title: Pyrrole-2-carboxylate decarboxylase from Bacillus megaterium PYR2910, an organic-acid-requiring enzyme.
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.
authors.affiliation: Department of Biomolecular Science, Faculty of Engineering, Gifu University, Gifu-Yanagido, Japan.
authors.forename: H
authors.initials: H
authors.lastname: Omura
authors.forename: M
authors.initials: M
authors.lastname: Wieser
authors.forename: T
authors.initials: T
authors.lastname: Nagasawa
mesh_terms: 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
chemical_list: D000085:Acetates; D001426:Bacterial Proteins; D012835:Silver Nitrate; D002262:Carboxy-Lyases; C113052:pyrrole-2-carboxylate decarboxylase