Activating Compound | Comment | Organism | Structure |
---|---|---|---|
Fe4-S4 cluster | active enzyme contains an iron-sulfur cluster | Sinorhizobium meliloti |
Cloned (Comment) | Organism |
---|---|
expressed in Escherichia coli as a His-tagged fusion protein | Sinorhizobium meliloti |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Sinorhizobium meliloti | - |
- |
- |
Purification (Comment) | Organism |
---|---|
using Ni-NTA chromatography | Sinorhizobium meliloti |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
isocitrate | - |
Sinorhizobium meliloti | cis-aconitate + H2O | - |
? |
Synonyms | Comment | Organism |
---|---|---|
AcnA | - |
Sinorhizobium meliloti |
aconitase | - |
Sinorhizobium meliloti |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.4 | - |
assay at | Sinorhizobium meliloti |
General Information | Comment | Organism |
---|---|---|
malfunction | acnA mutants grow very poorly, have secondary mutations, and are quickly outgrown by pseudorevertants. The acnA gene is stably interrupted in a citrate synthase (gltA) null background, indicating that the intracellular accumulation of citrate may be deleterious for survival. No aconitase activity is detected in this mutant. To uncover a function of AcnA beyond its catalytic role in the tricarboxylic acid cycle pathway, the citrate synthase/aconitase (acnA) double mutant is compared with the citrate synthase single mutant. No differences are found | Sinorhizobium meliloti |