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Ligand FADH2
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Basic Ligand Information
Related pathways
BRENDA
MetaCyc
2,4,5-trichlorophenoxyacetate degradation, 2,4,6-trichlorophenol degradation, 3,5,6-trichloro-2-pyridinol degradation, 4,4'-diapolycopenedioate biosynthesis, 4-hydroxyphenylacetate degradation 
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Show all BRENDA pathways known for FADH2
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open all tablesRoles as Enzyme Ligand
In Vivo Substrate in Enzyme-catalyzed Reactions (58 results)
top
EC NUMBER 
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
styrene + FADH2 + O2 = (S)-2-phenyloxirane + FAD + H2O
715240, 714557, 714187, 713814, 713817, 713820, 712306, 715353, 714587, 714556, 713815, 714558, 713945, 715248, 726776, 767427, 767542, 766017, 766411
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3-hydroxy-9,10-seconandrost-1,3,5(10)-triene-9,17-dione + FADH2 + O2 = 3,4-dihydroxy-9,10-seconandrost-1,3,5(10)-triene-9,17-dione + FAD + H2O
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(3S)-3-amino-3-(3-chloro-4-hydroxyphenyl)propanoyl-[peptidyl-carrier protein SgcC2] + FADH2 + O2 = (3S)-3-amino-3-(3-chloro-4,5-dihydroxyphenyl)propanoyl-[peptidyl-carrier protein SgcC2] + FAD + H2O
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S-((3S)-3-amino-3-(3-chloro-4-hydroxyphenyl)propanoyl)-[peptidyl-carrier protein SgcC2] + FADH2 + O2 = S-((3S)-3-amino-3-(3-chloro-4,5-dihydroxyphenyl)propanoyl)-[peptidyl-carrier protein SgcC2] + FAD + H2O
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3,5,6-trichloropyridin-2-ol + FADH2 + O2 = 3,6-dichloropyridine-2,5-dione + Cl- + FAD + H2O
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3,6-dichloropyridine-2,5-diol + FADH2 + O2 = 6-chloro-3-hydroxypyridine-2,5-dione + Cl- + FAD + H2O
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6-chloropyridine-2,3,5-triol + FADH2 + O2 = 3,6-dihydroxypyridine-2,5-dione + Cl- + FAD + H2O
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2,4,6-trichlorophenol + FADH2 + O2 = 2,6-dichloro-1,4-benzoquinone + Cl- + FAD + H2O
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2,4,6-trichlorophenol + FADH2 + O2 = 2,6-dichlorobenzoquinone + Cl- + FAD + H2O
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2,6-dichlorohydroquinone + FADH2 + O2 = 2-chloro-6-hydroxy-1,4-benzoquinone + Cl- + FAD + H2O
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phenol + FADH2 + O2 = catechol + FAD + H2O
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2-methylpropan-1-amine + FADH2 + O2 = N-(2-methylpropyl)hydroxylamine + FAD + H2O
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4-hydroxyphenylacetate + FADH2 + O2 = 3,4-dihydroxyphenylacetate + FAD + H2O
(4S)-tetracycline + FADH2 + chloride + O2 + H+ = 7-chloro-(4S)-tetracycline + FAD + 2 H2O
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L-tryptophan + FADH2 + bromide + O2 + H+ = 5-bromo-L-tryptophan + FAD + 2 H2O
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L-tryptophan + FADH2 + chloride + O2 + H+ = 5-chloro-L-tryptophan + FAD + 2 H2O
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L-tryptophan + FADH2 + Cl- + O2 + H+ = 5-chloro-L-tryptophan + FAD + 2 H2O
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7-chloro-L-tryptophan + FADH2 + chloride + O2 + H+ = 6,7-dichloro-L-tryptophan + FAD + 2 H2O
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L-tryptophan + FADH2 + bromide + O2 + H+ = 6-bromo-L-tryptophan + FAD + 2 H2O
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L-tryptophan + FADH2 + chloride + O2 + H+ = 6-chloro-L-tryptophan + FAD + 2 H2O
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7-chloro-L-tryptophan + FADH2 + Cl- + O2 + H+ = 6,7-dichloro-L-tryptophan + FAD + 2 H2O
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6-chloro-L-tryptophan + FADH2 + chloride + O2 + H+ = 6,7-dichloro-L-tryptophan + FAD + 2 H2O
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L-tryptophan + FADH2 + chloride + O2 + H+ = 7-chloro-L-tryptophan + FAD + 2 H2O
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S-(3S)-beta-tyrosyl-[peptidyl-carrier-protein SgcC2]-L-cysteine + 2 FADH2 + 2 H+ + Cl- + O2 = S-(S3)-3-chloro-beta-tyrosyl-[peptidyl-carrier-protein SgcC2]-L-cysteine + FAD + 2 H2O
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5,10-methylenetetrahydrofolate + FADH2 = 5-methyltetrahydrofolate + FAD
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5,10-methylenetetrahydrofolate + dUMP + FADH2 + O2 = dTMP + tetrahydrofolate + FAD + H2O2
5,10-methylenetetrahydrofolate + dUMP + FADH2 + O2 = dTMP + tetrahydrofolate + FAD + H2O2
5,10-methylenetetrahydrofolate + dUMP + FADH2 + O2 = dTMP + tetrahydrofolate + FAD + H2O2
5,10-methylenetetrahydrofolate + dUMP + FADH2 = dTMP + tetrahydrofolate + FAD
5,10-methylenetetrahydrofolate + dUMP + FADH2 = dTMP + tetrahydrofolate + FAD
5,10-methylenetetrahydrofolate + dUMP + FADH2 = dTMP + tetrahydrofolate + FAD
5,10-methylenetetrahydrofolate + tRNA containing uridine at position 54 + FADH2 = tetrahydrofolate + tRNA containing ribothymidine at position 54 + FAD
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5,10-methylenetetrahydrofolate + tRNA UpsiC + FADH2 = tetrahydrofolate + tRNA TpsiC + FAD
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In Vivo Product in Enzyme-catalyzed Reactions (48 results)
EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
trans,octacis-decaprenylphospho-beta-D-ribofuranose + FAD = trans,octacis-decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose + FADH2
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trans,octacis-decaprenylphospho-beta-D-ribofuranose + O2 + FAD = trans,octacis-decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose + H2O2 + FADH2
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N2-(D-1,3-dicarboxypropyl)-L-arginine + FAD + H2O = L-arginine + 2-oxoglutarate + FADH2
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Substrate in Enzyme-catalyzed Reactions (316 results)
EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
(1E)-prop-1-en-1-ylbenzene + FADH2 + O2 = (2R,3S)-2-methyl-3-phenyloxirane + FAD + H2O
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(2E)-3-phenylprop-2-en-1-ol + FADH2 + O2 = (3-phenyloxiran-2-yl)methanol + 1-phenylpropane-1,2,3-triol + FAD + H2O
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(2E)-3-phenylprop-2-en-1-yl acetate + FADH2 + O2 = (3-phenyloxiran-2-yl)methyl acetate + 2,3-dihydroxy-3-phenylpropyl acetate + FAD + H2O
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(2R)-2-(but-3-en-1-yl)oxirane + FADH2 + O2 = (2R,2'R)-2,2'-(ethane-1,2-diyl)bis(oxirane) + FAD + H2O
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1,2-dihydronaphthalene + FADH2 + O2 = (1aR,7bS)-1a,2,3,7b-tetrahydronaphtho[1,2-b]oxirene + 3,4-dihydronaphthalen-2(1H)-one + FAD + H2O
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1,2-dihydronaphthalene + FADH2 + O2 = (1R,2R)-1,2,3,4-tetrahydronaphthalene-1,2-diol + FAD + H2O
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1,2-dihydronaphthalene + FADH2 + O2 = (1R,2R)-1,2-dihydronaphthalene-1,2-diol + FAD + H2O
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1-bromo-2-(methylsulfanyl)benzene + FADH2 + O2 = 1-bromo-2-[(R)-methanesulfinyl]benzene + FAD + H2O
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1-bromo-2-ethenylbenzene + FADH2 + O2 = (2S)-2-(2-bromophenyl)oxirane + FAD + H2O
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1-bromo-3-(methylsulfanyl)benzene + FADH2 + O2 = 1-bromo-3-[(R)-methanesulfinyl]benzene + FAD + H2O
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1-bromo-3-ethenylbenzene + FADH2 + O2 = (2S)-2-(3-bromophenyl)oxirane + FAD + H2O
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1-bromo-4-(methylsulfanyl)benzene + FADH2 + O2 = 1-bromo-4-[(R)-methanesulfinyl]benzene + FAD + H2O
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1-bromo-4-ethenylbenzene + FADH2 + O2 = (2S)-2-(4-bromophenyl)oxirane + FAD + H2O
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1-chloro-2-(methylsulfanyl)benzene + FADH2 + O2 = 1-chloro-2-[(R)-methanesulfinyl]benzene + FAD + H2O
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1-chloro-2-ethenylbenzene + FADH2 + O2 = (2S)-2-(2-chlorophenyl)oxirane + FAD + H2O
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1-chloro-3-(methylsulfanyl)benzene + FADH2 + O2 = 1-chloro-3-[(R)-methanesulfinyl]benzene + FAD + H2O
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1-chloro-3-ethenylbenzene + FADH2 + O2 = (2S)-2-(3-chlorophenyl)oxirane + FAD + H2O
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1-chloro-4-(methylsulfanyl)benzene + FADH2 + O2 = 1-chloro-4-[(R)-methanesulfinyl]benzene + FAD + H2O
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1-chloro-4-ethenylbenzene + FADH2 + O2 = (2S)-2-(4-chlorophenyl)oxirane + FAD + H2O
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1-ethenyl-2-fluorobenzene + FADH2 + O2 = (2S)-2-(2-fluorophenyl)oxirane + FAD + H2O
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1-ethenyl-3-fluorobenzene + FADH2 + O2 = (2S)-2-(3-fluorophenyl)oxirane + FAD + H2O
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1-ethenyl-3-methoxybenzene + FADH2 + O2 = (2S)-2-(3-methoxyphenyl)oxirane + FAD + H2O
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1-ethenyl-3-methylbenzene + FADH2 + O2 = (2S)-2-(3-methylphenyl)oxirane + FAD + H2O
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1-ethenyl-4-fluorobenzene + FADH2 + O2 = (2S)-2-(4-fluorophenyl)oxirane + FAD + H2O
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1-ethenyl-4-methoxybenzene + FADH2 + O2 = (2S)-2-(4-methoxyphenyl)oxirane + FAD + H2O
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1-ethenyl-4-methylbenzene + FADH2 + O2 = (2S)-2-(4-methylphenyl)oxirane + FAD + H2O
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1-methylindole-5-carboxylate + FADH2 + O2 = 1-methyl-3-oxo-2,3-dihydro-1H-indole-5-carboxylic acid + FAD + H2O
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1-phenylprop-2-en-1-ol + FADH2 + O2 = (R)-[(2R)-oxiran-2-yl](phenyl)methanol + FAD + H2O
