IUBMB Enzyme Nomenclature


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 reaction 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, CAS registry number:


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. [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. [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. [PMID: 25236800]

[EC created 2014, modified 2022]

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