Aconitase

Aconitase (also known as aconitate hydratase) is an enzyme that catalyses the stereo-specific isomerization of citrate to isocitrate via cis-aconitate in the tricarboxylic acid cycle, a non-redox-active process.

Structure

Aconitase, displayed in the structures in the right margin of this page, has two slightly different structures, depending on whether it is activated or inactivated. In the inactive form, its structure is divided into four domains. The Fe-S cluster and a SO42− anion also reside in the active site.

Function

Aconitase has an iron-sulfur cluster, which is necessary for its function. The enzyme can exist in two forms - an active form that contains the iron-sulfur cluster, and an inactive form that does not contain the cluster. The inactive form is converted to the active form by the addition of an iron atom and a sulfur atom.

Clinical significance

Mutations in the ACO2 gene are associated with a rare form of metabolic disorder known as Infantile cerebellar-retinal degeneration (ICRD). This disorder is characterized by a variety of symptoms, including psychomotor delay, hypotonia, seizures, optic atrophy, and cerebellar atrophy.

See also

• Iron-sulfur protein
• Citric acid cycle
• Isocitrate

External links

• EC 4.2.1.3
• GeneCard for ACO2

Aconitase Resources
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