The Enzyme Database

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Accepted name: L-arabinose 1-dehydrogenase [NAD(P)+]
Reaction: α-L-arabinopyranose + NAD(P)+ = L-arabinono-1,4-lactone + NAD(P)H + H+
For diagram of L-Arabinose catabolism, click here
Other name(s): L-arabino-aldose dehydrogenase
Systematic name: α-L-arabinopyranose:NAD(P)+ 1-oxidoreductase
Comments: The enzymes from the bacterium Azospirillum brasilense and the archaeon Haloferax volcanii are part of the L-arabinose degradation pathway and prefer NADP+ over NAD+. In vitro the enzyme from Azospirillum brasilense shows also high catalytic efficiency with D-galactose. The enzyme is specific for α-L-arabinopyranose [3,4].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
1.  Novick, N.J. and Tyler, M.E. Partial purification and properties of an L-arabinose dehydrogenase from Azospirillum brasilense. Can. J. Microbiol. 29 (1983) 242–246.
2.  Watanabe, S., Kodaki, T. and Makino, K. Cloning, expression, and characterization of bacterial L-arabinose 1-dehydrogenase involved in an alternative pathway of L-arabinose metabolism. J. Biol. Chem. 281 (2006) 2612–2623. [DOI] [PMID: 16326697]
3.  Johnsen, U., Sutter, J.M., Zaiss, H. and Schonheit, P. L-Arabinose degradation pathway in the haloarchaeon Haloferax volcanii involves a novel type of L-arabinose dehydrogenase. Extremophiles 17 (2013) 897–909. [DOI] [PMID: 23949136]
4.  Aro-Karkkainen, N., Toivari, M., Maaheimo, H., Ylilauri, M., Pentikainen, O.T., Andberg, M., Oja, M., Penttila, M., Wiebe, M.G., Ruohonen, L. and Koivula, A. L-arabinose/D-galactose 1-dehydrogenase of Rhizobium leguminosarum bv. trifolii characterised and applied for bioconversion of L-arabinose to L-arabonate with Saccharomyces cerevisiae. Appl. Microbiol. Biotechnol. 98 (2014) 9653–9665. [DOI] [PMID: 25236800]
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