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
-
phospholipid-requiring
-
pyrroloquinoline
-
lipid-depleted
-
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
ECTree
1.1.5.4 malate dehydrogenase (quinone)Advanced search results
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results (Activating Compound
Activating Compound on EC 1.1.5.4 - malate dehydrogenase (quinone)
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ACTIVATING COMPOUND 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
2-methyl-1,4-naphthoquinone
reduction of 2,6-dichlorophenol indophenol by solubilized enzyme is activated significantly by addition of the quinones decylubiquinone, duroquinone, 2-methyl-1,4-naphthoquinone (vitamin K3), ubiquinone-0 and ubiquinone-1. Optimal activation is observed with ubiquinone-1
decylubiquinone
reduction of 2,6-dichlorophenol indophenol by solubilized enzyme is activated significantly by addition of the quinones decylubiquinone, duroquinone, 2-methyl-1,4-naphthoquinone (vitamin K3), ubiquinone-0 and ubiquinone-1. Optimal activation is observed with ubiquinone-1
duroquinone
reduction of 2,6-dichlorophenol indophenol by solubilized enzyme is activated significantly by addition of the quinones decylubiquinone, duroquinone, 2-methyl-1,4-naphthoquinone (vitamin K3), ubiquinone-0 and ubiquinone-1. Optimal activation is observed with ubiquinone-1
ubiquinone-0
reduction of 2,6-dichlorophenol indophenol by solubilized enzyme is activated significantly by addition of the quinones decylubiquinone, duroquinone, 2-methyl-1,4-naphthoquinone (vitamin K3), ubiquinone-0 and ubiquinone-1. Optimal activation is observed with ubiquinone-1
ubiquinone-1
reduction of 2,6-dichlorophenol indophenol by solubilized enzyme is activated significantly by addition of the quinones decylubiquinone, duroquinone, 2-methyl-1,4-naphthoquinone (vitamin K3), ubiquinone-0 and ubiquinone-1. Optimal activation is observed with ubiquinone-1
vitamin K3
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in absence of either cardiolipin or vitamin K-3 the enzyme shows about 3% of maximal activity
Phospholipid
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in absence of either cardiolipin or vitamin K-3 the enzyme shows about 3% of maximal activity
Phospholipid
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activity of purified enzyme is dependent on added phospholipid
Phospholipid
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the nature of the phospholipid required to activate the enzyme depends on the nature of the quinone used in the assay system. When 2-methyl-1,4-naphthoquinone is used, a wide variety of phospholipids, including all these isolated from the organism, will activate the enzyme, but when coenzyme Q9 is used the phospholipid specificity of the enzyme is much more restricted, and the most effective activator is the unsaturated phosphatidylethanolamine isolated from the organism
