Activating Compound | Comment | Organism | Structure |
---|---|---|---|
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 | Corynebacterium glutamicum | |
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 | Corynebacterium glutamicum | |
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 | Corynebacterium glutamicum | |
Lipid | activates | Corynebacterium glutamicum | |
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 | Corynebacterium glutamicum | |
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 | Corynebacterium glutamicum |
Cloned (Comment) | Organism |
---|---|
- |
Corynebacterium glutamicum |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
KSCN | - |
Corynebacterium glutamicum |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | a peripheral membrane protein that can be released from the membrane by addition of chelators | Corynebacterium glutamicum | 16020 | - |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
(S)-malate + acceptor | Corynebacterium glutamicum | the enzyme takes part in the citric acid cycle. It oxidizes L-malate to oxaloacetate and donates electrons to ubiquinone-1 and other artificial acceptors or, via the electron transfer chain, to oxygen. NAD is not an acceptor and the natural direct acceptor for the enzyme is most likely a quinone. A mutant completely lacking Mqo activity grows poorly on several substrates tested. This enzyme might be especially important when a net flux from malate to oxaloacetate is required, but the intracellular concentrations of the reactants are unfavourable for the NAD-dependent reaction (EC 1.1.1.37) | oxaloacetate + reduced acceptor | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Corynebacterium glutamicum | O69282 | a mutant completely lacking Mqo activity grows poorly on several substrates tested | - |
Purification (Comment) | Organism |
---|---|
native and His-tagged enzyme | Corynebacterium glutamicum |
Storage Stability | Organism |
---|---|
when frozen, the activity is stable for several months | Corynebacterium glutamicum |
when stored on ice, the half-life is approximately 120 h, important stabilizing conditions for storage on ice are the presence of EDTA and EGTA. the presence of glycerol, and pH 6. The presence of Mg2+ and Ca2+ has a destabilizing effect | Corynebacterium glutamicum |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(S)-malate + 2,6-dichlorophenol indophenol | - |
Corynebacterium glutamicum | oxaloacetate + reduced 2,6-dichlorophenol indophenol | - |
? | |
(S)-malate + acceptor | the enzyme takes part in the citric acid cycle. It oxidizes L-malate to oxaloacetate and donates electrons to ubiquinone-1 and other artificial acceptors or, via the electron transfer chain, to oxygen. NAD is not an acceptor and the natural direct acceptor for the enzyme is most likely a quinone. A mutant completely lacking Mqo activity grows poorly on several substrates tested. This enzyme might be especially important when a net flux from malate to oxaloacetate is required, but the intracellular concentrations of the reactants are unfavourable for the NAD-dependent reaction (EC 1.1.1.37) | Corynebacterium glutamicum | oxaloacetate + reduced acceptor | - |
? | |
(S)-malate + ubiquinone-1 | ubiquinone-1 is directly reduced by the enzyme | Corynebacterium glutamicum | oxaloacetate + reduced ubiquinone-1 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
malate dehydrogenase (acceptor) | - |
Corynebacterium glutamicum |
malate:quinone oxidoreductase | - |
Corynebacterium glutamicum |
Mqo | - |
Corynebacterium glutamicum |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | is probably a tightly but non-covalently bound prosthetic group | Corynebacterium glutamicum |