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The enzyme aconitate decarboxylase (EC 4.1.1.6) (i.e., ACOD1, also termed cis-aconitate decarboxylase, immune-responsive gene 1, immune response gene 1, and IRK1[1][2]) is a protein enzyme that in humans is encoded by the decarboxylase 1 aconitate decarboxylase 1 gene located at position 22.3 on the long arm (i.e., p-arm) of chromosome 13.[3] ACOD1 catalyzes the following reversible (i.e., runs in both directions, as indicated by ) decarboxylation chemical reaction:[4][5][6]
- cis-aconitate itaconate + CO2
| aconitate decarboxylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.1.1.6 | ||||||||
| CAS no. | 9025-01-8 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Hence, ACOD1 converts cis-aconitate into two products, itaconate and CO2 or itaconate and CO2 into one product, aconitate.
ACOD1 belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is cis-aconitate carboxy-lyase (itaconate-forming). Other names once in common use for this enzyme class include CAD and cis-aconitate carboxy-lyase. ACOD1 participates in c5-branched dibasic acid metabolism.[7]
Ustilago maydis (a species of Ustilago fungi) converts cis-aconitate to its thermodynamically favored product, trans-aconitate, by the enzyme aconitate delta-isomerase (i.e., Adi1). The trans-aconitate product is decarboxylated to itaconate by trans-aconitate decarboxylase (i.e., Tad1).[8] This Adi followed by Tad 1 enzymatic metabolic pathway is:
- cis-aconitate trans-itaconate → itaconate + CO2
Trans-aconitate decarboxylase does not metabolize cis-aconitate to itaconate.[8] (The genes for aconitate delta-isomerase and trans-aconitate decarboxylase have been reported in several types of fungi hut not in other organisms, including humand, and are classified as provisional, i.e., accepted provisional to further studies.)
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