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1H-indene + FADH2 + O2 = (1aS,6aR)-6,6a-dihydro-1aH-indeno[1,2-b]oxirene + FAD + H2O
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2,3,4,5-tetrahydro-1,1'-biphenyl + FADH2 + O2 = (1S)-1-phenyl-7-oxabicyclo[4.1.0]heptane + FAD + H2O
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2-chlorostyrene + FADH2 + O2 = (2S)-2-(2-chlorophenyl)oxirane + FAD + H2O
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3-chlorostyrene + FADH2 + O2 = (2S)-2-(3-chlorophenyl)oxirane + FAD + H2O
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4-chlorostyrene + FADH2 + O2 = (2S)-2-(4-chlorophenyl)oxirane + FAD + H2O
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4-ethenyl-2,3-dihydro-1-benzofuran + FADH2 + O2 = 4-[(2S)-oxiran-2-yl]-2,3-dihydro-1-benzofuran + FAD + H2O
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7-azaindole + FADH2 + O2 = 1,2-dihydro-3H-pyrrolo[2,3-b]pyridin-3-one + FAD + H2O
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indene + FADH2 + O2 = (1aS,6aR)-6,6a-dihydro-1aH-indeno[1,2-b]oxirene + 1,3-dihydro-2H-inden-2-one + FAD + H2O
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methyl (2E)-3-phenylprop-2-enoate + FADH2 + O2 = methyl 3-phenyloxirane-2-carboxylate + methyl 2,3-dihydroxy-3-phenylpropanoate + FAD + H2O
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styrene + FADH2 + O2 = (S)-2-phenyloxirane + FAD + H2O
715240, 714557, 714187, 713814, 713817, 713820, 712306, 715353, 714587, 714556, 713815, 714558, 713945, 715248, 714256, 713866, 726776, 767427, 767542, 766017, 766411, 766072, 766468, 766617
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styrene + FADH2 + O2 = (S)-styrene oxide + FAD + H2O
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[(1E)-prop-1-en-1-yl]benzene + FADH2 + O2 = (2S,3S)-2-methyl-3-phenyloxirane + FAD + H2O
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[(1E)-prop-1-en-1-yl]benzene + FADH2 + O2 = (3S)-2-methyl-3-phenyloxirane + FAD + H2O
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[(1Z)-prop-1-en-1-yl]benzene + FADH2 + O2 = (2R,3S)-2-methyl-3-phenyloxirane + FAD + H2O
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3-hydroxy-9,10-seconandrost-1,3,5(10)-triene-9,17-dione + FADH2 + O2 = 3,4-dihydroxy-9,10-seconandrost-1,3,5(10)-triene-9,17-dione + FAD + H2O
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(3S)-3-amino-3-(3-chloro-4-hydroxyphenyl)propanoyl-[peptidyl-carrier protein SgcC2] + FADH2 + O2 = (3S)-3-amino-3-(3-chloro-4,5-dihydroxyphenyl)propanoyl-[peptidyl-carrier protein SgcC2] + FAD + H2O
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S-((3S)-3-amino-3-(3-bromo-4-hydroxyphenyl)propanoyl)-[peptidyl-carrier protein SgcC2] + FADH2 + O2 = S-((3S)-3-amino-3-(3-bromo-4,5-dihydroxyphenyl)propanoyl)-[peptidyl-carrier protein SgcC2] + FAD + H2O
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S-((3S)-3-amino-3-(3-chloro-4-hydroxyphenyl)propanoyl)-[peptidyl-carrier protein SgcC2] + FADH2 + O2 = S-((3S)-3-amino-3-(3-chloro-4,5-dihydroxyphenyl)propanoyl)-[peptidyl-carrier protein SgcC2] + FAD + H2O
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S-((3S)-3-amino-3-(3-fluoro-4-hydroxyphenyl)propanoyl)-[peptidyl-carrier protein SgcC2] + FADH2 + O2 = S-((3S)-3-amino-3-(3-fluoro-4,5-dihydroxyphenyl)propanoyl)-[peptidyl-carrier protein SgcC2] + FAD + H2O
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S-((3S)-3-amino-3-(3-iodo-4-hydroxyphenyl)propanoyl)-[peptidyl-carrier protein SgcC2] + FADH2 + O2 = S-((3S)-3-amino-3-(3-iodo-4,5-dihydroxyphenyl)propanoyl)-[peptidyl-carrier protein SgcC2] + FAD + H2O
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S-((3S)-3-amino-3-(3-methyl-4-hydroxyphenyl)propanoyl)-[peptidyl-carrier protein SgcC2] + FADH2 + O2 = S-((3S)-3-amino-3-(3-methyl-4,5-dihydroxyphenyl)propanoyl)-[peptidyl-carrier protein SgcC2] + FAD + H2O
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3,5,6-trichloropyridin-2-ol + FADH2 + O2 = 3,6-dichloropyridine-2,5-dione + Cl- + FAD + H2O
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3,6-dichloropyridine-2,5-diol + FADH2 + O2 = 6-chloro-3-hydroxypyridine-2,5-dione + Cl- + FAD + H2O
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6-chloropyridine-2,3,5-triol + FADH2 + O2 = 3,6-dihydroxypyridine-2,5-dione + Cl- + FAD + H2O
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2,4,6-trichlorophenol + FADH2 + O2 = 2,6-dichloro-1,4-benzoquinone + Cl- + FAD + H2O
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2,4,6-trichlorophenol + FADH2 + O2 = 2,6-dichlorobenzoquinone + Cl- + FAD + H2O
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2,6-dichlorohydroquinone + FADH2 + O2 = 2-chloro-6-hydroxy-1,4-benzoquinone + Cl- + FAD + H2O
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2,6-dichlorophenol + FADH2 + O2 = 2,6-dichlorohydroquinone + FAD + H2O
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2-bromo-4-chlorophenol + FADH2 + O2 = 1,2,4-benzenetriol + Br- + Cl- + FAD + H2O
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2-chloro-4-nitrophenol + FADH2 + O2 = 1,2,4-benzenetriol + NH3 + Cl- + FAD + H2O
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phenol + FADH2 + O2 = catechol + FAD + H2O
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dibenzothiophene + 2 FADH2 + 2 O2 = dibenzothiophene-5,5-dioxide + 2 FAD + 2 H2O
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2-methylpropan-1-amine + FADH2 + O2 = N-(2-methylpropyl)hydroxylamine + FAD + H2O
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ethylenediaminetetraacetate + 2 FADH2 + 2 O2 = ethylenediamine-N,N'-diacetate + 2 glyoxylate + 2 FAD + 2 H2O
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3-(3,4-dihydroxyphenyl)-propanoic acid + FADH2 + O2 = 3-(3,4,5-trihydroxyphenyl)-propanoic acid + FAD + H2O
3-(4-hydroxyphenyl)-propanoic acid + FADH2 + O2 = 3-(3,4-dihydroxyphenyl)-propanoic acid + FAD + H2O
4-hydroxyphenylacetate + FADH2 + O2 = 3,4-dihydroxyphenylacetate + FAD + H2O
caffeic acid + FADH2 + O2 = 3,4,5-trihydroxycinnamic acid + FAD + H2O
(4S)-tetracycline + FADH2 + chloride + O2 + H+ = 7-chloro-(4S)-tetracycline + FAD + 2 H2O
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1H-pyrrole-2-carbonyl-[PltL peptidyl-carrier protein] + 2 FADH2 + 2 bromide + 2 O2 = 4,5-dibromo-1H-pyrrole-2-carbonyl-[PltL peptidyl-carrier protein] + 2 FAD + 4 H2O
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1H-pyrrole-2-carbonyl-[PltL peptidyl-carrier protein] + 2 FADH2 + 2 chloride + 2 O2 = 4,5-dichloro-1H-pyrrole-2-carbonyl-[PltL peptidyl-carrier protein] + 2 FAD + 4 H2O
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1H-pyrrole-2-carbonyl-[PltL peptidyl-carrier protein] + FADH2 + chloride + O2 = 5-chloro-1H-pyrrole-2-carbonyl-[PltL peptidyl-carrier protein] + FAD + 2 H2O
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5-chloro-1H-pyrrole-2-carbonyl-[PltL peptidyl-carrier protein] + FADH2 + chloride + O2 = 4,5-dichloro-1H-pyrrole-2-carbonyl-[PltL peptidyl-carrier protein] + FAD + H2O
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1H-pyrrole-2-carbonyl-[Bmp1 peptidyl-carrier protein] + 3 FADH2 + 3 bromide + 3 O2 = 3,4,5-tribromo-1H-pyrrole-2-carbonyl-[Bmp1 peptidyl-carrier protein] + 3 FAD + 6 H2O
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1H-pyrrole-2-carbonyl-[Bmp1 peptidyl-carrier protein] + FADH2 + bromide + O2 = 5-bromo-1H-pyrrole-2-carbonyl-[Bmp1 peptidyl-carrier protein] + FAD + 2 H2O
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4,5-dibromo-1H-pyrrole-2-carbonyl-[Bmp1 peptidyl-carrier protein] + FADH2 + bromide + O2 = 3,4,5-tribromo-1H-pyrrole-2-carbonyl-[Bmp1 peptidyl-carrier protein] + FAD + 2 H2O
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5-bromo-1H-pyrrole-2-carbonyl-[Bmp1 peptidyl-carrier protein] + FADH2 + bromide + O2 = 4,5-dibromo-1H-pyrrole-2-carbonyl-[Bmp1 peptidyl-carrier protein] + FAD + 2 H2O
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3-indolepropionate + FADH2 + chloride + O2 + H+ = 6-chloro-3-indolepropionate + 5-chloro-3-indolepropionate + FAD + 2 H2O
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5-hydroxy-L-tryptophan + FADH2 + chloride + O2 + H+ = 7-chloro-5-hydroxy-L-tryptophan + FAD + 2 H2O
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7-chloro-L-tryptophan + FADH2 + chloride + O2 + H+ = 5,7-dichloro-L-tryptophan + FAD + 2 H2O
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anthranilamide + FADH2 + chloride + O2 + H+ = 5-chloro-anthranilamide + FAD + 2 H2O
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indole-3-acetamide + FADH2 + chloride + O2 + H+ = 5-chloro-indole-3-acetamide + FAD + 2 H2O
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indole-3-acetamide + FADH2 + chloride + O2 + H+ = 5-chloroindole-3-acetamide + FAD + 2 H2O
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indole-3-acetic acid + FADH2 + chloride + O2 + H+ = 5-chloroindole-3-acetic acid + FAD + 2 H2O
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indole-3-acetonitrile + FADH2 + chloride + O2 + H+ = 5-chloro-indole-3-acetonitrile + FAD + 2 H2O
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indole-3-acetonitrile + FADH2 + chloride + O2 + H+ = 5-chloroindole-3-acetonitrile + FAD + 2 H2O
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indole-3-ethanol + FADH2 + chloride + O2 + H+ = 5-chloro-indole-3-ethanol + FAD + 2 H2O
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indole-3-ethanol + FADH2 + chloride + O2 + H+ = 5-chloroindole-3-ethanol + FAD + 2 H2O
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L-tryptophan + FADH2 + Br- + O2 + H+ = 5-bromo-L-tryptophan + FAD + 2 H2O
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L-tryptophan + FADH2 + bromide + O2 + H+ = 5-bromo-L-tryptophan + FAD + 2 H2O
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L-tryptophan + FADH2 + chloride + O2 + H+ = 5-chloro-L-tryptophan + FAD + 2 H2O
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L-tryptophan + FADH2 + Cl- + O2 + H+ = 5-chloro-L-tryptophan + FAD + 2 H2O
