Open AccessPyrrole‐2‐carboxylate decarboxylase from Bacillus megaterium PYR2910, an organic‐acid‐requiring enzyme
Author(s) -
Omura Hironori,
Wieser Marco,
Nagasawa Toru
Publication year - 1998
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1046/j.1432-1327.1998.2530480.x
Subject(s) - decarboxylation , pyrrole , chemistry , carboxylate , cofactor , propionate , bacillus megaterium , carboxylation , enzyme , catalysis , oxidative decarboxylation , organic chemistry , stereochemistry , biochemistry , bacteria , biology , genetics
Inducible pyrrole‐2‐carboxylate decarboxylase, which catalyzes the decarboxylation of pyrrole‐2‐carboxylate to pyrrole and CO 2 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.