In enzymology, a glyoxylate reductase (NADP⁺) (EC 1.1.1.79) is an enzyme that catalyzes the chemical reaction

glycolate + NADP⁺ glyoxylate + NADPH + H⁺

Thus, the two substrates of this enzyme are glycolate and NADP⁺, whereas its 3 products are glyoxylate, 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 glycolate:NADP⁺ oxidoreductase. Other names in common use include NADPH-glyoxylate reductase, and glyoxylate reductase (NADP⁺). This enzyme participates in pyruvate metabolism and glyoxylate and dicarboxylate metabolism.

As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 2GCG, 2H1S, and 2Q50.

• Cartwright LN; Hullin RP (1966). "Purification and properties of two glyoxylate reductases from a species of Pseudomonas". Biochem. J. 101 (3): 781–791. doi:10.1042/bj1010781. PMC 1270187. PMID 16742459.
• Kleczkowski LA, Randall DD, Blevins DG (1986). "Purification and characterization of a novel NADPH(NADH)-dependent glyoxylate reductase from spinach leaves. Comparison of immunological properties of leaf glyoxylate reductase and hydroxypyruvate reductase". Biochem. J. 239 (3): 653–9. doi:10.1042/bj2390653. PMC 1147336. PMID 3548703.