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lantibiotic NAI-107-[tryptophan] + FADH2 + Cl- + O2 + H+ = lantibiotic NAI-107-[5-chlorotryptophan] + FAD + 2 H2O
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N-phenylanthranilate + FADH2 + chloride + O2 + H+ = 5-chloro-N-phenylanthranilate + FAD + 2 H2O
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3-indolepropionate + FADH2 + chloride + O2 + H+ = 6-chloro-3-indolepropionate + 5-chloro-3-indolepropionate + FAD + 2 H2O
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7-chloro-L-tryptophan + FADH2 + chloride + O2 + H+ = 6,7-dichloro-L-tryptophan + FAD + 2 H2O
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anthranilamide + FADH2 + chloride + O2 + H+ = 5-chloro-anthranilamide + FAD + 2 H2O
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L-tryptophan + FADH2 + bromide + O2 + H+ = 6-bromo-L-tryptophan + 5-bromo-L-tryptophan + FAD + 2 H2O
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L-tryptophan + FADH2 + bromide + O2 + H+ = 6-bromo-L-tryptophan + FAD + 2 H2O
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L-tryptophan + FADH2 + chloride + O2 + H+ = 6-chloro-L-tryptophan + FAD + 2 H2O
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N-methyl-L-tryptophan + FADH2 + chloride + O2 + H+ = 6-chloro-N-methyl-L-tryptophan + FAD + 2 H2O
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N-methyltryptophan + FADH2 + chloride + O2 + H+ = 6-chloro-N-methyltryptophan + FAD + 2 H2O
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N-phenylanthranilate + FADH2 + chloride + O2 + H+ = 5-chloro-N-phenylanthranilate + FAD + 2 H2O
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7-chloro-L-tryptophan + FADH2 + Cl- + O2 + H+ = 6,7-dichloro-L-tryptophan + FAD + 2 H2O
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5-amino-L-tryptophan + FADH2 + chloride + O2 + H+ = 7-chloro-5-amino-L-tryptophan + FAD + 2 H2O
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5-bromo-L-tryptophan + FADH2 + chloride + O2 + H+ = 7-chloro-5-bromo-L-tryptophan + FAD + 2 H2O
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5-fluoro-L-tryptophan + FADH2 + chloride + O2 + H+ = 7-chloro-5-fluoro-L-tryptophan + FAD + 2 H2O
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5-hydroxy-L-tryptophan + FADH2 + chloride + O2 + H+ = 7-chloro-5-hydroxy-L-tryptophan + FAD + 2 H2O
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5-methyl-L-tryptophan + FADH2 + chloride + O2 + H+ = 7-chloro-5-methyl-L-tryptophan + FAD + 2 H2O
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6-chloro-L-tryptophan + FADH2 + chloride + O2 + H+ = 6,7-dichloro-L-tryptophan + FAD + 2 H2O
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L-tryptophan + FADH2 + bromide + O2 + H+ = 7-bromo-L-tryptophan + FAD + 2 H2O
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L-tryptophan + FADH2 + chloride + O2 + H+ = 7-chloro-L-tryptophan + FAD + 2 H2O
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L-tryptophan + FADH2 + Cl- + O2 + H+ = 7-chloro-L-tryptophan + FAD + H2O
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2-methylindole + FADH2 + bromide + O2 + H+ = 2-methyl-3-bromoindole + FAD + 2 H2O
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3-methylindole + FADH2 + bromide + O2 + H+ = 3-methyl-2-bromoindole + FAD + 2 H2O
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5-cyanoindole + FADH2 + bromide + O2 + H+ = 5-cyano-3-bromoindole + FAD + 2 H2O
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5-fluoroindole + FADH2 + bromide + O2 + H+ = 5-fluoro-3-bromoindole + FAD + 2 H2O
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5-hydroxyindole + FADH2 + bromide + O2 + H+ = 5-hydroxy-3-bromoindole + FAD + 2 H2O
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5-methylindole + FADH2 + bromide + O2 + H+ = 5-methyl-3-bromoindole + FAD + 2 H2O
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5-nitroindole + FADH2 + bromide + O2 + H+ = 5-nitro-3-bromoindole + FAD + 2 H2O
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indole-2-carboxylic acid + FADH2 + bromide + O2 + H+ = 3-bromoindole-2-carboxylic acid + FAD + 2 H2O
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S-(3R)-beta-tyrosyl-[peptidyl-carrier-protein SgcC2]-L-cysteine + 2 FADH2 + 2 H+ + Cl- + O2 = S-(3R)-3-chloro-beta-tyrosyl-[peptidyl-carrier-protein SgcC2]-L-cysteine + FAD + 2 H2O
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S-(3S)-beta-tyrosyl-[peptidyl-carrier-protein SgcC2]-L-cysteine + 2 FADH2 + 2 H+ + Br- + O2 = S-(3S)-3-bromo-beta-tyrosyl-[peptidyl-carrier-protein SgcC2]-L-cysteine + FAD + 2 H2O
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S-(3S)-beta-tyrosyl-[peptidyl-carrier-protein SgcC2]-L-cysteine + 2 FADH2 + 2 H+ + Cl- + O2 = S-(3S)-3-chloro-beta-tyrosyl-[peptidyl-carrier-protein SgcC2]-L-cysteine + FAD + 2 H2O
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S-(3S)-beta-tyrosyl-[peptidyl-carrier-protein SgcC2]-L-cysteine + 2 FADH2 + 2 H+ + Cl- + O2 = S-(S3)-3-chloro-beta-tyrosyl-[peptidyl-carrier-protein SgcC2]-L-cysteine + FAD + 2 H2O
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5,10-methylenetetrahydrofolate + FADH2 = 5-methyltetrahydrofolate + FAD
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5,10-methylenetetrahydrofolate + dUMP + FADH2 + O2 = dTMP + tetrahydrofolate + FAD + H2O2
5,10-methylenetetrahydrofolate + dUMP + FADH2 + O2 = dTMP + tetrahydrofolate + FAD + H2O2
5,10-methylenetetrahydrofolate + dUMP + FADH2 + O2 = dTMP + tetrahydrofolate + FAD + H2O2
5,10-methylenetetrahydrofolate + dUMP + FADH2 = dTMP + tetrahydrofolate + FAD
5,10-methylenetetrahydrofolate + dUMP + FADH2 = dTMP + tetrahydrofolate + FAD
5,10-methylenetetrahydrofolate + dUMP + FADH2 = dTMP + tetrahydrofolate + FAD
5,10-methylenetetrahydrofolate + tRNA containing uridine at position 54 + FADH2 = tetrahydrofolate + tRNA containing ribothymidine at position 54 + FAD
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5,10-methylenetetrahydrofolate + tRNA UpsiC + FADH2 = tetrahydrofolate + tRNA TpsiC + FAD
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5,10-methylenetetrahydrofolate + uracil54 in tRNA + FADH2 = tetrahydrofolate + 5-methyluracil54 in tRNA + FAD
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N5,N10-methylenetetrahydrofolate + tRNA containing uridine at position 54 + FADH2 = tetrahydrofolate + tRNA containing ribothymidine at position 54 + FAD
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5,10-methylentetrahydrofolate + uracil1939 in 23S rRNA + FADH2 = tetrahydrofolate + 5-methyluracil1939 in 23S rRNA + FAD
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Product in Enzyme-catalyzed Reactions (124 results)
EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
(2Z,6E)-farnesylphosphoryl-beta-D-ribofuranose + FAD = (2Z,6E)-farnesylphosphoryl-D-beta-D-erythro-pentofuranosid-2-ulose + FADH2
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trans,octacis-decaprenylphospho-beta-D-ribofuranose + FAD = trans,octacis-decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose + FADH2
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trans,octacis-decaprenylphospho-beta-D-ribofuranose + O2 + FAD = trans,octacis-decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose + H2O2 + FADH2
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trans,octacis-decaprenylphospho-beta-D-ribofuranose + resazurin + FAD = trans,octacis-decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose + resorufin + FADH2
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3,4-dihydroxyphenylacetate + FAD + H2O = 4-hydroxyphenylacetate + FADH2 + O2
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9alpha-hydroxy-4-androstene-3,17-dione + FAD = 9alpha-hydroxy-1,4-androstadiene-3,17-dione + FADH2
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D-histidine + H2O + FAD = 3-(1H-imidazol-4-yl)-2-oxopropanoate + NH3 + FADH2
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N2-(D-1,3-dicarboxypropyl)-L-arginine + FAD + H2O = L-arginine + 2-oxoglutarate + FADH2
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Enzyme Cofactor/Cosubstrate (318 results)
EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
direct electrochemical regeneration of FADH2 to substitute for the complex native regeneration cycle including StyB and NADH
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flavin binding and redox equilibria are tightly coupled such that reduced FAD binds apo NSMOA about 8000times more tightly than the oxidized coenzyme
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no epoxidation activity is observed for the StyAB system when FAD is replaced by FMN or riboflavin. At a FAD concentration exceeding 0.015 mM, the styrene oxide formation rate decreases
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StyA1 is not active with free FADH2 and recognizes StyA2B as its natural partner. FADH2-induced activation of StyA1 requires interprotein communication with StyA2B. StyA1/StyA2B is a member of the family of two-component flavin-dependent monooxygenases. StyA1 is the major monooxygenase, and StyA2B functions mainly as a FAD reductase with little oxygenating side activity
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the enzyme is specific for FADH2. No activity with FADH2-dependent monooxygenase (in this case StyA) can be regenerated directly by means of non-native redox catalysts such as [Cp*Rh(bpy)-(H2O)]2+
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the enzyme needs flavin reductase TcpX to supply FADH2 when transforming 3,5,6-trichloropyridin-2-ol
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PheA2 is a single domain homodimeric protein with each FAD-containing subunit being organized around a six-stranded beta-sheet and a capping alpha-helix. The tightly bound FAD prosthetic group binds near the dimer interface, and the re face of the FAD isoalloxazine ring is fully exposed to solvent, binding structure, overview
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contains approximately 1 mol of FAD for each polypeptide chain. The enzyme uses FADH2 as a substrate rather than a cofactor. FADH2 is provided by flavin reductase (NADH)
