocrotaline + NADPH + O2
monocrotaline N-oxide + NADP+ + H2O
Substrates: 92% of the activity with senecionine, native enzyme. 94% of the activity with senecionine, recombinant enzyme
Products: -
?
retrorsine + NADPH + O2
retrorsine N-oxide + NADP+ + H2O
-
Substrates: as active as senecionine
Products: -
?
retrorsine + NADPH + O2
retrorsine N-oxide + NADP+ + H2O
-
Substrates: 93% of the activity with senecionine
Products: -
?
retrorsine + NADPH + O2
retrorsine N-oxide + NADP+ + H2O
-
Substrates: 97% of the activity with senecionine
Products: -
?
rinderine + NADPH + O2
rinderine N-oxide + NADP+ + H2O
Substrates: 43% of the activity with monocrotaline
Products: -
?
rinderine + NADPH + O2
rinderine N-oxide + NADP+ + H2O
-
Substrates: 79% of the activity with senecionine
Products: -
?
rinderine + NADPH + O2
rinderine N-oxide + NADP+ + H2O
-
Substrates: 81% of the activity with senecionine
Products: -
?
rinderine + NADPH + O2
rinderine N-oxide + NADP+ + H2O
-
Substrates: 23% of the activity with senecionine
Products: -
?
senecionine + NADPH + H+ + O2
senecionine N-oxide + NADP+ + H2O
-
Substrates: -
Products: -
?
senecionine + NADPH + H+ + O2
senecionine N-oxide + NADP+ + H2O
Substrates: -
Products: -
?
senecionine + NADPH + H+ + O2
senecionine N-oxide + NADP+ + H2O
-
Substrates: most efficient substrate
Products: -
?
senecionine + NADPH + O2
senecionine N-oxide + NADP+ + H2O
Substrates: 61% of the activity with monocrotaline
Products: -
?
senecionine + NADPH + O2
senecionine N-oxide + NADP+ + H2O
-
Substrates: -
Products: -
?
senecionine + NADPH + O2
senecionine N-oxide + NADP+ + H2O
-
Substrates: -
Products: -
?
senecionine + NADPH + O2
senecionine N-oxide + NADP+ + H2O
-
Substrates: -
Products: -
?
senecionine + NADPH + O2
senecionine N-oxide + NADP+ + H2O
Substrates: -
Products: -
?
senecionine + NADPH + O2
senecionine N-oxide + NADP+ + H2O
-
Substrates: -
Products: -
?
seneciphylline + NADPH + O2
seneciphylline N-oxide + NADP+ + H2O
Substrates: 59% of the activity with monocrotaline
Products: -
?
seneciphylline + NADPH + O2
seneciphylline N-oxide + NADP+ + H2O
-
Substrates: 117% of the activity with senecionine
Products: -
?
seneciphylline + NADPH + O2
seneciphylline N-oxide + NADP+ + H2O
-
Substrates: 119% of the activity with senecionine
Products: -
?
seneciphylline + NADPH + O2
seneciphylline N-oxide + NADP+ + H2O
-
Substrates: 95% of the activity with senecionine
Products: -
?
seneciphylline + NADPH + O2
seneciphylline N-oxide + NADP+ + H2O
Substrates: 95% of the activity with senecionine, native enzyme. 93% of the activity with senecionine, recombinant enzyme
Products: -
?
senecivernine + NADPH + O2
senecivernine N-oxide + NADP+ + H2O
-
Substrates: 107% of the activity with senecionine
Products: -
?
senecivernine + NADPH + O2
senecivernine N-oxide + NADP+ + H2O
-
Substrates: 113% of the activity with senecionine
Products: -
?
senecivernine + NADPH + O2
senecivernine N-oxide + NADP+ + H2O
-
Substrates: 81% of the activity with senecionine
Products: -
?
additional information
?
-
Substrates: the enzyme shows activity with glutathione (41% of the activity with monocrotaline)
Products: -
?
additional information
?
-
-
Substrates: the enzyme shows activity with glutathione (41% of the activity with monocrotaline)
Products: -
?
additional information
?
