Inhibitors | Comment | Organism | Structure |
---|---|---|---|
4-nitrobenzoate | inhibition of COQ2 by 4-nitrobenzoate, leading to 40-50% residual CoQ10, is associated with increased oxidative stress and reduced viability, together with moderately decreased ATP levels and ATP/ADP ratio | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
gene COQ2 | - |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
fibroblast | - |
Homo sapiens | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | decaprenyl diphosphate and 4-hydroxybenzoate are condensed in a reaction catalyzed by 4-hydroxybenzoate:polyprenyl transferase, i.e. COQ2 | Homo sapiens | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
4-para-hydroxybenzoate:polyprenyl transferase | - |
Homo sapiens |
COQ2 | - |
Homo sapiens |
General Information | Comment | Organism |
---|---|---|
malfunction | cell viability in skin fibroblasts with CoQ10 deficiency due to different molecular defects including mutations in COQ2. Treatment of multiple cell lines with increasing dosages of 4-nitrobenzoate, which inhibits 4-hydroxybenzoate:polyprenyltransferase, leads to dose-dependent decreases of CoQ in mammalian cells without directly inducing oxidative stress or mitochondrial respiration impairment. Fibroblasts from a patient with a homozygous COQ2 mutation require uridine to maintain cell growth and proposed that deficiency of CoQ10 impaired pyrimidine biosynthesis due to dependence of dihydro-orotate dehydrogenase on ubiquinol. Oxidative stress plays an important role in the demise of COQ2 mutant fibroblasts by activating cell-death related pathways, which are averted by antioxidant supplementation | Homo sapiens |
metabolism | the enzyme catalyzes one of the first steps in ubiquinone or coenzyme Q, CoQ, biosynthesis | Homo sapiens |