Pyrrole-2-carboxylate decarboxylase from Bacillus megaterium PYR2910, an organic-acid-requiring enzyme.
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.
Omura
H
H
Department of Biomolecular Science, Faculty of Engineering, Gifu University, Gifu-Yanagido, Japan.
Wieser
M
M
Nagasawa
T
T
D000085:Acetates / Q000494:pharmacology; D001410:Bacillus megaterium / Q000201:enzymology*; D001426:Bacterial Proteins / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D002262:Carboxy-Lyases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D012835:Silver Nitrate / Q000494:pharmacology; D013379:Substrate Specificity
D000085:Acetates; D001426:Bacterial Proteins; D012835:Silver Nitrate; D002262:Carboxy-Lyases; C113052:pyrrole-2-carboxylate decarboxylase