Add time:09/24/2019         Source:sciencedirect.com

The review is concerned with three Na+-dependent biotin-containing decarboxylases, which catalyse the substitution of CO2 by H+ with retention of configuration (ΔG°′=−30 kJ/mol): oxaloacetate decarboxylase from enterobacteria, methylmalonyl-CoA decarboxylase from Veillonella parvula and Propiogenium modestum, and glutaconyl-CoA decarboxylase from Acidaminococcus fermentans. The enzymes represent complexes of four functional domains or subunits, a carboxytransferase, a mobile alanine- and proline-rich biotin carrier, a 9–11 membrane-spanning helix-containing Na+-dependent carboxybiotin decarboxylase and a membrane anchor. In the first catalytic step the carboxyl group of the substrate is converted to a kinetically activated carboxylate in N-carboxybiotin. After swing-over to the decarboxylase, an electrochemical Na+ gradient is generated; the free energy of the decarboxylation is used to translocate 1–2 Na+ from the inside to the outside, whereas the proton comes from the outside. At high [Na+], however, the decarboxylases appear to catalyse a mere Na+/Na+ exchange. This finding has implications for the life of P. modestum in sea water, which relies on the synthesis of ATP via ΔμNa+ generated by decarboxylation. In many sequenced genomes from Bacteria and Archaea homologues of the carboxybiotin decarboxylase from A. fermentans with up to 80% sequence identity have been detected.

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