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bound to the enzyme in vivo, which has a high affinity for FADH2, cosubstrate needs to be protected by the enzyme against oxidation to FAD by O2
used as substrate and cofactor, enzyme binds FADH in absence of 4-hydroxyphenlyacetate and protects it from rapid autoxidation by O2
flavin-dependent halogenase, FAD-binding site structure analysis. A50, S347, T348, and I350 are the key residues found to form stable hydrogen-bonding interactions with the flavin ring moiety of FAD. The backbone carbonyl groups of E346 and P344 interact with the hydroxyl group of FAD. The interaction between hydroxy-FAD and E346 can influence the communication between FAD and Trp-S
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recycling of the reduced cofactor FADH2 requires NADH-dependent flavin reductase RebF
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required, purified enzyme does not contain flavin. FADH2 may be provided by a flavin reductase or by regeneration via the organometallic complex (pentamethylcyclopentadienyl)rhodium-bipyridine
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flavoprotein, reduced acceptor in forward reaction
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the flavin is oxidized after dUMP reacts with 5,10-methylenetetrahydrofolate
the flavin is oxidized after dUMP reacts with 5,10-methylenetetrahydrofolate
the flavin is oxidized after dUMP reacts with 5,10-methylenetetrahydrofolate
using spectroscopic characterization it is shown that TrmFO stabilizes the protonated semiquinone FADH and a catalytic intermediate containing most likely both methylenetetrahydrofolate and an FAD reduced form. TrmFO, in the absence of tRNA, maintains an insulated active site that locks up the methyl donor and protects the reduced forms of the flavin from deleterious oxidative reactions
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computational calculations demonstrate that the localization of the FADH-donor state on the flavin ring enhances the electronic coupling between the flavin and the dimer by permitting shorter electron-transfer pathways to the dimer that have single through-space jumps. Therefore, in photolyase, the photo-excitation itself enhances the electron transfer rate by moving the electron towards the dimer
computational calculations demonstrate that the localization of the FADH-donor state on the flavin ring enhances the electronic coupling between the flavin and the dimer by permitting shorter electron-transfer pathways to the dimer that have single through-space jumps. Therefore, in photolyase, the photo-excitation itself enhances the electron transfer rate by moving the electron towards the dimer
computational calculations demonstrate that the localization of the FADH-donor state on the flavin ring enhances the electronic coupling between the flavin and the dimer by permitting shorter electron-transfer pathways to the dimer that have single through-space jumps. Therefore, in photolyase, the photo-excitation itself enhances the electron transfer rate by moving the electron towards the dimer
computational calculations demonstrate that the localization of the FADH-donor state on the flavin ring enhances the electronic coupling between the flavin and the dimer by permitting shorter electron-transfer pathways to the dimer that have single through-space jumps. Therefore, in photolyase, the photo-excitation itself enhances the electron transfer rate by moving the electron towards the dimer
computational calculations demonstrate that the localization of the FADH-donor state on the flavin ring enhances the electronic coupling between the flavin and the dimer by permitting shorter electron-transfer pathways to the dimer that have single through-space jumps. Therefore, in photolyase, the photo-excitation itself enhances the electron transfer rate by moving the electron towards the dimer
computational calculations demonstrate that the localization of the FADH-donor state on the flavin ring enhances the electronic coupling between the flavin and the dimer by permitting shorter electron-transfer pathways to the dimer that have single through-space jumps. Therefore, in photolyase, the photo-excitation itself enhances the electron transfer rate by moving the electron towards the dimer
computational calculations demonstrate that the localization of the FADH-donor state on the flavin ring enhances the electronic coupling between the flavin and the dimer by permitting shorter electron-transfer pathways to the dimer that have single through-space jumps. Therefore, in photolyase, the photo-excitation itself enhances the electron transfer rate by moving the electron towards the dimer
computational calculations demonstrate that the localization of the FADH-donor state on the flavin ring enhances the electronic coupling between the flavin and the dimer by permitting shorter electron-transfer pathways to the dimer that have single through-space jumps. Therefore, in photolyase, the photo-excitation itself enhances the electron transfer rate by moving the electron towards the dimer
computational calculations demonstrate that the localization of the FADH-donor state on the flavin ring enhances the electronic coupling between the flavin and the dimer by permitting shorter electron-transfer pathways to the dimer that have single through-space jumps. Therefore, in photolyase, the photo-excitation itself enhances the electron transfer rate by moving the electron towards the dimer
computational calculations demonstrate that the localization of the FADH-donor state on the flavin ring enhances the electronic coupling between the flavin and the dimer by permitting shorter electron-transfer pathways to the dimer that have single through-space jumps. Therefore, in photolyase, the photo-excitation itself enhances the electron transfer rate by moving the electron towards the dimer
computational calculations demonstrate that the localization of the FADH-donor state on the flavin ring enhances the electronic coupling between the flavin and the dimer by permitting shorter electron-transfer pathways to the dimer that have single through-space jumps. Therefore, in photolyase, the photo-excitation itself enhances the electron transfer rate by moving the electron towards the dimer
computational calculations demonstrate that the localization of the FADH-donor state on the flavin ring enhances the electronic coupling between the flavin and the dimer by permitting shorter electron-transfer pathways to the dimer that have single through-space jumps. Therefore, in photolyase, the photo-excitation itself enhances the electron transfer rate by moving the electron towards the dimer
electron donation by excited states of enzyme-bound FADH2 is the mechanism of flavin photosensitized dimer repair by DNA photolyase
electron donation by excited states of enzyme-bound FADH2 is the mechanism of flavin photosensitized dimer repair by DNA photolyase
electron donation by excited states of enzyme-bound FADH2 is the mechanism of flavin photosensitized dimer repair by DNA photolyase
electron donation by excited states of enzyme-bound FADH2 is the mechanism of flavin photosensitized dimer repair by DNA photolyase
electron donation by excited states of enzyme-bound FADH2 is the mechanism of flavin photosensitized dimer repair by DNA photolyase
electron donation by excited states of enzyme-bound FADH2 is the mechanism of flavin photosensitized dimer repair by DNA photolyase
electron donation by excited states of enzyme-bound FADH2 is the mechanism of flavin photosensitized dimer repair by DNA photolyase
electron donation by excited states of enzyme-bound FADH2 is the mechanism of flavin photosensitized dimer repair by DNA photolyase
electron donation by excited states of enzyme-bound FADH2 is the mechanism of flavin photosensitized dimer repair by DNA photolyase
electron donation by excited states of enzyme-bound FADH2 is the mechanism of flavin photosensitized dimer repair by DNA photolyase
electron donation by excited states of enzyme-bound FADH2 is the mechanism of flavin photosensitized dimer repair by DNA photolyase
electron donation by excited states of enzyme-bound FADH2 is the mechanism of flavin photosensitized dimer repair by DNA photolyase
enzyme contains FADH2 and a second chromophore. Enzyme with a photodecomposed second chromophore retains full activity
enzyme contains FADH2 and a second chromophore. Enzyme with a photodecomposed second chromophore retains full activity
enzyme contains FADH2 and a second chromophore. Enzyme with a photodecomposed second chromophore retains full activity
enzyme contains FADH2 and a second chromophore. Enzyme with a photodecomposed second chromophore retains full activity
enzyme contains FADH2 and a second chromophore. Enzyme with a photodecomposed second chromophore retains full activity
enzyme contains FADH2 and a second chromophore. Enzyme with a photodecomposed second chromophore retains full activity
enzyme contains FADH2 and a second chromophore. Enzyme with a photodecomposed second chromophore retains full activity
enzyme contains FADH2 and a second chromophore. Enzyme with a photodecomposed second chromophore retains full activity
enzyme contains FADH2 and a second chromophore. Enzyme with a photodecomposed second chromophore retains full activity
enzyme contains FADH2 and a second chromophore. Enzyme with a photodecomposed second chromophore retains full activity
enzyme contains FADH2 and a second chromophore. Enzyme with a photodecomposed second chromophore retains full activity
enzyme contains FADH2 and a second chromophore. Enzyme with a photodecomposed second chromophore retains full activity
heterogeneous dynamics continuously tune local configurations to optimize photolyase's function through resonance energy transfer from the antenna to the cofactor for energy efficiency and then electron transfer between the cofactor and the substrate for repair of damaged DNA
heterogeneous dynamics continuously tune local configurations to optimize photolyase's function through resonance energy transfer from the antenna to the cofactor for energy efficiency and then electron transfer between the cofactor and the substrate for repair of damaged DNA
