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EC Number Cofactor Commentary Reference
Show all pathways known for 4.2.1.167Display the reaction diagram Show all sequences 4.2.1.1674Fe-4S-center the enzyme contains [4F-4S] clusters 733761
Show all pathways known for 4.2.1.167Display the reaction diagram Show all sequences 4.2.1.167riboflavin 5'-phosphate the enzyme contains 1.0 mol of riboflavin 5'-phosphate per mol of heterodimeric enzyme 733766
Show all pathways known for 4.2.1.167Display the reaction diagram Show all sequences 4.2.1.167riboflavin presence of trace amounts 733770
Show all pathways known for 4.2.1.167Display the reaction diagram Show all sequences 4.2.1.167riboflavin 5'-phosphate 1 mol per mol of heterodimeric dehydratase 733770
Show all pathways known for 4.2.1.167Display the reaction diagram Show all sequences 4.2.1.167[4Fe-4S]-center each active component contains an oxygen sensitive diamagnetic [4Fe-4S]2+ cluster. Reduction of the [4Fe-4S]2+ cluster of the activator protein with dithionite yields a paramagnetic [4Fe-4S]1+ cluster with the unusual electron spin ground state S=3/2. Under air the activator protein looses its activity within seconds due to irreversible degradation of its [4Fe-4S]2+ cluster to a [2Fe-2S]2+ cluster. The [4Fe-4S]2+ cluster of the heterodimeric dehydratase cannot be reduced to a [4Fe-4S]1+ cluster 733770
Show all pathways known for 4.2.1.167Display the reaction diagram Show all sequences 4.2.1.167Ferredoxin alternative electron donor besides flavodoxin is a two [4Fe-4S]1+/2+-cluster-containing ferredoxin, with redox potentials of –405 mV and –340mV. The flavodoxin is the dominant electron donor protein under iron-limiting conditions. The concentration of ferredoxin increases stepwise from about 0.2 micromol/g at 7–13 microM Fe to 1.1 micromol/g at 17–45 microM Fe 737565
Show all pathways known for 4.2.1.167Display the reaction diagram Show all sequences 4.2.1.167flavodoxin dominant electron donor protein under iron-limiting conditions 737565
Show all pathways known for 4.2.1.167Display the reaction diagram Show all sequences 4.2.1.167riboflavin 5'-phosphate the actual dehydration is mediated by component D, which contains 1.0 [4Fe-4S]2+ cluster, 1.0 reduced riboflavin-5'-phosphate and about 0.1 molybdenum (VI) per heterodimer 737565
Show all pathways known for 4.2.1.167Display the reaction diagram Show all sequences 4.2.1.167[4Fe-4S]-center the actual dehydration is mediated by component D, which contains 1.0 [4Fe-4S]2+ cluster, 1.0 reduced riboflavin-5'-phosphate and about 0.1 molybdenum (VI) per heterodimer 737565
Show all pathways known for 4.2.1.167Display the reaction diagram Show all sequences 4.2.1.167[4Fe-4S]-center the [4Fe-4S](1+/2+) cluster of the activator protein is exposed to the solvent. Upon exchange of the bound ADP by ATP, the chelation rate by iron chelators is 8fold enhanced, indicating a large conformational change. Oxidized activator exhibits ATPase activity of 6 s(-1), which is completely abolished upon reduction by one electron 737664
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