Oxaloacetate decarboxylase

A oxaloacetate decarboxylase found in mitochondria and soluble cytoplasm was isolated and purified from rat liver cells in 1974 by Wojtcak et al.

[4] Found in different microorganisms such as Pseudomonas, Acetobacter, C. glutamicum, Veillonella parvula, and A. vinelandii, cytoplasmic oxaloacetate decarboxylases are dependent on the presence of divalent cations such as Mn2+, Co2+, Mg2+, Ni2+, or Ca2+.

[6] Decarboxylating the beta-keto acid of oxaloacetate affords the necessary free energy to pump sodium ions across the lipid bilayer.

The crystal structure of the CT domain forms a TIM barrel fold in a dimer formation that coordinates with a Zn2+ ion in a catalytic site.

[13] The enzyme is completely inactivated by specific mutagenesis of Asp17, His207, and His209, which serve as ligands for the Zn2+ metal ion, or by Lys178 near the active site, suggesting that Zn2+ as well as Lys178 are essential for catalysis.

Crystal structure of the carboxyltransferase domain of the oxaloacetate decarboxylase Na+ pump from Vibrio cholerae [ 1 ]
Oxaloacetate decarboxylase catalyzes the break down of oxaloacetate into pyruvate and carbon dioxide