heterogeneous dynamics continuously tune local configurations to optimize photolyase's function through resonance energy transfer from the antenna to the cofactor for energy efficiency and then electron transfer between the cofactor and the substrate for repair of damaged DNA
heterogeneous dynamics continuously tune local configurations to optimize photolyase's function through resonance energy transfer from the antenna to the cofactor for energy efficiency and then electron transfer between the cofactor and the substrate for repair of damaged DNA
heterogeneous dynamics continuously tune local configurations to optimize photolyase's function through resonance energy transfer from the antenna to the cofactor for energy efficiency and then electron transfer between the cofactor and the substrate for repair of damaged DNA
heterogeneous dynamics continuously tune local configurations to optimize photolyase's function through resonance energy transfer from the antenna to the cofactor for energy efficiency and then electron transfer between the cofactor and the substrate for repair of damaged DNA
heterogeneous dynamics continuously tune local configurations to optimize photolyase's function through resonance energy transfer from the antenna to the cofactor for energy efficiency and then electron transfer between the cofactor and the substrate for repair of damaged DNA
heterogeneous dynamics continuously tune local configurations to optimize photolyase's function through resonance energy transfer from the antenna to the cofactor for energy efficiency and then electron transfer between the cofactor and the substrate for repair of damaged DNA
heterogeneous dynamics continuously tune local configurations to optimize photolyase's function through resonance energy transfer from the antenna to the cofactor for energy efficiency and then electron transfer between the cofactor and the substrate for repair of damaged DNA
heterogeneous dynamics continuously tune local configurations to optimize photolyase's function through resonance energy transfer from the antenna to the cofactor for energy efficiency and then electron transfer between the cofactor and the substrate for repair of damaged DNA
heterogeneous dynamics continuously tune local configurations to optimize photolyase's function through resonance energy transfer from the antenna to the cofactor for energy efficiency and then electron transfer between the cofactor and the substrate for repair of damaged DNA
heterogeneous dynamics continuously tune local configurations to optimize photolyase's function through resonance energy transfer from the antenna to the cofactor for energy efficiency and then electron transfer between the cofactor and the substrate for repair of damaged DNA
photoreduction of FADH proceeds along the conserved tryptophan triad W306-W359-W382
photoreduction of FADH proceeds along the conserved tryptophan triad W306-W359-W382
photoreduction of FADH proceeds along the conserved tryptophan triad W306-W359-W382
photoreduction of FADH proceeds along the conserved tryptophan triad W306-W359-W382
photoreduction of FADH proceeds along the conserved tryptophan triad W306-W359-W382
photoreduction of FADH proceeds along the conserved tryptophan triad W306-W359-W382
photoreduction of FADH proceeds along the conserved tryptophan triad W306-W359-W382
photoreduction of FADH proceeds along the conserved tryptophan triad W306-W359-W382
photoreduction of FADH proceeds along the conserved tryptophan triad W306-W359-W382
photoreduction of FADH proceeds along the conserved tryptophan triad W306-W359-W382
photoreduction of FADH proceeds along the conserved tryptophan triad W306-W359-W382
photoreduction of FADH proceeds along the conserved tryptophan triad W306-W359-W382
purified enzyme contains a stable neutral radical FAD that is not active in dimer repair. Dimer repair observed with the enzyme containing FAD in the radical form at shorter wavelength is probably photoreduction of the radical FAD followed by dimer repair by enzyme-bound FADH2
purified enzyme contains a stable neutral radical FAD that is not active in dimer repair. Dimer repair observed with the enzyme containing FAD in the radical form at shorter wavelength is probably photoreduction of the radical FAD followed by dimer repair by enzyme-bound FADH2
purified enzyme contains a stable neutral radical FAD that is not active in dimer repair. Dimer repair observed with the enzyme containing FAD in the radical form at shorter wavelength is probably photoreduction of the radical FAD followed by dimer repair by enzyme-bound FADH2
purified enzyme contains a stable neutral radical FAD that is not active in dimer repair. Dimer repair observed with the enzyme containing FAD in the radical form at shorter wavelength is probably photoreduction of the radical FAD followed by dimer repair by enzyme-bound FADH2
purified enzyme contains a stable neutral radical FAD that is not active in dimer repair. Dimer repair observed with the enzyme containing FAD in the radical form at shorter wavelength is probably photoreduction of the radical FAD followed by dimer repair by enzyme-bound FADH2
purified enzyme contains a stable neutral radical FAD that is not active in dimer repair. Dimer repair observed with the enzyme containing FAD in the radical form at shorter wavelength is probably photoreduction of the radical FAD followed by dimer repair by enzyme-bound FADH2
purified enzyme contains a stable neutral radical FAD that is not active in dimer repair. Dimer repair observed with the enzyme containing FAD in the radical form at shorter wavelength is probably photoreduction of the radical FAD followed by dimer repair by enzyme-bound FADH2
purified enzyme contains a stable neutral radical FAD that is not active in dimer repair. Dimer repair observed with the enzyme containing FAD in the radical form at shorter wavelength is probably photoreduction of the radical FAD followed by dimer repair by enzyme-bound FADH2
purified enzyme contains a stable neutral radical FAD that is not active in dimer repair. Dimer repair observed with the enzyme containing FAD in the radical form at shorter wavelength is probably photoreduction of the radical FAD followed by dimer repair by enzyme-bound FADH2
purified enzyme contains a stable neutral radical FAD that is not active in dimer repair. Dimer repair observed with the enzyme containing FAD in the radical form at shorter wavelength is probably photoreduction of the radical FAD followed by dimer repair by enzyme-bound FADH2
purified enzyme contains a stable neutral radical FAD that is not active in dimer repair. Dimer repair observed with the enzyme containing FAD in the radical form at shorter wavelength is probably photoreduction of the radical FAD followed by dimer repair by enzyme-bound FADH2
purified enzyme contains a stable neutral radical FAD that is not active in dimer repair. Dimer repair observed with the enzyme containing FAD in the radical form at shorter wavelength is probably photoreduction of the radical FAD followed by dimer repair by enzyme-bound FADH2
results indicate that both charge recombination of the primary charge separation state FADH-W382 and electron transfer from W359 to W382 occur with time constants below 4 ps, considerably faster than the initial W382-FADH electron-transfer step.
results indicate that both charge recombination of the primary charge separation state FADH-W382 and electron transfer from W359 to W382 occur with time constants below 4 ps, considerably faster than the initial W382-FADH electron-transfer step.
results indicate that both charge recombination of the primary charge separation state FADH-W382 and electron transfer from W359 to W382 occur with time constants below 4 ps, considerably faster than the initial W382-FADH electron-transfer step.
results indicate that both charge recombination of the primary charge separation state FADH-W382 and electron transfer from W359 to W382 occur with time constants below 4 ps, considerably faster than the initial W382-FADH electron-transfer step.
results indicate that both charge recombination of the primary charge separation state FADH-W382 and electron transfer from W359 to W382 occur with time constants below 4 ps, considerably faster than the initial W382-FADH electron-transfer step.
results indicate that both charge recombination of the primary charge separation state FADH-W382 and electron transfer from W359 to W382 occur with time constants below 4 ps, considerably faster than the initial W382-FADH electron-transfer step.
results indicate that both charge recombination of the primary charge separation state FADH-W382 and electron transfer from W359 to W382 occur with time constants below 4 ps, considerably faster than the initial W382-FADH electron-transfer step.
results indicate that both charge recombination of the primary charge separation state FADH-W382 and electron transfer from W359 to W382 occur with time constants below 4 ps, considerably faster than the initial W382-FADH electron-transfer step.
results indicate that both charge recombination of the primary charge separation state FADH-W382 and electron transfer from W359 to W382 occur with time constants below 4 ps, considerably faster than the initial W382-FADH electron-transfer step.
results indicate that both charge recombination of the primary charge separation state FADH-W382 and electron transfer from W359 to W382 occur with time constants below 4 ps, considerably faster than the initial W382-FADH electron-transfer step.
results indicate that both charge recombination of the primary charge separation state FADH-W382 and electron transfer from W359 to W382 occur with time constants below 4 ps, considerably faster than the initial W382-FADH electron-transfer step.
results indicate that both charge recombination of the primary charge separation state FADH-W382 and electron transfer from W359 to W382 occur with time constants below 4 ps, considerably faster than the initial W382-FADH electron-transfer step.
