D-threo-aldose 1-dehydrogenase

{{DISPLAYTITLE:D-threo-aldose 1-dehydrogenase}}

{{infobox enzyme

| Name = {{sm|d}}-threo-aldose 1-dehydrogenase

| EC_number = 1.1.1.122

| CAS_number = 9082-70-6

| GO_code = 0047834

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In enzymology, {{sm|d}}-threo-aldose 1-dehydrogenase{{EC number|1.1.1.122}} is an enzyme that catalyzes the chemical reaction

: {{sm|d}}-threo-aldose + NAD⁺ $\backslash rightleftharpoons$ {{sm|d}}-threo-aldono-1,5-lactone + NADH + H⁺

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

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

{{sm|d}}-threo-aldose 1-dehydrogenase is capable of oxidizing L-Glucose, Xylose, Arabinose, and Fucose, allowing Trinickia caryophylli, the organism from which it was first isolated, to use L-Glucose as a source of energy. Oxidation of these monosaccharides is inhibited by their respective enantiomers.{{Cite journal |last=Sasajima |first=Ken-Ichi |last2=Sinskey |first2=Anthony J. |date=1979 |title=Oxidation of l-glucose by a Pseudomonad |url=https://linkinghub.elsevier.com/retrieve/pii/0005274479902328 |journal=Biochimica et Biophysica Acta (BBA) - Enzymology |language=en |volume=571 |issue=1 |pages=120–126 |doi=10.1016/0005-2744(79)90232-8|url-access=subscription }}