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Ligand reduced riboflavin Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Basic Ligand Information Molecular Structure
C1 7 H2 2 N4 O6
reduced riboflavin
UTKDOUCGQVLJIN-QNMSZWNNSA-N
Show all BRENDA pathways known for reduced riboflavin
Roles as Enzyme Ligand
In Vivo Product in Enzyme-catalyzed Reactions (5 results)
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riboflavin + NADPH + H+ = reduced riboflavin + NADP+
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riboflavin + NADPH = reduced riboflavin + NADP+
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riboflavin + NADH + H+ = reduced riboflavin + NAD+
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riboflavin + NADH + H+ = reduced riboflavin + NAD+
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riboflavin + NADPH + H+ = reduced riboflavin + NADP+
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Substrate in Enzyme-catalyzed Reactions (3 results)
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phenol + reduced riboflavin + O2 = catechol + riboflavin + H2O
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dibenzothiophene + 2 reduced riboflavin + 2 O2 = dibenzothiophene-5,5-dioxide + 2 riboflavin + 2 H2O
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adenylyl sulfate + reduced riboflavin = AMP + sulfite + oxidized riboflavin
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Product in Enzyme-catalyzed Reactions (17 results)
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riboflavin + NADH + H+ = reduced riboflavin + NAD+
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catechol + riboflavin + H2O = phenol + reduced riboflavin + O2
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riboflavin + NADH + H+ = reduced riboflavin + NAD+
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xanthine + riboflavin + H2O = urate + reduced riboflavin
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formate + riboflavin = CO2 + reduced riboflavin
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oxidized riboflavin + NADPH + H+ = reduced riboflavin + NADP+
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riboflavin + NAD(P)H = reduced riboflavin + NAD(P)+
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riboflavin + NAD(P)H = reduced riboflavin + NADP+
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riboflavin + NADH + H+ = reduced riboflavin + NAD+
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riboflavin + NADPH + H+ = reduced riboflavin + NADP+
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riboflavin + NADPH = reduced riboflavin + NADP+
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riboflavin + NADH + H+ = reduced riboflavin + NAD+
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riboflavin + NADH = reduced riboflavin + NAD+
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riboflavin + NADH + H+ = reduced riboflavin + NAD+
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riboflavin + NADPH + H+ = reduced riboflavin + NADP+
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riboflavin + NADH + H+ = reduced riboflavin + NAD+
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riboflavin + NADPH + H+ = reduced riboflavin + NADP+
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Inhibitor in Enzyme-catalyzed Reactions (1 result)
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Enzyme Kinetic Parameters
KM Value (1 result)
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References & Links Literature References (5)
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Studies on luciferase from Photobacterium phosphoreum. VI. Stoichiometry and mode of binding of FMNH2 and O2 to stripped luciferase
1974
Watanabe, T.; Tomita, G.; Nakamura, T.
J. Biochem.
75
1249-1255
Catalytic properties of adenylylsulfate reductase from Desulfovibrio vulgaris Miyazaki
1996
Yagi, T.; Ogata, M.
Biochimie
78
838-846
Characterization of xanthine dehydrogenase from the anaerobic bacterium Veillonella atypica and identification of molybdopterin-cytosine-dinucleotide-containing molybdenum cofactor
1996
Gremer, L.; Meyer, O.
Eur. J. Biochem.
238
862-866
Phenol hydroxylase from Bacillus thermoglucosidasius A7, a two-protein component monooxygenase with a dual role for FAD
2003
Kirchner, U.; Westphal, A.H.; Muller, R.; van Berkel, W.J.
J. Biol. Chem.
278
47545-47553
Gene overexpression, purification, and identification of a desulfurization enzyme from Rhodococcus sp. strain IGTS8 as a sulfide/sulfoxide monooxygenase
1996
Lei, B.; Tu, S.C.
J. Bacteriol.
178
5699-5705
Links to other databases for reduced riboflavin