the isoalloxazine ring is sandwiched between a salt bridge comprising an arginine and an aspartate residue
the isoalloxazine ring is sandwiched between a salt bridge comprising an arginine and an aspartate residue
the isoalloxazine ring is sandwiched between a salt bridge comprising an arginine and an aspartate residue
the isoalloxazine ring is sandwiched between a salt bridge comprising an arginine and an aspartate residue
the isoalloxazine ring is sandwiched between a salt bridge comprising an arginine and an aspartate residue
the isoalloxazine ring is sandwiched between a salt bridge comprising an arginine and an aspartate residue
the isoalloxazine ring is sandwiched between a salt bridge comprising an arginine and an aspartate residue
the isoalloxazine ring is sandwiched between a salt bridge comprising an arginine and an aspartate residue
the isoalloxazine ring is sandwiched between a salt bridge comprising an arginine and an aspartate residue
the isoalloxazine ring is sandwiched between a salt bridge comprising an arginine and an aspartate residue
the isoalloxazine ring is sandwiched between a salt bridge comprising an arginine and an aspartate residue
the isoalloxazine ring is sandwiched between a salt bridge comprising an arginine and an aspartate residue
the isoalloxazine ring is sandwiched between a salt bridge comprising an arginine and an aspartate residue: R344/D372 and short polypeptide stretches: A377-N378/G381-W382. Another conserved interaction is a hydrogen bond formed between the N5 nitrogen of the isoalloxazine group and a conserved asparagine: N378
the isoalloxazine ring is sandwiched between a salt bridge comprising an arginine and an aspartate residue: R344/D372 and short polypeptide stretches: A377-N378/G381-W382. Another conserved interaction is a hydrogen bond formed between the N5 nitrogen of the isoalloxazine group and a conserved asparagine: N378
the isoalloxazine ring is sandwiched between a salt bridge comprising an arginine and an aspartate residue: R344/D372 and short polypeptide stretches: A377-N378/G381-W382. Another conserved interaction is a hydrogen bond formed between the N5 nitrogen of the isoalloxazine group and a conserved asparagine: N378
the isoalloxazine ring is sandwiched between a salt bridge comprising an arginine and an aspartate residue: R344/D372 and short polypeptide stretches: A377-N378/G381-W382. Another conserved interaction is a hydrogen bond formed between the N5 nitrogen of the isoalloxazine group and a conserved asparagine: N378
the isoalloxazine ring is sandwiched between a salt bridge comprising an arginine and an aspartate residue: R344/D372 and short polypeptide stretches: A377-N378/G381-W382. Another conserved interaction is a hydrogen bond formed between the N5 nitrogen of the isoalloxazine group and a conserved asparagine: N378
the isoalloxazine ring is sandwiched between a salt bridge comprising an arginine and an aspartate residue: R344/D372 and short polypeptide stretches: A377-N378/G381-W382. Another conserved interaction is a hydrogen bond formed between the N5 nitrogen of the isoalloxazine group and a conserved asparagine: N378
the isoalloxazine ring is sandwiched between a salt bridge comprising an arginine and an aspartate residue: R344/D372 and short polypeptide stretches: A377-N378/G381-W382. Another conserved interaction is a hydrogen bond formed between the N5 nitrogen of the isoalloxazine group and a conserved asparagine: N378
the isoalloxazine ring is sandwiched between a salt bridge comprising an arginine and an aspartate residue: R344/D372 and short polypeptide stretches: A377-N378/G381-W382. Another conserved interaction is a hydrogen bond formed between the N5 nitrogen of the isoalloxazine group and a conserved asparagine: N378
the isoalloxazine ring is sandwiched between a salt bridge comprising an arginine and an aspartate residue: R344/D372 and short polypeptide stretches: A377-N378/G381-W382. Another conserved interaction is a hydrogen bond formed between the N5 nitrogen of the isoalloxazine group and a conserved asparagine: N378
the isoalloxazine ring is sandwiched between a salt bridge comprising an arginine and an aspartate residue: R344/D372 and short polypeptide stretches: A377-N378/G381-W382. Another conserved interaction is a hydrogen bond formed between the N5 nitrogen of the isoalloxazine group and a conserved asparagine: N378
the isoalloxazine ring is sandwiched between a salt bridge comprising an arginine and an aspartate residue: R344/D372 and short polypeptide stretches: A377-N378/G381-W382. Another conserved interaction is a hydrogen bond formed between the N5 nitrogen of the isoalloxazine group and a conserved asparagine: N378
the isoalloxazine ring is sandwiched between a salt bridge comprising an arginine and an aspartate residue: R344/D372 and short polypeptide stretches: A377-N378/G381-W382. Another conserved interaction is a hydrogen bond formed between the N5 nitrogen of the isoalloxazine group and a conserved asparagine: N378
the isoalloxazine ring is sandwiched between a salt bridge comprising an arginine and an aspartate residue: R352/D380 and short polypeptide stretches: A385-N386/G389-W390. Another conserved interaction is a hydrogen bond formed between the N5 nitrogen of the isoalloxazine group and a conserved asparagine: N386. Mutagenesis and ultrafast kinetic spectroscopy revealed a consecutive chain of three conserved tryptophan residues with the order: Y469 -(?)- W314- W367- W390- FAD(H)
the isoalloxazine ring is sandwiched between a salt bridge comprising an arginine and an aspartate residue: R352/D380 and short polypeptide stretches: A385-N386/G389-W390. Another conserved interaction is a hydrogen bond formed between the N5 nitrogen of the isoalloxazine group and a conserved asparagine: N386. Mutagenesis and ultrafast kinetic spectroscopy revealed a consecutive chain of three conserved tryptophan residues with the order: Y469 -(?)- W314- W367- W390- FAD(H)
the isoalloxazine ring is sandwiched between a salt bridge comprising an arginine and an aspartate residue: R352/D380 and short polypeptide stretches: A385-N386/G389-W390. Another conserved interaction is a hydrogen bond formed between the N5 nitrogen of the isoalloxazine group and a conserved asparagine: N386. Mutagenesis and ultrafast kinetic spectroscopy revealed a consecutive chain of three conserved tryptophan residues with the order: Y469 -(?)- W314- W367- W390- FAD(H)
the isoalloxazine ring is sandwiched between a salt bridge comprising an arginine and an aspartate residue: R352/D380 and short polypeptide stretches: A385-N386/G389-W390. Another conserved interaction is a hydrogen bond formed between the N5 nitrogen of the isoalloxazine group and a conserved asparagine: N386. Mutagenesis and ultrafast kinetic spectroscopy revealed a consecutive chain of three conserved tryptophan residues with the order: Y469 -(?)- W314- W367- W390- FAD(H)
the isoalloxazine ring is sandwiched between a salt bridge comprising an arginine and an aspartate residue: R352/D380 and short polypeptide stretches: A385-N386/G389-W390. Another conserved interaction is a hydrogen bond formed between the N5 nitrogen of the isoalloxazine group and a conserved asparagine: N386. Mutagenesis and ultrafast kinetic spectroscopy revealed a consecutive chain of three conserved tryptophan residues with the order: Y469 -(?)- W314- W367- W390- FAD(H)
the isoalloxazine ring is sandwiched between a salt bridge comprising an arginine and an aspartate residue: R352/D380 and short polypeptide stretches: A385-N386/G389-W390. Another conserved interaction is a hydrogen bond formed between the N5 nitrogen of the isoalloxazine group and a conserved asparagine: N386. Mutagenesis and ultrafast kinetic spectroscopy revealed a consecutive chain of three conserved tryptophan residues with the order: Y469 -(?)- W314- W367- W390- FAD(H)
the isoalloxazine ring is sandwiched between a salt bridge comprising an arginine and an aspartate residue: R352/D380 and short polypeptide stretches: A385-N386/G389-W390. Another conserved interaction is a hydrogen bond formed between the N5 nitrogen of the isoalloxazine group and a conserved asparagine: N386. Mutagenesis and ultrafast kinetic spectroscopy revealed a consecutive chain of three conserved tryptophan residues with the order: Y469 -(?)- W314- W367- W390- FAD(H)
the isoalloxazine ring is sandwiched between a salt bridge comprising an arginine and an aspartate residue: R352/D380 and short polypeptide stretches: A385-N386/G389-W390. Another conserved interaction is a hydrogen bond formed between the N5 nitrogen of the isoalloxazine group and a conserved asparagine: N386. Mutagenesis and ultrafast kinetic spectroscopy revealed a consecutive chain of three conserved tryptophan residues with the order: Y469 -(?)- W314- W367- W390- FAD(H)
the isoalloxazine ring is sandwiched between a salt bridge comprising an arginine and an aspartate residue: R352/D380 and short polypeptide stretches: A385-N386/G389-W390. Another conserved interaction is a hydrogen bond formed between the N5 nitrogen of the isoalloxazine group and a conserved asparagine: N386. Mutagenesis and ultrafast kinetic spectroscopy revealed a consecutive chain of three conserved tryptophan residues with the order: Y469 -(?)- W314- W367- W390- FAD(H)
the isoalloxazine ring is sandwiched between a salt bridge comprising an arginine and an aspartate residue: R352/D380 and short polypeptide stretches: A385-N386/G389-W390. Another conserved interaction is a hydrogen bond formed between the N5 nitrogen of the isoalloxazine group and a conserved asparagine: N386. Mutagenesis and ultrafast kinetic spectroscopy revealed a consecutive chain of three conserved tryptophan residues with the order: Y469 -(?)- W314- W367- W390- FAD(H)
the isoalloxazine ring is sandwiched between a salt bridge comprising an arginine and an aspartate residue: R352/D380 and short polypeptide stretches: A385-N386/G389-W390. Another conserved interaction is a hydrogen bond formed between the N5 nitrogen of the isoalloxazine group and a conserved asparagine: N386. Mutagenesis and ultrafast kinetic spectroscopy revealed a consecutive chain of three conserved tryptophan residues with the order: Y469 -(?)- W314- W367- W390- FAD(H)
the isoalloxazine ring is sandwiched between a salt bridge comprising an arginine and an aspartate residue: R352/D380 and short polypeptide stretches: A385-N386/G389-W390. Another conserved interaction is a hydrogen bond formed between the N5 nitrogen of the isoalloxazine group and a conserved asparagine: N386. Mutagenesis and ultrafast kinetic spectroscopy revealed a consecutive chain of three conserved tryptophan residues with the order: Y469 -(?)- W314- W367- W390- FAD(H)
the photoactivation of FADH- immediately preceding the electron transfer is a key step in the repair mechanism
the photoactivation of FADH- immediately preceding the electron transfer is a key step in the repair mechanism
the photoactivation of FADH- immediately preceding the electron transfer is a key step in the repair mechanism
the photoactivation of FADH- immediately preceding the electron transfer is a key step in the repair mechanism
the photoactivation of FADH- immediately preceding the electron transfer is a key step in the repair mechanism
the photoactivation of FADH- immediately preceding the electron transfer is a key step in the repair mechanism
the photoactivation of FADH- immediately preceding the electron transfer is a key step in the repair mechanism
the photoactivation of FADH- immediately preceding the electron transfer is a key step in the repair mechanism
the photoactivation of FADH- immediately preceding the electron transfer is a key step in the repair mechanism
the photoactivation of FADH- immediately preceding the electron transfer is a key step in the repair mechanism
the photoactivation of FADH- immediately preceding the electron transfer is a key step in the repair mechanism
the photoactivation of FADH- immediately preceding the electron transfer is a key step in the repair mechanism
