Creative Enzymes offers services of enzyme activity measurement to customers in all industries. In the past few years, we have helped thousands of scientists accomplish testing of enzymatic activity. The accurate results and rapid services are testified by many customers. The exact assay method can measure virtually all oxidoreductases, including L-arabinose 1-dehydrogenase.

L-Arabinose 1-dehydrogenase belongs to the family of oxidoreductases. It uses NAD⁺ or NADP⁺ as the electron acceptor. The systematic name of this enzyme class is L-arabinose: NAD⁺ 1-oxidoreductase. The enzyme catalyzes the transformation from L-arabinose to L-arabinono-1,4-lactone, accompanied with generation of NADH.

L-Arabinose 1-dehydrogenase participates in ascorbate and aldarate metabolism. L-Arabinose is a major component of some plant tissues, and L-arabinose catabolism is therefore critical for microorganisms that use plant tissues as a carbon source. It is believed that there are two alternative pathways for bacterial L-arabinose metabolism. In the first pathway, L-arabinose is oxidized to L-arabino-γ-lactone by NAD(P)⁺-dependent dehydrogenase. The second pathway has the same initial three steps as the first pathway, but the products are glycoaldehyde and pyruvate. It has been reported that Azospirillum brasiliense, a bacterium, can grow on L-arabinose as the sole carbon source and has the first alternative pathway of L-arabinose metabolism. L-Arabinose 1-dehydrogenase, therefore, is thought to have significant potential in applications in agriculture and biotechnology industries, in the sense of regulating the bacterial activities. Unfortunately, other information about these alternative pathways of L-arabinose metabolism has not been identified so far. Yet little is known about this enzyme, which slows down future research aiming at commercial use of the enzyme. As the first step of product development, proper activity measurement of this enzyme is essential to support studies on applications. Creative Enzymes has developed reliable activity assays for L-arabinose 1-dehydrogenase using advanced equipment. The principle is to detect the catalytic activity of EC 1.1.1.46 in either the reduction of NAD⁺ at 260 nm or the oxidation of NADH at 340 nm, using spectrophotometric analysis.

Figure: Alternative pathways proposed by Novick and Tyler for A. brasiliense (first pathway). L-KDA is also converted to pyruvate and glycolaldehyde in several bacteria (second pathway).
Reference: Seiya Watanabe et al. J Biol Chem. 2006 281(5):2612-23

Creative Enzymes provides the best services of enzyme activity assays with professional teams. We offer accurate testing results with high reproducibility, which established our leading position is the enzyme service market. Overall, Creative Enzymes will continue to be your trust-worthy partner to support every possible applications and development activity.