-
-
Substrates: the enzyme N-oxidizes only alkaloids with structural elements which are essential for hepatotoxic and genotoxic pyrrolizidine alkaloids, i.e. 1,2-double bond, esterification of the allylic hydroxyl group, presence of a second free or esterified hydroxyl group at carbon 7. No activity with: triangularine, senkirkine, sarracine, supinine, phalaenopsine, retronecine, heliotridine, supinidine, isoretronecanol, nicotine, caffeine, tropane alkaloids, quinolizidine alkaloids, indole alkaloids, isoquinolines and synthetic heterocyclic tertiary amines
Products: -
?
additional information
?
-
-
Substrates: the enzyme N-oxidizes only alkaloids with structural elements which are essential for hepatotoxic and genotoxic pyrrolizidine alkaloids, i.e. 1,2-double bond, esterification of the allylic hydroxyl group, presence of a second free or esterified hydroxyl group at carbon 7. No activity with: triangularine, senkirkine, sarracine, supinine, phalaenopsine, retronecine, heliotridine, supinidine, isoretronecanol, nicotine, caffeine, tropane alkaloids, quinolizidine alkaloids, indole alkaloids, isoquinolines and synthetic heterocyclic tertiary amines
Products: -
?
additional information
?
-
Substrates: the enzyme is highly specific for toxic pyrrolizidine alkaloids. No activity with: senkirkine, dimethylaniline, L-Pro, caffeine, atropine, supinidine, retronecine, phalaenopsine
Products: -
?
additional information
?
-
-
Substrates: the enzyme is highly specific for toxic pyrrolizidine alkaloids. No activity with: senkirkine, dimethylaniline, L-Pro, caffeine, atropine, supinidine, retronecine, phalaenopsine
Products: -
?
additional information
?
-
-
Substrates: the enzyme N-oxidizes only alkaloids with structural elements which are essential for hepatotoxic and genotoxic pyrrolizidine alkaloids, i.e. 1,2-double bond, esterification of the allylic hydroxyl group, presence of a second free or esterified hydroxyl group at carbon 7. No activity with: senkirkine, sarracine, supinine, phalaenopsine, retronecine, heliotridine, supinidine, isoretronecanol, nicotine, caffeine, tropane alkaloids, quinolizidine alkaloids, indole alkaloids, isoquinolines and synthetic heterocyclic tertiary amines
Products: -
?
additional information
?
-
Substrates: the enzyme allows the larvae to feed on pyrrolizidine alkaloid-containing plants and to accumulate predation-deterrent pyrrolizidine alkaloids in the hemolymph
Products: -
?
additional information
?
-
-
Substrates: the enzyme allows the larvae to feed on pyrrolizidine alkaloid-containing plants and to accumulate predation-deterrent pyrrolizidine alkaloids in the hemolymph
Products: -
?
additional information
?
-
-
Substrates: no activity with senkirkine, heliotridine, supinidine, ephedrine, dimethylaniline, L-cysteine, hydroxylamine, and glutathione
Products: -
?
additional information
?
-
Substrates: class B FMOs such as those from Zonocerus variegatus consist of two domains, each of which contains a dinucleotide-binding domain in the form of a Rossmann fold, which is responsible for cofactor binding. In its native state, oxidized FAD is tightly bound to the enzyme as a prosthetic group. NADPH is recruited as a co-substrate and transfers reducing equivalents to FAD. Upon the reaction of reduced FAD by molecular oxygen, a C4a-hydroperoxy-FAD intermediate is formed. This intermediate is capable of inserting one O atom into a substrate compound and ends up as C4a-hydroxy-FAD, which may then release the second O atom as part of a water molecule, restoring the oxidized FAD cofactor. A cocked-gun mechanism has been proposed for the reaction cycle of FMOs, meaning that the activated C4a-hydroperoxy-FAD intermediate can be stabilized within the enzyme until a substrate accesses the active site and is then immediately oxygenated. The presence of NADP+ seems to be crucial for the stabilization of this intermediate and therefore it has to remain bound to the enzyme throughout the whole catalytic cycle, making it the last compound to be released from the enzyme. NADP+ binding structure analysis, overview. The NADP+ cofactor is bound to the GXGXXG motif (residues 191-196) of the smaller structural domain in an extended conformation via hydrogen bonds to its diphosphate moiety. The 2'-phosphate of NADP+ is coordinated by Lys223 and His351. Interactions between the nicotinamide moiety and Phe64 and Arg398 as well as between the ribose moiety and Asn66 further support the binding and positioning of the cofactor. In comparison to the ZvPNO-FAD complex, the presence of NADP+ leads to a small conformational change of helix alpha4 such that it provides additional cofactor stabilization by interactions between a positive partial charge of the helix dipole and the diphosphate of NADP+. The conformational change in the preceding loop region is caused by a flipping alanine, which reduces steric hindrance when binding the NADP+ cofactor. The ribose moiety of NADP+ and Asn66 are supposed to coordinate molecular oxygen and stabilize the C4a-hydroperoxy-FAD intermediate
Products: -
-
additional information
?