requires the reduced cofactor for activity. The enzyme requires anaerobic conditions for activity. Km: 0.00055 mM
-
reduced FAD is required for activity. Reconstitution of apoenzyme with other FAD analogues, e.g. with methoxy-FAD, trifluoromethyl-FAD, or chloro-FAD, which are less effective than FAD, overview
reduced FAD is required for activity. Reconstitution of apoenzyme with other FAD analogues, e.g. with methoxy-FAD, trifluoromethyl-FAD, or chloro-FAD, which are less effective than FAD, overview
reduced FAD is required for activity. Reconstitution of apoenzyme with other FAD analogues, e.g. with methoxy-FAD, trifluoromethyl-FAD, or chloro-FAD, which are less effective than FAD, overview
reduced FAD is required for activity. Reconstitution of apoenzyme with other FAD analogues, e.g. with methoxy-FAD, trifluoromethyl-FAD, or chloro-FAD, which are less effective than FAD, overview
reduced FAD is required for activity. Reconstitution of apoenzyme with other FAD analogues, e.g. with methoxy-FAD, trifluoromethyl-FAD, or chloro-FAD, which are less effective than FAD, overview
reduced FAD is required for activity. Reconstitution of apoenzyme with other FAD analogues, e.g. with methoxy-FAD, trifluoromethyl-FAD, or chloro-FAD, which are less effective than FAD, overview
reduced FAD is required for activity. Reconstitution of apoenzyme with other FAD analogues, e.g. with methoxy-FAD, trifluoromethyl-FAD, or chloro-FAD, which are less effective than FAD, overview
reduced FAD is required for activity. Reconstitution of apoenzyme with other FAD analogues, e.g. with methoxy-FAD, trifluoromethyl-FAD, or chloro-FAD, which are less effective than FAD, overview
reduced FAD is required for activity. Reconstitution of apoenzyme with other FAD analogues, e.g. with methoxy-FAD, trifluoromethyl-FAD, or chloro-FAD, which are less effective than FAD, overview
reduced FAD is required for activity. Reconstitution of apoenzyme with other FAD analogues, e.g. with methoxy-FAD, trifluoromethyl-FAD, or chloro-FAD, which are less effective than FAD, overview
reduced FAD is required for activity. Reconstitution of apoenzyme with other FAD analogues, e.g. with methoxy-FAD, trifluoromethyl-FAD, or chloro-FAD, which are less effective than FAD, overview
reduced FAD is required for activity. Reconstitution of apoenzyme with other FAD analogues, e.g. with methoxy-FAD, trifluoromethyl-FAD, or chloro-FAD, which are less effective than FAD, overview
reduced FAD is required for activity. Reconstitution of apoenzyme with other FAD analogues, e.g. with methoxy-FAD, trifluoromethyl-FAD, or chloro-FAD, which are less effective than FAD, overview
reduced FAD is required for activity. Reconstitution of apoenzyme with other FAD analogues, e.g. with methoxy-FAD, trifluoromethyl-FAD, or chloro-FAD, which are less effective than FAD, overview
reduced FAD is required for activity. Reconstitution of apoenzyme with other FAD analogues, e.g. with methoxy-FAD, trifluoromethyl-FAD, or chloro-FAD, which are less effective than FAD, overview
reduced FAD is required for activity. Reconstitution of apoenzyme with other FAD analogues, e.g. with methoxy-FAD, trifluoromethyl-FAD, or chloro-FAD, which are less effective than FAD, overview
reduced FAD is required for activity. Reconstitution of apoenzyme with other FAD analogues, e.g. with methoxy-FAD, trifluoromethyl-FAD, or chloro-FAD, which are less effective than FAD, overview
reduced FAD is required for activity. Reconstitution of apoenzyme with other FAD analogues, e.g. with methoxy-FAD, trifluoromethyl-FAD, or chloro-FAD, which are less effective than FAD, overview
reduced FAD is required for activity. Reconstitution of apoenzyme with other FAD analogues, e.g. with methoxy-FAD, trifluoromethyl-FAD, or chloro-FAD, which are less effective than FAD, overview
reduced FAD is required for activity. Reconstitution of apoenzyme with other FAD analogues, e.g. with methoxy-FAD, trifluoromethyl-FAD, or chloro-FAD, which are less effective than FAD, overview
reduced FAD is required for activity. Reconstitution of apoenzyme with other FAD analogues, e.g. with methoxy-FAD, trifluoromethyl-FAD, or chloro-FAD, which are less effective than FAD, overview
Activator in Enzyme-catalyzed Reactions (50 results)
EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
FADH-/FADH reduction potential of the cryptochrome 1 is significantly higher than that of the photolyase at 164 mV vs normal hydrogen electrode, but it also increases upon substrate binding (to 195 mV vs normal hydrogen electrode) similar to what is observed in photolyase. FADH-/FADH reduction potential is insensitive to ATP binding
FADH-/FADH reduction potential of the cryptochrome 1 is significantly higher than that of the photolyase at 164 mV vs normal hydrogen electrode, but it also increases upon substrate binding (to 195 mV vs normal hydrogen electrode) similar to what is observed in photolyase. FADH-/FADH reduction potential is insensitive to ATP binding
FADH-/FADH reduction potential of the cryptochrome 1 is significantly higher than that of the photolyase at 164 mV vs normal hydrogen electrode, but it also increases upon substrate binding (to 195 mV vs normal hydrogen electrode) similar to what is observed in photolyase. FADH-/FADH reduction potential is insensitive to ATP binding
FADH-/FADH reduction potential of the cryptochrome 1 is significantly higher than that of the photolyase at 164 mV vs normal hydrogen electrode, but it also increases upon substrate binding (to 195 mV vs normal hydrogen electrode) similar to what is observed in photolyase. FADH-/FADH reduction potential is insensitive to ATP binding
FADH-/FADH reduction potential of the cryptochrome 1 is significantly higher than that of the photolyase at 164 mV vs normal hydrogen electrode, but it also increases upon substrate binding (to 195 mV vs normal hydrogen electrode) similar to what is observed in photolyase. FADH-/FADH reduction potential is insensitive to ATP binding
FADH-/FADH reduction potential of the cryptochrome 1 is significantly higher than that of the photolyase at 164 mV vs normal hydrogen electrode, but it also increases upon substrate binding (to 195 mV vs normal hydrogen electrode) similar to what is observed in photolyase. FADH-/FADH reduction potential is insensitive to ATP binding
FADH-/FADH reduction potential of the cryptochrome 1 is significantly higher than that of the photolyase at 164 mV vs normal hydrogen electrode, but it also increases upon substrate binding (to 195 mV vs normal hydrogen electrode) similar to what is observed in photolyase. FADH-/FADH reduction potential is insensitive to ATP binding
FADH-/FADH reduction potential of the cryptochrome 1 is significantly higher than that of the photolyase at 164 mV vs normal hydrogen electrode, but it also increases upon substrate binding (to 195 mV vs normal hydrogen electrode) similar to what is observed in photolyase. FADH-/FADH reduction potential is insensitive to ATP binding
FADH-/FADH reduction potential of the cryptochrome 1 is significantly higher than that of the photolyase at 164 mV vs normal hydrogen electrode, but it also increases upon substrate binding (to 195 mV vs normal hydrogen electrode) similar to what is observed in photolyase. FADH-/FADH reduction potential is insensitive to ATP binding
FADH-/FADH reduction potential of the cryptochrome 1 is significantly higher than that of the photolyase at 164 mV vs normal hydrogen electrode, but it also increases upon substrate binding (to 195 mV vs normal hydrogen electrode) similar to what is observed in photolyase. FADH-/FADH reduction potential is insensitive to ATP binding
FADH-/FADH reduction potential of the cryptochrome 1 is significantly higher than that of the photolyase at 164 mV vs normal hydrogen electrode, but it also increases upon substrate binding (to 195 mV vs normal hydrogen electrode) similar to what is observed in photolyase. FADH-/FADH reduction potential is insensitive to ATP binding
FADH-/FADH reduction potential of the cryptochrome 1 is significantly higher than that of the photolyase at 164 mV vs normal hydrogen electrode, but it also increases upon substrate binding (to 195 mV vs normal hydrogen electrode) similar to what is observed in photolyase. FADH-/FADH reduction potential is insensitive to ATP binding
FADH-/FADH reduction potential of the cryptochrome1 is significantly higher than that of the photolyase at 164 mV vs normal hydrogen electrode, but it also increases upon substrate binding (to 195 mV vs normal hydrogen electrode) similar to what is observed in photolyase. FADH-/FADH reduction potential is insensitive to ATP binding
FADH-/FADH reduction potential of the cryptochrome1 is significantly higher than that of the photolyase at 164 mV vs normal hydrogen electrode, but it also increases upon substrate binding (to 195 mV vs normal hydrogen electrode) similar to what is observed in photolyase. FADH-/FADH reduction potential is insensitive to ATP binding
FADH-/FADH reduction potential of the cryptochrome1 is significantly higher than that of the photolyase at 164 mV vs normal hydrogen electrode, but it also increases upon substrate binding (to 195 mV vs normal hydrogen electrode) similar to what is observed in photolyase. FADH-/FADH reduction potential is insensitive to ATP binding
FADH-/FADH reduction potential of the cryptochrome1 is significantly higher than that of the photolyase at 164 mV vs normal hydrogen electrode, but it also increases upon substrate binding (to 195 mV vs normal hydrogen electrode) similar to what is observed in photolyase. FADH-/FADH reduction potential is insensitive to ATP binding
FADH-/FADH reduction potential of the cryptochrome1 is significantly higher than that of the photolyase at 164 mV vs normal hydrogen electrode, but it also increases upon substrate binding (to 195 mV vs normal hydrogen electrode) similar to what is observed in photolyase. FADH-/FADH reduction potential is insensitive to ATP binding
FADH-/FADH reduction potential of the cryptochrome1 is significantly higher than that of the photolyase at 164 mV vs normal hydrogen electrode, but it also increases upon substrate binding (to 195 mV vs normal hydrogen electrode) similar to what is observed in photolyase. FADH-/FADH reduction potential is insensitive to ATP binding
FADH-/FADH reduction potential of the cryptochrome1 is significantly higher than that of the photolyase at 164 mV vs normal hydrogen electrode, but it also increases upon substrate binding (to 195 mV vs normal hydrogen electrode) similar to what is observed in photolyase. FADH-/FADH reduction potential is insensitive to ATP binding
FADH-/FADH reduction potential of the cryptochrome1 is significantly higher than that of the photolyase at 164 mV vs normal hydrogen electrode, but it also increases upon substrate binding (to 195 mV vs normal hydrogen electrode) similar to what is observed in photolyase. FADH-/FADH reduction potential is insensitive to ATP binding
FADH-/FADH reduction potential of the cryptochrome1 is significantly higher than that of the photolyase at 164 mV vs normal hydrogen electrode, but it also increases upon substrate binding (to 195 mV vs normal hydrogen electrode) similar to what is observed in photolyase. FADH-/FADH reduction potential is insensitive to ATP binding
FADH-/FADH reduction potential of the cryptochrome1 is significantly higher than that of the photolyase at 164 mV vs normal hydrogen electrode, but it also increases upon substrate binding (to 195 mV vs normal hydrogen electrode) similar to what is observed in photolyase. FADH-/FADH reduction potential is insensitive to ATP binding
FADH-/FADH reduction potential of the cryptochrome1 is significantly higher than that of the photolyase at 164 mV vs normal hydrogen electrode, but it also increases upon substrate binding (to 195 mV vs normal hydrogen electrode) similar to what is observed in photolyase. FADH-/FADH reduction potential is insensitive to ATP binding
FADH-/FADH reduction potential of the cryptochrome1 is significantly higher than that of the photolyase at 164 mV vs normal hydrogen electrode, but it also increases upon substrate binding (to 195 mV vs normal hydrogen electrode) similar to what is observed in photolyase. FADH-/FADH reduction potential is insensitive to ATP binding
