Pyrrole‐2‐carboxylate decarboxylase from Bacillus megaterium PYR2910, an organic‐acid‐requiring enzyme
Open Access
- 15 April 1998
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 253 (2) , 480-484
- https://doi.org/10.1046/j.1432-1327.1998.2530480.x
Abstract
Inducible pyrrole‐2‐carboxylate decarboxylase, which catalyzes the decarboxylation of pyrrole‐2‐carboxylate to pyrrole and CO2 in stoichiometric amounts, was purified from Bacillus megaterium PYR2910. The purity of the enzyme was shown by SDS/PAGE and gel‐permeation HLPC. The enzyme has a molecular mass of approximately 98 kDa and consists of two identical subunits. It is highly specific for pyrrole‐2‐carboxylate, and also catalyzes the reverse reaction, the carboxylation of pyrrole. A unique feature of this enzyme is its requirement of an organic acid, such as acetate, propionate, butyrate or pimelate. A possible catalytic mechanism including a cofactor function of organic acid is discussed.Keywords
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