Glucuronate reductase

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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⁺ $\rightleftharpoons$ 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.

[edit] References

IUBMB entry for 1.1.1.19
BRENDA references for 1.1.1.19 (Recommended.)
PubMed references for 1.1.1.19
PubMed Central references for 1.1.1.19
Google Scholar references for 1.1.1.19
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Jakoby, W.B. (Ed.), Enzymatic Basis of Detoxication, vol. 1, Academic Press, New York, 1980, p. 249-260.
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