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Ligand ubiquinone-9 Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Basic Ligand Information Molecular Structure
C5 4 H8 2 O4
ubiquinone-9
UUGXJSBPSRROMU-WJNLUYJISA-N
coenzyme Q9, ubiquinone 9
Roles as Enzyme Ligand
In Vivo Substrate in Enzyme-catalyzed Reactions (1 result)Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NADH + ubiquinone-9 = NAD+ + ubiquinol-9
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Substrate in Enzyme-catalyzed Reactions (11 results)
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(S)-malate + ubiquinone-9 = oxaloacetate + ubiquinol-9
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(S)-dihydroorotate + coenzyme Q9 = orotate + reduced coenzyme Q9
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sulfide + ubiquinone-9 = sulfur + ubiquinol-9
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NADH + ubiquinone-9 = NAD+ + ubiquinol-9
NADH + ubiquinone-9 = NAD+ + ubiquinol-9
NADH + ubiquinone-9 = NAD+ + ubiquinol-9
NADH + ubiquinone-9 = NAD+ + ubiquinol-9
NADH + ubiquinone-9 = NAD+ + ubiquinol-9
NADH + ubiquinone-9 = NAD+ + ubiquinol-9
NADH + ubiquinone-9 = NAD+ + ubiquinol-9
NADH + ubiquinone-9 = NAD+ + ubiquinol-9
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Product in Enzyme-catalyzed Reactions (1 result)
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ubiquinol 9 + cytochrome c = ubiquinone 9 + reduced cytochrome c
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Enzyme Cofactor/Cosubstrate (1 result)
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triple cofactor requirement for FAD, quinone and phospholipid. The formation of reduced forms of FAD is not detected, but in the presence of both FAD and phospholipid the enzyme catalyzes the reduction of quinone by L-malate at rates equivalent to the rate obtained with 2,6-dichlorophenol-indophenol as terminal acceptor. The quinone is identified as ubiquinone 9. Km-value for ubiquinone 9 is 0.0024 mM
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3D Structure of Enzyme-Ligand-Complex (PDB) (26 results)
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Enzyme Kinetic Parameters
KM Value (4 results)
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0.00643
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in 50 mM Tris-HCl, pH 7.4, 40°C
0.00643
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pH 7.4, temperature not specified in the publication
References & Links Literature References (6)
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Malate dehydrogenase (FAD-linked) from Pseudomonas ovalis Chester
1969
Phizackerley, P.J.R.
Methods Enzymol.
13
135-140
Characterization of NAD(P)H-dependent ubiquinone reductase activities in rat liver microsomes
1993
Shigemura, T.; Kang, D.; Nagata-Kuno, K.; Takeshige, K.; Hamasaki, N.
Biochim. Biophys. Acta
1141
213-220
Energy converting NADH:quinone oxidoreductase (complex I)
2006
Brandt, U.
Annu. Rev. Biochem.
75
69-92
Cofactor requirements of the L-malate dehydrogenase of Pseudomonas ovalis Chester
1966
Phizackerley, P.J.; Francis, M.J.
Biochem. J.
101
524-535
Characterizing a monotopic membrane enzyme. Biochemical, enzymatic and crystallization studies on Aquifex aeolicus sulfide:quinone oxidoreductase
2010
Marcia, M.; Langer, J.D.; Parcej, D.; Vogel, V.; Peng, G.; Michel, H.
Biochim. Biophys. Acta
1798
2114-2123
Phytophthora infestans dihydroorotate dehydrogenase is a potential target for chemical control - a comparison with the enzyme from Solanum tuberosum
2019
Garavito, M.F.; Narvaez-Ortiz, H.Y.; Pulido, D.C.; Loeffler, M.; Judelson, H.S.; Restrepo, S.; Zimmermann, B.H.
Front. Microbiol.
10
1479
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