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Glutaconyl-CoA decarboxylase

In enzymology, a glutaconyl-CoA decarboxylase () is an enzyme that catalyzes the chemical reaction

(2E)-glutaconyl-CoA + H<sup>+</sup> + Na<sup>+</sup><small>(in)</small> (2E)-butenoyl-CoA + + Na<sup>+</sup><small>(out)</small>

Hence, this enzyme has one substrate, (2E)-glutaconyl-CoA, and two products, (2E)-butenoyl-CoA and CO<sub>2</sub>. During the process, a sodium ion is transported across the membrane. Previously, this enzyme was classified as EC 4.1.1.70.

This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is 4-carboxybut-2-enoyl-CoA carboxy-lyase (but-2-enoyl-CoA-forming). Other names in common use include glutaconyl coenzyme A decarboxylase, pent-2-enoyl-CoA carboxy-lyase, and 4-carboxybut-2-enoyl-CoA carboxy-lyase. This enzyme participates in benzoate degradation via coa ligation and butanoate metabolism.

As a decarboxylase, the enzyme requires biotin for its function.

Structural studies

As of mid-2024, five structures have been solved for this class of enzymes, with the PDB accession codes , , , and .

References