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词条 Glyoxylate reductase (NADP+)
释义

  1. Structural studies

  2. References

{{DISPLAYTITLE:Glyoxylate reductase (NADP+)}}{{enzyme
| Name = glyoxylate reductase (NADP)
| EC_number = 1.1.1.79
| CAS_number = 37250-17-2
| IUBMB_EC_number = 1/1/1/79
| GO_code = 0030267
| image =
| width =
| caption =
}}

In enzymology, a glyoxylate reductase (NADP+) ({{EC number|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.

Structural studies

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

References

  • {{cite journal |author1 = Cartwright LN |author2 =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}}
  • {{cite journal | vauthors = 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 }}
{{Alcohol oxidoreductases}}{{Enzymes}}{{Portal bar|Molecular and Cellular Biology|border=no}}{{1.1.1-enzyme-stub}}

3 : EC 1.1.1|NADPH-dependent enzymes|Enzymes of known structure

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