Yatake Yoshito, Miyamoto Kenji, Ohta Hiromichi
Department of Biosciences and Informatics, Faculty of Science and Technology, Keio University, 3-14-1 Hiyoshi, Kohoku-ku, Yokohama 223-8522, Japan.
Appl Microbiol Biotechnol. 2008 Apr;78(5):793-9. doi: 10.1007/s00253-008-1375-8. Epub 2008 Feb 19.
We have already isolated, purified, and characterized arylmalonate decarboxylases (AMDase; EC. 4.1.1.76) from Alcaligenes bronchisepticus KU1201 and Achromobacter sp. KU1311. These are unique enzymes that give optically pure alpha-arylpropionates from the corresponding alpha-aryl-alpha-methylmalonates. Recently, we have further screened novel AMDase producers from soil samples under acidic conditions and succeeded in isolating Enterobacter cloacae KU1313. The gene encoding the enzyme was cloned by polymerase chain reaction and sequenced. The AMDase gene consists of 720 nucleotides, which specifies a 240-amino-acid protein. The recombinant enzyme was purified and shown that the pH-activity profiles were quite different from those of known AMDases.
我们已经从支气管败血碱杆菌KU1201和无色杆菌属菌株KU1311中分离、纯化并鉴定了芳基丙二酸脱羧酶（AMDase；EC. 4.1.1.76）。这些是独特的酶，能从相应的α-芳基-α-甲基丙二酸生成光学纯的α-芳基丙酸。最近，我们在酸性条件下进一步从土壤样品中筛选新型AMDase产生菌，并成功分离出阴沟肠杆菌KU1313。通过聚合酶链反应克隆了编码该酶的基因并进行了测序。AMDase基因由720个核苷酸组成，指定了一个240个氨基酸的蛋白质。对重组酶进行了纯化，结果表明其pH-活性曲线与已知的AMDase有很大不同。
