1.1.5.4: malate dehydrogenase (quinone)
This is an abbreviated version!
For detailed information about malate dehydrogenase (quinone), go to the full flat file.
Word Map on EC 1.1.5.4
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1.1.5.4
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oxaloacetate
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glutamicum
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phospholipid-requiring
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pyrroloquinoline
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lipid-depleted
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1.1.1.37
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biotechnology
- 1.1.5.4
- oxaloacetate
- glutamicum
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phospholipid-requiring
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pyrroloquinoline
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lipid-depleted
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1.1.1.37
- biotechnology
Reaction
Synonyms
EC 1.1.3.3, EC 1.1.99.16, FAD-dependent malate dehydrogenase, L-malate-quinone oxidoreductase, L-malate:quinone oxidoreductase, malate dehydrogenase, malate dehydrogenase (acceptor), malate-quinone oxidoreductase, malate-vitamin K reductase, malate: quinone oxidoreductase, malate:quinine oxidoreductase, malate:quinone oxidoreductase, malate:quinone reductase, menaquinone reductase, Mqo, MqoB, MQR, PfMQO
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Cofactor
Cofactor on EC 1.1.5.4 - malate dehydrogenase (quinone)
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menadione
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triple cofactor requirement for FAD, quinone and phospholipid. Maximum rate when phosphatidylethanolamine is added to the enzyme before the quinone
ubiquinone-0
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triple cofactor requirement for FAD, quinone and phospholipid. Maximum activation rate when phosphatidylethanolamine is added to the enzyme before the quinone
ubiquinone-1
the route of electrons in this assay is unclear, but it probably leads from the enzyme either directly or via quinones to 2,6-dichlorophenol indophenol. The malate-dependent 2,6-dichlorophenol indophenol reduction rate catalyzed by Helicobacter pylori membranes could be stimulated by 30 to 50% by the addition of 60 mM ubiquinone-1. This suggests that quinones play, at least in part, an intermediary role in the reduction of the dye
ubiquinone-9
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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
FAD
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in absence of FAD no reduction of 2,6-dichlorophenol indophenol is observed
FAD
is probably a tightly but non-covalently bound prosthetic group
FAD
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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. Km-value for FAD is 0.0004 mM
vitamin K1
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with both vitamin K1 and ubiquinone-9, maximum rates are obtained by exposing the enzyme to phospholipid and quinone simultaneously, but, when phosphatidylethanolamine is added to the enzyme before either of these quinones, the rates are much lower
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no spectral evidence for the presence of a flavin or quinone in the purified enzyme
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additional information
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the enzyme is active with 2,6-dichlorophenolindophenol
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additional information
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the enzymeis active with duroquinone and dimethyl naphthoquinone
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