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| {{DISPLAYTITLE:Glyoxylate reductase (NADP<sup>+</sup>)}}
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| {{enzyme
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| | Name = glyoxylate reductase (NADP)
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| | EC_number = 1.1.1.79
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| | CAS_number = 37250-17-2
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| | IUBMB_EC_number = 1/1/1/79
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| | GO_code = 0030267
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| In [[enzymology]], a '''glyoxylate reductase (NADP<sup>+</sup>)''' ({{EC number|1.1.1.79}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]
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| :glycolate + NADP<sup>+</sup> <math>\rightleftharpoons</math> glyoxylate + NADPH + H<sup>+</sup> | |
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| Thus, the two [[substrate (biochemistry)|substrates]] of this enzyme are [[glycolate]] and [[nicotinamide adenine dinucleotide phosphate|NADP<sup>+</sup>]], whereas its 3 [[product (chemistry)|products]] are [[glyoxylate]], [[nicotinamide adenine dinucleotide phosphate|NADPH]], and [[hydrogen ion|H<sup>+</sup>]].
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| This enzyme belongs to the family of [[oxidoreductase]]s, 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 '''glycolate:NADP<sup>+</sup> oxidoreductase'''. Other names in common use include '''NADPH-glyoxylate reductase''', and '''glyoxylate reductase (NADP<sup>+</sup>)'''. This enzyme participates in [[pyruvate metabolism]] and [[glyoxylate and dicarboxylate metabolism]].
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| ==Structural studies==
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| As of late 2007, 3 [[tertiary structure|structures]] have been solved for this class of enzymes, with [[Protein Data Bank|PDB]] accession codes {{PDB link|2GCG}}, {{PDB link|2H1S}}, and {{PDB link|2Q50}}.
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| ==References==
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| {{reflist|1}}
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| * {{cite journal | author = Cartwright LN and Hullin RP | year = 1966 | title = Purification and properties of two glyoxylate reductases from a species of ''Pseudomonas'' | journal = Biochem. J. | volume = 101 | pages = 781–791 | pmid=16742459 | issue = 3 | pmc = 1270187}}
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| * {{cite journal | author = Kleczkowski LA, Randall DD, Blevins DG | year = 1986 | title = 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 | journal = Biochem. J. | volume = 239 | pages = 653–9 | pmid = 3548703 | issue = 3 | pmc = 1147336 }}
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| [[Category:EC 1.1.1]]
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| [[Category:NADPH-dependent enzymes]]
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| [[Category:Enzymes of known structure]]
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| {{1.1.1-enzyme-stub}}
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