title: Purification and characterization of arylmalonate decarboxylase from Achromobacter sp. KU1311.
abstract: We have isolated, purified and characterized arylmalonate decarboxylase (AMDase; EC 4.1.1.76). This is an unique enzyme that gives optically pure arylpropionates from the corresponding arylmalonates. Recently, we have screened similar enzyme producers from soil samples and succeeded in isolating Achromobacter sp. KU1311. The gene encoding the enzyme was cloned and sequenced. The AMDase gene consists of 720 nucleotides, which specifies a 240 amino acid protein with a relative molecular mass of 24,735. This enzyme was purified and its characteristics were compared with those of the hitherto known enzyme from Alcaligenes bronchisepticus KU1201.
authors.affiliation: Department of Biosciences and Informatics, Faculty of Science and Technology, Keio University, 3-14-1 Hiyoshi, Kohoku-ku, Yokohama 223-8522, Japan.
authors.forename: Kenji
authors.initials: K
authors.lastname: Miyamoto
authors.forename: Yoshito
authors.initials: Y
authors.lastname: Yatake
authors.forename: Keisuke
authors.initials: K
authors.lastname: Tamura
authors.forename: Yosuke
authors.initials: Y
authors.lastname: Terao
authors.forename: Hiromichi
authors.initials: H
authors.lastname: Ohta
mesh_terms: D042402:Achromobacter / Q000145:classification* / Q000201:enzymology*; D002262:Carboxy-Lyases / Q000737:chemistry* / Q000302:isolation & purification*; D004789:Enzyme Activation; D004795:Enzyme Stability; D013045:Species Specificity
chemical_list: D002262:Carboxy-Lyases; C071852:malonate decarboxylase