Creative Enzymes is one of the few companies in the world that provide spectrophotometric assays for activity measurement of L-arabinitol 4-dehydrogenase. Our service team includes experienced enzymologists equipped with the latest models of UV/vis spectrometer. Creative Enzymes is able to perform precise and fast measurement of the enzymatic activity of L-arabinitol 4-dehydrogenase.

L-arabinitol 4-dehydrogenase (EC1.1.1.12; LAD; also known as pentitol-DPN dehydrogenase (ambiguous) and L-arabitol dehydrogenase) is an enzyme that catalyzes the oxidation of L-arabinitol, using NAD as the redox cofactor to produce L-xylulose. This enzyme is a member of the oxidoreductase family, more specifically, the oxidoreductases that catalyze the CH-OH group of the substrate and use NAD+ or NADP+ as the cofactor. The systematic name of this enzyme class is L-arabinitol:NAD+ 4-oxidoreductase (L-xylulose-forming). This enzyme plays an important role in the biological pathways such as pentose and glucuronate interconversions. It is also an essential enzyme in the fungal L-arabinose catabolic pathway. Therefore, L-arabinitol 4-dehydrogenase is used to develop recombinant organisms that convert L-arabinose into biofuels and other chemicals.

Although the enzyme holds a valuable function in many fields such as chemical and environmental industries, the activity assay has not been fully developed due to low availability of the substrate and the complex nature of the reaction mixture. Creative Enzymes is proud to provide the proper activity assay for L-arabinitol 4-dehydrogenase, based on years of experiences on testing and characterizing the enzymes. To help our customer’s development activities, Creative Enzymes offers spectrophotometric assays to accurately measure the enzymatic activity. Overall, Creative Enzymes is your trustworthy partner for activity measurement for L-arabinitol 4-dehydrogenase.

Figure: Ribbon diagram for the overall structure of LAD with bound NAD+ cofactor. The catalytic domain housing both catalytic and structural zinc ions is shown in blue, and the cofactor-binding domain is shown in magenta. The two zinc atoms are shown as green spheres, and the bound NAD+ cofactor is shown as a yellow ball-and-stick model.
Reference: Brian Bae, Ryan P. et. al., J. Mol. Biol. (2010) 402, 230-240