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EC Tree
IUBMB Comments Requires Mn2+ or Co2+. While FAD was the best substrate tested , the enzyme also splits ribonucleoside diphosphate-X compounds in which X is an acyclic or cyclic monosaccharide or derivative bearing an X-OH group that is able to attack internally the proximal phosphorus with the geometry necessary to form a P=X product; either a five-atom monocyclic phosphodiester or a cis-bicyclic phosphodiester-pyranose fusion. The reaction is strongly inhibited by ADP or ATP but is unaffected by the presence of the product, cFMN.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
dAK , Flavine-adenine-dinucleotide cyclase, FMN cyclase, FMN cyclase/dha kinase, Rivoflavin cyclic phosphate synthase, TKFC, triokinase/FMN cyclase,
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Flavine-adenine-dinucleotide cyclase
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Rivoflavin cyclic phosphate synthase
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triokinase/FMN cyclase
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FMN cyclase
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FMN cyclase/dha kinase
bifunctional enzyme
FMN cyclase/dha kinase
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bifunctional enzyme
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FAD = AMP + riboflavin cyclic-4',5'-phosphate
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P-O bond cleavage
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FAD AMP-lyase (riboflavin-cyclic-4',5'-phosphate-forming)
Requires Mn2+ or Co2+. While FAD was the best substrate tested [2], the enzyme also splits ribonucleoside diphosphate-X compounds in which X is an acyclic or cyclic monosaccharide or derivative bearing an X-OH group that is able to attack internally the proximal phosphorus with the geometry necessary to form a P=X product; either a five-atom monocyclic phosphodiester or a cis-bicyclic phosphodiester-pyranose fusion. The reaction is strongly inhibited by ADP or ATP but is unaffected by the presence of the product, cFMN.
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FAD
AMP + riboflavin cyclic-4',5'-phosphate
FAD
AMP + riboflavin cyclic-4',5'-phosphate
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FAD
AMP + riboflavin cyclic-4',5'-phosphate
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FAD
AMP + riboflavin cyclic-4',5'-phosphate
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FAD
AMP + riboflavin cyclic-4',5'-phosphate
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FAD
AMP + riboflavin cyclic-4',5'-phosphate
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FAD
AMP + riboflavin cyclic-4',5'-phosphate
FAD
AMP + riboflavin cyclic-4',5'-phosphate
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FAD
AMP + riboflavin cyclic-4',5'-phosphate
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FAD
AMP + riboflavin cyclic-4',5'-phosphate
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Co2+
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enzyme-activating cation
additional information
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Mg2+ , Ca2+, Zn2+, Ni2+, Cu2+, Fe3+, Li+, Na+, K+ not required for activity
Mn2+
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dependent on
Mn2+
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enzyme-activating cation
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ATP
inhibits the FMN cyclase activity
ATP
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competitive inhibitor
ATP
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inhibits the FMN cyclase activity
FAD
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concentration higher than 0.1 mM
FAD
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concentration higher than 0.3 mM
additional information
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not inhibited by glycerol
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additional information
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twelve nucleotidic compounds tested, not inhibited by FMN, cFMN, dADP, dATP, AMP
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additional information
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thirty-five compounds structurally related to FAD tested
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Cataract
Bi-allelic Variants in TKFC Encoding Triokinase/FMN Cyclase Are Associated with Cataracts and Multisystem Disease.
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0.006 - 0.008
FAD
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0.009
FAD
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Mn2+, pH: 7.5
0.036 - 0.045
FAD
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Mn2+, pH: 8.3
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4.82
FAD
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Mn2+, pH: 7.5
19.3 - 24.1
FAD
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Mn2+, pH: 8.3
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0.01 - 0.02
FMN cyclase activity, lysate supernatant of BL21 cells, pH7.5, 37°C
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p-nitrophenyl-d-TMP as substrate
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7.3
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Co2+ as activating cation
8.5
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Mn2+ as activating cation
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SwissProt
brenda
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brenda
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brenda
female Wistar rats
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brenda
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brenda
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brenda
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brenda
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59400
x * 59400, SDS-PAGE
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-20°C, 1 mg/ml bovine serum albumin
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-80°C, TE: buffer 20 mM Tris-HCl and 0.5 mM EDTA, pH 8.2 at 4°C, 10 months
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chromatography on DEAE-cellulose
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expressed in Escherichia coli BL21 cells
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Fraiz, F.J.; Pinto, R.M.; Costas, M.J.; Avalos, M.; Canales, J.; Cabezas, A.; Cameselle, J.C.
Enzymic formation of riboflavin 4',5'-cyclic phosphate from FAD: evidence for a specific low-Km FMN cyclase in rat liver
Biochem. J.
330
881-888
1998
Rattus norvegicus
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brenda
Cabezas, A.; Pinto, R.M.; Fraiz, F.; Canales, J.; Gonzalez-Santiago, S.; Cameselle, J.C.
Purification, characterization, and substrate and inhibitor structure-activity studies of rat liver FAD-AMP lyase (cyclizing): Preference for FAD and specificity for splitting ribonucleoside diphosphate-X into ribonucleotide and a five-atom cyclic phosphodiester of X, either a monocyclic compound or a cis-bicyclic phosphodiester-pyranose fusion
Biochemistry
40
13710-13722
2001
Rattus norvegicus
brenda
Cabezas, A.; Costas, M.J.; Pinto, R.M.; Couto, A.; Cameselle, J.C.
Identification of human and rat FAD-AMP lyase (cyclic FMN forming) as ATP-dependent dihydroxyacetone kinases
Biochem. Biophys. Res. Commun.
338
1682-1689
2005
Rattus norvegicus, Homo sapiens (Q3LXA3), Homo sapiens
brenda
Rodrigues, J.R.; Couto, A.; Cabezas, A.; Pinto, R.M.; Ribeiro, J.M.; Canales, J.; Costas, M.J.; Cameselle, J.C.
Bifunctional homodimeric triokinase/FMN cyclase: contribution of protein domains to the activities of the human enzyme and molecular dynamics simulation of domain movements
J. Biol. Chem.
289
10620-10636
2014
Homo sapiens
brenda
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