, Volume 17, Issue 6, pp 897–909

l-Arabinose degradation pathway in the haloarchaeon Haloferax volcanii involves a novel type of l-arabinose dehydrogenase


  • Ulrike Johnsen
    • Institut für Allgemeine MikrobiologieChristian-Albrechts-Universität Kiel
  • Jan-Moritz Sutter
    • Institut für Allgemeine MikrobiologieChristian-Albrechts-Universität Kiel
  • Henning Zaiß
    • Institut für Allgemeine MikrobiologieChristian-Albrechts-Universität Kiel
    • Institut für Allgemeine MikrobiologieChristian-Albrechts-Universität Kiel
Original Paper

DOI: 10.1007/s00792-013-0572-2

Cite this article as:
Johnsen, U., Sutter, J., Zaiß, H. et al. Extremophiles (2013) 17: 897. doi:10.1007/s00792-013-0572-2


The pathway of l-arabinose degradation was studied in the haloarchaeon Haloferax volcanii. It is shown that l-arabinose is oxidatively degraded to α-ketoglutarate. During growth on l-arabinose, l-arabinose dehydrogenase (l-AraDH) was induced. The enzyme was purified as a 130 kDa homotetrameric protein catalyzing the oxidation of l-arabinose with both NADP+ and NAD+. The gene encoding l-AraDH was identified as HVO_B0032 and recombinant l-AraDH showed similar properties as the native enzyme. The l-AraDH deletion mutant did not grow on l-arabinose, but grew unaffected on glucose and d-xylose, indicating a specific involvement in l-arabinose degradation. Phylogenetic analyses attribute the first archaeal l-AraDH to the extended short-chain dehydrogenase/reductase (SDRe) family, where it is part of a novel cluster and thus differs from known archaeal and bacterial pentose dehydrogenases. Further, cell extracts of H. volcanii catalyzed the NADP+-dependent conversion of l-arabinoate to α-ketoglutarate. The genes involved in that conversion were identified by analyses of transcripts and deletion mutants as HVO_B0038A, HVO_B0027 and HVO_B0039 recently reported to be involved in d-xylonate conversion to α-ketoglutarate in H. volcanii (Johnsen et al. 2009).


l-Arabinose dehydrogenase Archaea Haloferax volcanii Metabolic pathways Extended short-chain dehydrogenase/reductase Pentose catabolism

Supplementary material

792_2013_572_MOESM1_ESM.docx (440 kb)
Supplementary material (DOCX 440 kb)

Copyright information

© Springer Japan 2013