Structural Research of Decarboxylases

Decarboxylases are a class of enzymes that play an essential role in various biological processes. They are responsible for catalyzing the decarboxylation reaction, which involves the removal of a carboxyl group from a molecule. Decarboxylases are found in a wide range of organisms, including bacteria, fungi, plants, and animals. They are involved in many important physiological processes such as neurotransmitter synthesis, amino acid metabolism, and energy production.

The oxaloacetate decarboxylase sodium pump (OAD) is a primary-active transporter that employs the energy released from oxaloacetate decarboxylation to move sodium ions across the cell membrane. Comprising of three subunits, the α subunit catalyzes the transfer of carboxyl from oxaloacetate to biotin, while the β subunit, integrated into the membrane, performs the subsequent carboxyl-biotin decarboxylation and sodium transport, and the γ subunit interacts with the α and β subunits and stabilizes the OAD complex. The structure of the Salmonella typhimurium OAD βγ sub-complex was determined, which reveals that the β and γ subunits combine to form a β3γ3 hetero-hexamer with extensive subunit interactions, providing insights into OAD holo-enzyme assembly. Guided by the structure, functional studies offer further understanding of the sodium binding sites in the β subunit and the coupling between carboxyl-biotin decarboxylation and sodium transport by the OAD β subunit. These structural studies have provided important insights into the mechanism of decarboxylation and have paved the way for the development of new drugs that target these enzymes.

Figure 1. The overall structure of the StOAD βγ sub-complex. (Xu X, et al., 2020)

Table 1. Structural Research of Decarboxylases.

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Reference

1. Xu X, et al. Structural insights into sodium transport by the oxaloacetate decarboxylase sodium pump. Elife. 2020, 9: e53853.