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Nucleic Acids Symposium Series 2005 49(1):309-310; doi:10.1093/nass/49.1.309
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© 2005 Oxford University Press

L-Arabinose 1-dehydrogenase: A novel enzyme involving in bacterial L-arabinose metabolism

Seiya Watanabe1,2,3, Tsutomu Kodaki2,3 and Keisuke Makino2,3,4

1 Faculty of Engineering, Kyoto University Kyotodaigakukatsura, Saikyou-ku, Kyoto 615-8530, Japan, 2 Institute of Advanced Energy, Kyoto University, Gokasyo, Uji, Kyoto 611-0011, Japan, 3 CREST, JST (Japan Science and Technology Agency), Gokasyo, Uji, Kyoto 611-0011, Japan, 4 International Innovation Center, Kyoto University, Yoshidahonmachi, Sakyo-ku, Kyoto 606-8501, Japan

Azospirillum brasiliense converts L-arabinose to {alpha}-ketoglutarate via five hypothetical enzymatic steps. We purified and characterized L-arabinose 1-dehydrogenase (EC 1.1.1.46) catalyzing conversion of L-arabinose to L-arabino-{gamma}-lactone as an enzyme involved in the first step of this L-arabinose metabolic pathway. The purified enzyme was preferred NADP+ to NAD+ as a coenzyme. Kinetic analysis revealed that the enzyme had a high catalytic efficiency for both L-arabinose and D-galactose and that the L-arabinose-specific configuration at C3 and C4 is important for a preference of the substrate sugar. The N-terminal and internal amino acid sequences had some similarity to glucose-fructose oxidoreductase, D-xylose 1-dehydorgenase and D-galactose 1-dehydorgenases.


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