Pyrrole-2-carboxylate decarboxylase from Bacillus megaterium PYR2910 attains a balanced reaction equilibrium with an equilibrium constant of 0.3-0.4 M. Therefore, the enzyme catalyzes the reverse carboxylation of pyrrole after addition of bicarbonate. For the synthesis of pyrrole-2-carboxylate, the reverse reaction was optimized and the equilibrium was shifted towards the carboxylate. The product yield was 230 mM (25.5 g/l) pyrrole-2-carboxylate from 300 mM pyrrole in a batch reaction and 325 mM (36.1 g/l) from 400 mM pyrrole in a fed-batch reaction, using both whole cells and the purified enzyme in a pH 8.0 reaction mixture with bicarbonate saturation of 1.9 M. Kinetic studies indicated, that bicarbonate is the reactive species used by this carbon dioxide-fixation enzyme.