-
Substrates: class B FMOs such as those from Zonocerus variegatus consist of two domains, each of which contains a dinucleotide-binding domain in the form of a Rossmann fold, which is responsible for cofactor binding. In its native state, oxidized FAD is tightly bound to the enzyme as a prosthetic group. NADPH is recruited as a co-substrate and transfers reducing equivalents to FAD. Upon the reaction of reduced FAD by molecular oxygen, a C4a-hydroperoxy-FAD intermediate is formed. This intermediate is capable of inserting one O atom into a substrate compound and ends up as C4a-hydroxy-FAD, which may then release the second O atom as part of a water molecule, restoring the oxidized FAD cofactor. A cocked-gun mechanism has been proposed for the reaction cycle of FMOs, meaning that the activated C4a-hydroperoxy-FAD intermediate can be stabilized within the enzyme until a substrate accesses the active site and is then immediately oxygenated. The presence of NADP+ seems to be crucial for the stabilization of this intermediate and therefore it has to remain bound to the enzyme throughout the whole catalytic cycle, making it the last compound to be released from the enzyme. NADP+ binding structure analysis, overview. The NADP+ cofactor is bound to the GXGXXG motif (residues 191-196) of the smaller structural domain in an extended conformation via hydrogen bonds to its diphosphate moiety. The 2'-phosphate of NADP+ is coordinated by Lys223 and His351. Interactions between the nicotinamide moiety and Phe64 and Arg398 as well as between the ribose moiety and Asn66 further support the binding and positioning of the cofactor. In comparison to the ZvPNO-FAD complex, the presence of NADP+ leads to a small conformational change of helix alpha4 such that it provides additional cofactor stabilization by interactions between a positive partial charge of the helix dipole and the diphosphate of NADP+. The conformational change in the preceding loop region is caused by a flipping alanine, which reduces steric hindrance when binding the NADP+ cofactor. The ribose moiety of NADP+ and Asn66 are supposed to coordinate molecular oxygen and stabilize the C4a-hydroperoxy-FAD intermediate
Products: -
-
additional information
?
-
-
Substrates: class B FMOs such as those from Zonocerus variegatus consist of two domains, each of which contains a dinucleotide-binding domain in the form of a Rossmann fold, which is responsible for cofactor binding. In its native state, oxidized FAD is tightly bound to the enzyme as a prosthetic group. NADPH is recruited as a co-substrate and transfers reducing equivalents to FAD. Upon the reaction of reduced FAD by molecular oxygen, a C4a-hydroperoxy-FAD intermediate is formed. This intermediate is capable of inserting one O atom into a substrate compound and ends up as C4a-hydroxy-FAD, which may then release the second O atom as part of a water molecule, restoring the oxidized FAD cofactor. A cocked-gun mechanism has been proposed for the reaction cycle of FMOs, meaning that the activated C4a-hydroperoxy-FAD intermediate can be stabilized within the enzyme until a substrate accesses the active site and is then immediately oxygenated. The presence of NADP+ seems to be crucial for the stabilization of this intermediate and therefore it has to remain bound to the enzyme throughout the whole catalytic cycle, making it the last compound to be released from the enzyme. NADP+ binding structure analysis, overview. The NADP+ cofactor is bound to the GXGXXG motif (residues 191-196) of the smaller structural domain in an extended conformation via hydrogen bonds to its diphosphate moiety. The 2'-phosphate of NADP+ is coordinated by Lys223 and His351. Interactions between the nicotinamide moiety and Phe64 and Arg398 as well as between the ribose moiety and Asn66 further support the binding and positioning of the cofactor. In comparison to the ZvPNO-FAD complex, the presence of NADP+ leads to a small conformational change of helix alpha4 such that it provides additional cofactor stabilization by interactions between a positive partial charge of the helix dipole and the diphosphate of NADP+. The conformational change in the preceding loop region is caused by a flipping alanine, which reduces steric hindrance when binding the NADP+ cofactor. The ribose moiety of NADP+ and Asn66 are supposed to coordinate molecular oxygen and stabilize the C4a-hydroperoxy-FAD intermediate
Products: -
-
additional information
?
