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Literature summary for 4.2.1.3 extracted from

  • Koziol, U.; Hannibal, L.; Rodriguez, M.C.; Fabiano, E.; Kahn, M.L.; Noya, F.
    Deletion of citrate synthase restores growth of Sinorhizobium meliloti 1021 aconitase mutants (2009), J. Bacteriol., 191, 7581-7586.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
Fe4-S4 cluster active enzyme contains an iron-sulfur cluster Sinorhizobium meliloti

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli as a His-tagged fusion protein Sinorhizobium meliloti

Organism

Organism UniProt Comment Textmining
Sinorhizobium meliloti
-
-
-

Purification (Commentary)

Purification (Comment) Organism
using Ni-NTA chromatography Sinorhizobium meliloti

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
isocitrate
-
Sinorhizobium meliloti cis-aconitate + H2O
-
?

Synonyms

Synonyms Comment Organism
AcnA
-
Sinorhizobium meliloti
aconitase
-
Sinorhizobium meliloti

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
assay at Sinorhizobium meliloti

General Information

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