in wild-type, substantial losses occur prior to formation of the ultimate (FADH- 306TrpH°+) charge pair but that there is no significant kinetic development in the 100 ps-to-10 ns time window. The quantum yield of FADH- W306°+ is at 19%, in reference to the established quantum yield of the long-lived excited state of [Ru(bpy)3]2+
in wild-type, substantial losses occur prior to formation of the ultimate (FADH- 306TrpH°+) charge pair but that there is no significant kinetic development in the 100 ps-to-10 ns time window. The quantum yield of FADH- W306°+ is at 19%, in reference to the established quantum yield of the long-lived excited state of [Ru(bpy)3]2+
in wild-type, substantial losses occur prior to formation of the ultimate (FADH- 306TrpH°+) charge pair but that there is no significant kinetic development in the 100 ps-to-10 ns time window. The quantum yield of FADH- W306°+ is at 19%, in reference to the established quantum yield of the long-lived excited state of [Ru(bpy)3]2+
in wild-type, substantial losses occur prior to formation of the ultimate (FADH- 306TrpH°+) charge pair but that there is no significant kinetic development in the 100 ps-to-10 ns time window. The quantum yield of FADH- W306°+ is at 19%, in reference to the established quantum yield of the long-lived excited state of [Ru(bpy)3]2+
in wild-type, substantial losses occur prior to formation of the ultimate (FADH- 306TrpH°+) charge pair but that there is no significant kinetic development in the 100 ps-to-10 ns time window. The quantum yield of FADH- W306°+ is at 19%, in reference to the established quantum yield of the long-lived excited state of [Ru(bpy)3]2+
in wild-type, substantial losses occur prior to formation of the ultimate (FADH- 306TrpH°+) charge pair but that there is no significant kinetic development in the 100 ps-to-10 ns time window. The quantum yield of FADH- W306°+ is at 19%, in reference to the established quantum yield of the long-lived excited state of [Ru(bpy)3]2+
in wild-type, substantial losses occur prior to formation of the ultimate (FADH- 306TrpH°+) charge pair but that there is no significant kinetic development in the 100 ps-to-10 ns time window. The quantum yield of FADH- W306°+ is at 19%, in reference to the established quantum yield of the long-lived excited state of [Ru(bpy)3]2+
in wild-type, substantial losses occur prior to formation of the ultimate (FADH- 306TrpH°+) charge pair but that there is no significant kinetic development in the 100 ps-to-10 ns time window. The quantum yield of FADH- W306°+ is at 19%, in reference to the established quantum yield of the long-lived excited state of [Ru(bpy)3]2+
in wild-type, substantial losses occur prior to formation of the ultimate (FADH- 306TrpH°+) charge pair but that there is no significant kinetic development in the 100 ps-to-10 ns time window. The quantum yield of FADH- W306°+ is at 19%, in reference to the established quantum yield of the long-lived excited state of [Ru(bpy)3]2+
in wild-type, substantial losses occur prior to formation of the ultimate (FADH- 306TrpH°+) charge pair but that there is no significant kinetic development in the 100 ps-to-10 ns time window. The quantum yield of FADH- W306°+ is at 19%, in reference to the established quantum yield of the long-lived excited state of [Ru(bpy)3]2+
in wild-type, substantial losses occur prior to formation of the ultimate (FADH- 306TrpH°+) charge pair but that there is no significant kinetic development in the 100 ps-to-10 ns time window. The quantum yield of FADH- W306°+ is at 19%, in reference to the established quantum yield of the long-lived excited state of [Ru(bpy)3]2+
in wild-type, substantial losses occur prior to formation of the ultimate (FADH- 306TrpH°+) charge pair but that there is no significant kinetic development in the 100 ps-to-10 ns time window. The quantum yield of FADH- W306°+ is at 19%, in reference to the established quantum yield of the long-lived excited state of [Ru(bpy)3]2+
two pathways for the electron transfer: the direct one, where the electron is transferred from the terminal methyl group of flavin to the carbonyl group of a thymine, and the indirect one, where the electron is ultimately transferred from the amino group of adenine to the carbonyl groups of the thymine dimer. Adenine in photolyase acts as an electrostatic bouncer that shoves the charge flow from flavin toward the DNA lesion that photolyase repairs. Electron transfer occurs from the flavin photolyase cofactor to the cyclobutane ring of DNA, previously formed by light-induced cycloaddition of adjacent pyrimidine bases
two pathways for the electron transfer: the direct one, where the electron is transferred from the terminal methyl group of flavin to the carbonyl group of a thymine, and the indirect one, where the electron is ultimately transferred from the amino group of adenine to the carbonyl groups of the thymine dimer. Adenine in photolyase acts as an electrostatic bouncer that shoves the charge flow from flavin toward the DNA lesion that photolyase repairs. Electron transfer occurs from the flavin photolyase cofactor to the cyclobutane ring of DNA, previously formed by light-induced cycloaddition of adjacent pyrimidine bases
two pathways for the electron transfer: the direct one, where the electron is transferred from the terminal methyl group of flavin to the carbonyl group of a thymine, and the indirect one, where the electron is ultimately transferred from the amino group of adenine to the carbonyl groups of the thymine dimer. Adenine in photolyase acts as an electrostatic bouncer that shoves the charge flow from flavin toward the DNA lesion that photolyase repairs. Electron transfer occurs from the flavin photolyase cofactor to the cyclobutane ring of DNA, previously formed by light-induced cycloaddition of adjacent pyrimidine bases
two pathways for the electron transfer: the direct one, where the electron is transferred from the terminal methyl group of flavin to the carbonyl group of a thymine, and the indirect one, where the electron is ultimately transferred from the amino group of adenine to the carbonyl groups of the thymine dimer. Adenine in photolyase acts as an electrostatic bouncer that shoves the charge flow from flavin toward the DNA lesion that photolyase repairs. Electron transfer occurs from the flavin photolyase cofactor to the cyclobutane ring of DNA, previously formed by light-induced cycloaddition of adjacent pyrimidine bases
two pathways for the electron transfer: the direct one, where the electron is transferred from the terminal methyl group of flavin to the carbonyl group of a thymine, and the indirect one, where the electron is ultimately transferred from the amino group of adenine to the carbonyl groups of the thymine dimer. Adenine in photolyase acts as an electrostatic bouncer that shoves the charge flow from flavin toward the DNA lesion that photolyase repairs. Electron transfer occurs from the flavin photolyase cofactor to the cyclobutane ring of DNA, previously formed by light-induced cycloaddition of adjacent pyrimidine bases
two pathways for the electron transfer: the direct one, where the electron is transferred from the terminal methyl group of flavin to the carbonyl group of a thymine, and the indirect one, where the electron is ultimately transferred from the amino group of adenine to the carbonyl groups of the thymine dimer. Adenine in photolyase acts as an electrostatic bouncer that shoves the charge flow from flavin toward the DNA lesion that photolyase repairs. Electron transfer occurs from the flavin photolyase cofactor to the cyclobutane ring of DNA, previously formed by light-induced cycloaddition of adjacent pyrimidine bases
two pathways for the electron transfer: the direct one, where the electron is transferred from the terminal methyl group of flavin to the carbonyl group of a thymine, and the indirect one, where the electron is ultimately transferred from the amino group of adenine to the carbonyl groups of the thymine dimer. Adenine in photolyase acts as an electrostatic bouncer that shoves the charge flow from flavin toward the DNA lesion that photolyase repairs. Electron transfer occurs from the flavin photolyase cofactor to the cyclobutane ring of DNA, previously formed by light-induced cycloaddition of adjacent pyrimidine bases
two pathways for the electron transfer: the direct one, where the electron is transferred from the terminal methyl group of flavin to the carbonyl group of a thymine, and the indirect one, where the electron is ultimately transferred from the amino group of adenine to the carbonyl groups of the thymine dimer. Adenine in photolyase acts as an electrostatic bouncer that shoves the charge flow from flavin toward the DNA lesion that photolyase repairs. Electron transfer occurs from the flavin photolyase cofactor to the cyclobutane ring of DNA, previously formed by light-induced cycloaddition of adjacent pyrimidine bases
two pathways for the electron transfer: the direct one, where the electron is transferred from the terminal methyl group of flavin to the carbonyl group of a thymine, and the indirect one, where the electron is ultimately transferred from the amino group of adenine to the carbonyl groups of the thymine dimer. Adenine in photolyase acts as an electrostatic bouncer that shoves the charge flow from flavin toward the DNA lesion that photolyase repairs. Electron transfer occurs from the flavin photolyase cofactor to the cyclobutane ring of DNA, previously formed by light-induced cycloaddition of adjacent pyrimidine bases
two pathways for the electron transfer: the direct one, where the electron is transferred from the terminal methyl group of flavin to the carbonyl group of a thymine, and the indirect one, where the electron is ultimately transferred from the amino group of adenine to the carbonyl groups of the thymine dimer. Adenine in photolyase acts as an electrostatic bouncer that shoves the charge flow from flavin toward the DNA lesion that photolyase repairs. Electron transfer occurs from the flavin photolyase cofactor to the cyclobutane ring of DNA, previously formed by light-induced cycloaddition of adjacent pyrimidine bases
two pathways for the electron transfer: the direct one, where the electron is transferred from the terminal methyl group of flavin to the carbonyl group of a thymine, and the indirect one, where the electron is ultimately transferred from the amino group of adenine to the carbonyl groups of the thymine dimer. Adenine in photolyase acts as an electrostatic bouncer that shoves the charge flow from flavin toward the DNA lesion that photolyase repairs. Electron transfer occurs from the flavin photolyase cofactor to the cyclobutane ring of DNA, previously formed by light-induced cycloaddition of adjacent pyrimidine bases
two pathways for the electron transfer: the direct one, where the electron is transferred from the terminal methyl group of flavin to the carbonyl group of a thymine, and the indirect one, where the electron is ultimately transferred from the amino group of adenine to the carbonyl groups of the thymine dimer. Adenine in photolyase acts as an electrostatic bouncer that shoves the charge flow from flavin toward the DNA lesion that photolyase repairs. Electron transfer occurs from the flavin photolyase cofactor to the cyclobutane ring of DNA, previously formed by light-induced cycloaddition of adjacent pyrimidine bases
Inhibitor in Enzyme-catalyzed Reactions (2 results)
3D Structure of Enzyme-Ligand-Complex (PDB) (280 results)
EC NUMBER
ENZYME 3D STRUCTURE
Enzyme Kinetic Parameters
kcat Value (Turnover Number) (2 results)
EC NUMBER
TURNOVER NUMBER [1/S]
TURNOVER NUMBER MAXIMUM [1/S]
COMMENTARY
LITERATURE
KM Value (3 results)
EC NUMBER
KM VALUE [MM]
KM VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
References & Links
Literature References (238)
Links to other databases for FADH2
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