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In enzymology, a glucuronate reductase (EC 1.1.1.19) is an enzyme that catalyzes the chemical reaction

L-gulonate + NADP ${\displaystyle \rightleftharpoons }$ D-glucuronate + NADPH + H

Thus, the two substrates of this enzyme are L-gulonate and NADP, whereas its 3 products are D-glucuronate, NADPH, 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 L-gulonate:NADP 6-oxidoreductase. Other names in common use include aldehyde reductase, L-hexonate:NADP dehydrogenase, TPN-L-gulonate dehydrogenase, aldehyde reductase II, NADP-L-gulonate dehydrogenase, D-glucuronate dehydrogenase, D-glucuronate reductase, and L-glucuronate reductase (incorrect). This enzyme participates in pentose and glucuronate interconversions and ascorbate and aldarate metabolism.

References

• Sivak A, Hoffmann-Ostenhof O (1961). "Enzymes of mesoinositol catabolism in the yeast Schwanniomyces occidentalis". Biochim. Biophys. Acta. 53 (2): 426–8. doi:10.1016/0006-3002(61)90462-0. PMID 13913518.
• Jakoby, W. B. (Ed.), Enzymatic Basis of Detoxication, vol. 1, Academic Press, New York, 1980, p. 249–260.
• York JL, Grollman AP, Bublitz C (1961). "TPN-L-gluonate dehydrogenase". Biochim. Biophys. Acta. 47 (2): 298–306. doi:10.1016/0006-3002(61)90290-6. PMID 13787380.

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