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D-threo-aldose 1-dehydrogenase

In enzymology, -threo-aldose 1-dehydrogenase is an enzyme that catalyzes the chemical reaction

-threo-aldose + NAD<sup>+</sup> -threo-aldono-1,5-lactone + NADH + H<sup>+</sup>

Thus, the two substrates of this enzyme are -threo-aldose and NAD<sup>+</sup>, whereas its 3 products are -threo-aldono-1,5-lactone, NADH, and H<sup>+</sup>.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD<sup>+</sup> or NADP<sup>+</sup> as acceptor. The systematic name of this enzyme class is -threo-aldose:NAD<sup>+</sup> 1-oxidoreductase. Other names in common use include -fucose dehydrogenase, (2S,3R)-aldose dehydrogenase, dehydrogenase, -fucose, and -fucose (-arabinose) dehydrogenase. This enzyme participates in ascorbate and aldarate metabolism.

-threo-aldose 1-dehydrogenase is capable of oxidizing -glucose, -xylose, -arabinose, and -fucose, allowing Trinickia caryophylli, the organism from which it was first isolated, to use -Glucose as a source of energy. Oxidation of these monosaccharides is inhibited by their respective enantiomers.

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