Characterization of NADP(+)-specific L-rhamnose dehydrogenase from the thermoacidophilic Archaeon Thermoplasma acidophilum
SCIE
SCOPUS
- Title
- Characterization of NADP(+)-specific L-rhamnose dehydrogenase from the thermoacidophilic Archaeon Thermoplasma acidophilum
- Authors
- Kim, SM; Paek, KH; Lee, SB
- Date Issued
- 2012-05
- Publisher
- SPRINGER TOKYO
- Abstract
- 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.
- Keywords
- NADP-specific L-rhamnose dehydrogenase; Thermoplasma acidophilum; Thermophilic enzyme; Archaea; Non-phosphorylated pathway; ENTNER-DOUDOROFF PATHWAY; ESCHERICHIA-COLI; SULFOLOBUS-SOLFATARICUS; L-RHAMNULOSE; GLUCOSE-DEHYDROGENASE; COENZYME SPECIFICITY; CARBONYL REDUCTASE; INTRACELLULAR PH; METABOLISM; ALDOLASE
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/15031
- DOI
- 10.1007/S00792-012-0444-1
- ISSN
- 1431-0651
- Article Type
- Article
- Citation
- EXTREMOPHILES, vol. 16, no. 3, page. 447 - 454, 2012-05
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