원문정보
초록
영어
It has been suggested that thermoacidophilic archaea, such as Thermoplasma acidophilum and Sulfolobus solfataricus, are known to metabolize glucose via the non-phosphorylated Entner-Doudoroff pathway involving non-phosphorylated intermediates. Recently, we have identified and characterized the L-rhamnose dehydrogenase, an enzyme involved in the first step of the non-phosphorylated L-rhamnose pathway. To characterize this enzyme, the gene encoding the
L-rhamnose dehydrogenase from Thermoplasma acidophilum was cloned and expressed in E. coli BL21 (DE3). The L-rhamnose dehydrogenase from Thermoplasma acidophilum is a 27 kDa enzyme that belongs to the short-chain dehydrogenase/reductase superfamily. This enzyme effectively catalyzes the oxidation of L-rhamnose and L-lyxose, with a preference of NADP+ rather than NAD+ as cofactor. The optimal temperature and pH were determined to be 55～
60℃ and 8.0, respectively. This is the first report on the characterization of the L-rhamnose dehydrogenase from Archaea.