title: L-Arabinose 1-dehydrogenase: a novel enzyme involving in bacterial L-arabinose metabolism.
abstract: 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-dehydrogenase and D-galactose 1-dehydrogenases.
authors.affiliation: Faculty of Engineering, Kyoto University Kyotodaigakukatsura, Saikyou-ku, Kyoto 615-8530, Japan.
authors.forename: Seiya
authors.initials: S
authors.lastname: Watanabe
authors.forename: Tsutomu
authors.initials: T
authors.lastname: Kodaki
authors.forename: Keisuke
authors.initials: K
authors.lastname: Makino
mesh_terms: D000595:Amino Acid Sequence; D001089:Arabinose / Q000737:chemistry / Q000378:metabolism*; D015806:Azospirillum brasilense / Q000201:enzymology*; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D002237:Carbohydrate Dehydrogenases / Q000737:chemistry / Q000378:metabolism*; D002384:Catalysis; D007700:Kinetics; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity
chemical_list: D001426:Bacterial Proteins; D001089:Arabinose; D002237:Carbohydrate Dehydrogenases; C033519:L-arabinose dehydrogenase