Journal
EXTREMOPHILES
Volume 16, Issue 3, Pages 447-454Publisher
SPRINGER JAPAN KK
DOI: 10.1007/s00792-012-0444-1
Keywords
NADP-specific L-rhamnose dehydrogenase; Thermoplasma acidophilum; Thermophilic enzyme; Archaea; Non-phosphorylated pathway
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Funding
- Korean Ministry of Land, Transport and Maritime Affairs
- 21C Frontier Microbial Genomics and Applications Centre of Korean Ministry of Education, Science and Technology
- National Research Foundation of Korea [11-2008-02-002-00] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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utilizes -rhamnose as a sole carbon source. To determine the metabolic pathway of -rhamnose in Archaea, we identified and characterized -rhamnose dehydrogenase (RhaD) in . Ta0747P gene, which encodes the putative RhaD (Ta_RhaD) enzyme belonging to the short-chain dehydrogenase/reductase family, was expressed in as an active enzyme catalyzing the oxidation of -rhamnose to -rhamnono-1,4-lactone. Analysis of catalytic properties revealed that Ta_RhaD oxidized -rhamnose, -lyxose, and -mannose using only NADP(+) as a cofactor, which is different from NAD(+)/NADP(+)-specific bacterial RhaDs and NAD(+)-specific eukaryal RhaDs. Ta_RhaD showed the highest activity toward -rhamnose at 60 A degrees C and pH 7. The (m) and (cat) values were 0.46 mM, 1,341.3 min(-1) for -rhamnose and 0.1 mM, 1,027.2 min(-1) for NADP(+), respectively. Phylogenetic analysis indicated that branched lineages of archaeal RhaD are quite distinct from those of Bacteria and Eukarya. This is the first report on the identification and characterization of NADP(+)-specific RhaD.
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