EC Number | Cloned (Comment) | Organism |
---|---|---|
1.1.2.4 | gene DLD, expression of C-terminally GFP-tagged full-length enzyme under control of the CaMV35S promoter in Nicotiana benthamiana leaf epidermi. Overexpression of D-LDH ameliorates the growth of wild-type plants in the presence of D-lactate and methylglyoxal and reverses the increased sensitivity of dldh loss-of-function lines to these compounds | Arabidopsis thaliana |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.1.2.4 | additional information | antimycin A does not affect the enzyme activity. Myxothiazol binds to the quinone-binding site and blocks electron transfer from ubiquinol to cytochrome b. At 20 mM myxothiazol the sensitivity of wild-type plants to D-lactate is not affected. Inhibition of complex III does not affect D-lactate oxidation | Arabidopsis thaliana |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
1.1.2.4 | mitochondrial intermembrane space | localization of recombinantly expressed GFP-tagged enzyme | Arabidopsis thaliana | 5758 | - |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
1.1.2.4 | 110000 | - |
recombinant enzyme, native PAGE | Arabidopsis thaliana |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.2.4 | (R)-lactate + 2 ferricytochrome c | Arabidopsis thaliana | enzyme D-LDH is absolutely specific for these substrates in vivo | pyruvate + 2 ferrocytochrome c | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.1.2.4 | Arabidopsis thaliana | Q94AX4 | - |
- |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
1.1.2.4 | cell suspension culture | - |
Arabidopsis thaliana | - |
1.1.2.4 | leaf | - |
Arabidopsis thaliana | - |
1.1.2.4 | seedling | - |
Arabidopsis thaliana | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.2.4 | (R)-lactate + 2 ferricytochrome c | - |
Arabidopsis thaliana | pyruvate + 2 ferrocytochrome c | - |
? | |
1.1.2.4 | (R)-lactate + 2 ferricytochrome c | enzyme D-LDH is absolutely specific for these substrates in vivo | Arabidopsis thaliana | pyruvate + 2 ferrocytochrome c | - |
? | |
1.1.2.4 | additional information | D-LDH does not use glycolate as a substrate | Arabidopsis thaliana | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.1.2.4 | homodimer | x * 62000, recombinant enzyme, SDS-PAGE | Arabidopsis thaliana |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.1.2.4 | AtD-LDH | - |
Arabidopsis thaliana |
1.1.2.4 | D-lactate dehydrogenase [cytochrome], mitochondrial | - |
Arabidopsis thaliana |
1.1.2.4 | D-lactate ferricytochrome c oxidoreductase | - |
Arabidopsis thaliana |
1.1.2.4 | DLD | - |
Arabidopsis thaliana |
1.1.2.4 | glycolate deshydrogenase | - |
Arabidopsis thaliana |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.1.2.4 | cytochrome c | evaluation of the role of cytochrome c in D-lactate and methylglyoxal degradation. Recombinant expression of CYTC-1 in either the wild-type or cytc mutant background leads to increased tolerance to toxic concentrations of D-lactate and to a lesser extent also to methylglyoxal | Arabidopsis thaliana | |
1.1.2.4 | additional information | ubiquinone and its associated dehydrogenase systems do not serve as electron acceptors and are upstream of the entry site of D-LDH-derived electrons into the electron transport chain | Arabidopsis thaliana |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.1.2.4 | physiological function | transgenic plants overexpressing both D-LDH and cytochrome c have enhanced capacity to detoxify D-lactate and methylglyoxal, indicating that both proteins can be limiting factors in the detoxification process | Arabidopsis thaliana |