Literature summary 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.

Activating Compound

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

Cloned(Commentary)

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

Organism

EC Number	Organism	UniProt	Comment	Textmining
4.2.1.3	Sinorhizobium meliloti	-	-	-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Synonyms

EC Number	Synonyms	Comment	Organism
4.2.1.3	AcnA	-	Sinorhizobium meliloti
4.2.1.3	aconitase	-	Sinorhizobium meliloti

pH Optimum

EC Number	pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
4.2.1.3	7.4	-	assay at	Sinorhizobium meliloti

General Information

EC Number	General Information	Comment	Organism
4.2.1.3	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

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Release 2023.1 (January 2023)