-
Substrates: class B FMOs such as those from Zonocerus variegatus consist of two domains, each of which contains a dinucleotide-binding domain in the form of a Rossmann fold, which is responsible for cofactor binding. In its native state, oxidized FAD is tightly bound to the enzyme as a prosthetic group. NADPH is recruited as a co-substrate and transfers reducing equivalents to FAD. Upon the reaction of reduced FAD by molecular oxygen, a C4a-hydroperoxy-FAD intermediate is formed. This intermediate is capable of inserting one O atom into a substrate compound and ends up as C4a-hydroxy-FAD, which may then release the second O atom as part of a water molecule, restoring the oxidized FAD cofactor. A cocked-gun mechanism has been proposed for the reaction cycle of FMOs, meaning that the activated C4a-hydroperoxy-FAD intermediate can be stabilized within the enzyme until a substrate accesses the active site and is then immediately oxygenated. The presence of NADP+ seems to be crucial for the stabilization of this intermediate and therefore it has to remain bound to the enzyme throughout the whole catalytic cycle, making it the last compound to be released from the enzyme. The ribose moiety of NADP+ and Asn66 are supposed to coordinate molecular oxygen and stabilize the C4a-hydroperoxy-FAD intermediate
Products: -
-
additional information
?
-
Substrates: class B FMOs such as those from Zonocerus variegatus consist of two domains, each of which contains a dinucleotide-binding domain in the form of a Rossmann fold, which is responsible for cofactor binding. In its native state, oxidized FAD is tightly bound to the enzyme as a prosthetic group. NADPH is recruited as a co-substrate and transfers reducing equivalents to FAD. Upon the reaction of reduced FAD by molecular oxygen, a C4a-hydroperoxy-FAD intermediate is formed. This intermediate is capable of inserting one O atom into a substrate compound and ends up as C4a-hydroxy-FAD, which may then release the second O atom as part of a water molecule, restoring the oxidized FAD cofactor. A cocked-gun mechanism has been proposed for the reaction cycle of FMOs, meaning that the activated C4a-hydroperoxy-FAD intermediate can be stabilized within the enzyme until a substrate accesses the active site and is then immediately oxygenated. The presence of NADP+ seems to be crucial for the stabilization of this intermediate and therefore it has to remain bound to the enzyme throughout the whole catalytic cycle, making it the last compound to be released from the enzyme. The ribose moiety of NADP+ and Asn66 are supposed to coordinate molecular oxygen and stabilize the C4a-hydroperoxy-FAD intermediate
Products: -
-
additional information
?
-
-
Substrates: class B FMOs such as those from Zonocerus variegatus consist of two domains, each of which contains a dinucleotide-binding domain in the form of a Rossmann fold, which is responsible for cofactor binding. In its native state, oxidized FAD is tightly bound to the enzyme as a prosthetic group. NADPH is recruited as a co-substrate and transfers reducing equivalents to FAD. Upon the reaction of reduced FAD by molecular oxygen, a C4a-hydroperoxy-FAD intermediate is formed. This intermediate is capable of inserting one O atom into a substrate compound and ends up as C4a-hydroxy-FAD, which may then release the second O atom as part of a water molecule, restoring the oxidized FAD cofactor. A cocked-gun mechanism has been proposed for the reaction cycle of FMOs, meaning that the activated C4a-hydroperoxy-FAD intermediate can be stabilized within the enzyme until a substrate accesses the active site and is then immediately oxygenated. The presence of NADP+ seems to be crucial for the stabilization of this intermediate and therefore it has to remain bound to the enzyme throughout the whole catalytic cycle, making it the last compound to be released from the enzyme. The ribose moiety of NADP+ and Asn66 are supposed to coordinate molecular oxygen and stabilize the C4a-hydroperoxy-FAD intermediate
Products: -
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.