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. 1992 Oct;100(2):552–556. doi: 10.1104/pp.100.2.552

The Enzymic Reduction of Glyoxylate and Hydroxypyruvate in Leaves of Higher Plants

Curtis V Givan 1,2, Leszek A Kleczkowski 1,2
PMCID: PMC1075593  PMID: 16653027

Abstract

Glyoxylate and hydroxypyruvate are metabolites involved in the pathway of carbon in photorespiration. The chief glyoxylate-reducing enzyme in leaves is now known to be a cytosolic glyoxylate reductase that uses NADPH as the preferred cofactor but can also use NADH. Glyoxylate reductase has been isolated from spinach leaves, purified to homogeneity, and characterized kinetically and structurally. Chloroplasts contain lower levels of glyoxylate reductase activity supported by both NADPH and NADH, but it is not yet known whether a single chloroplastic enzyme catalyzes glyoxylate reduction with both cofactors. The major hydroxypyruvate reductase activity of leaves has long been known to be a highly active enzyme located in peroxisomes; it uses NADH as the preferred cofactor. To a lesser extent, NADPH can also be used by the peroxisomal enzyme. A second hydroxypyruvate reductase enzyme is located in the cytosol; it preferentially uses NADPH but can also use NADH as cofactor. In a barley mutant deficient in peroxisomal hydroxypyruvate reductase, the NADPH-preferring cytosolic form of the enzyme permits sufficient rates of hydroxypyruvate reduction to support continued substrate flow through the terminal stages of the photosynthetic carbon oxidation (glycolate/glycerate) pathway. The properties and metabolic significance of the cytosolic and organelle-localized glyoxylate and hydroxypyruvate reductase enzymes are discussed.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Givan C. V., Joy K. W., Kleczkowski L. A. A decade of photorespiratory nitrogen cycling. Trends Biochem Sci. 1988 Nov;13(11):433–437. doi: 10.1016/0968-0004(88)90217-4. [DOI] [PubMed] [Google Scholar]
  2. Heupel R., Markgraf T., Robinson D. G., Heldt H. W. Compartmentation studies on spinach leaf peroxisomes : evidence for channeling of photorespiratory metabolites in peroxisomes devoid of intact boundary membrane. Plant Physiol. 1991 Jul;96(3):971–979. doi: 10.1104/pp.96.3.971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Kleczkowski L. A., Edwards G. E., Blackwell R. D., Lea P. J., Givan C. V. Enzymology of the reduction of hydroxypyruvate and glyoxylate in a mutant of barley lacking peroxisomal hydroxypyruvate reductase. Plant Physiol. 1990 Oct;94(2):819–825. doi: 10.1104/pp.94.2.819. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Kleczkowski L. A., Edwards G. E. Identification of hydroxypyruvate and glyoxylate reductases in maize leaves. Plant Physiol. 1989 Sep;91(1):278–286. doi: 10.1104/pp.91.1.278. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Kleczkowski L. A., Givan C. V., Hodgson J. M., Randall D. D. Subcellular Location of NADPH-Dependent Hydroxypyruvate Reductase Activity in Leaf Protoplasts of Pisum sativum L. and Its Role in Photorespiratory Metabolism. Plant Physiol. 1988 Dec;88(4):1182–1185. doi: 10.1104/pp.88.4.1182. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Kleczkowski L. A., Randall D. D., Blevins D. G. Inhibition of Spinach Leaf NADPH(NADH)-Glyoxylate Reductase by Acetohydroxamate, Aminooxyacetate, and Glycidate. Plant Physiol. 1987 Jul;84(3):619–623. doi: 10.1104/pp.84.3.619. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Kleczkowski L. A., Randall D. D., Blevins D. G. 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. 1986 Nov 1;239(3):653–659. doi: 10.1042/bj2390653. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Kleczkowski L. A., Randall D. D., Edwards G. E. Oxalate as a potent and selective inhibitor of spinach (Spinacia oleracea) leaf NADPH-dependent hydroxypyruvate reductase. Biochem J. 1991 May 15;276(Pt 1):125–127. doi: 10.1042/bj2760125. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Kleczkowski L. A., Randall D. D. Purification and characterization of a novel NADPH(NADH)-dependent hydroxypyruvate reductase from spinach leaves. Comparison of immunological properties of leaf hydroxypyruvate reductases. Biochem J. 1988 Feb 15;250(1):145–152. doi: 10.1042/bj2500145. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Kohn L. D., Warren W. A. The kinetic properties of spinach leaf glyoxylic acid reductase. J Biol Chem. 1970 Aug 10;245(15):3831–3839. [PubMed] [Google Scholar]
  11. Lawyer A. L., Cornwell K. L., Gee S. L., Bassham J. A. Glyoxylate and glutamate effects on photosynthetic carbon metabolism in isolated chloroplasts and mesophyll cells of spinach. Plant Physiol. 1983 Jun;72(2):420–425. doi: 10.1104/pp.72.2.420. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Mulligan R. M., Wilson B., Tolbert N. E. Effects of glyoxylate on photosynthesis by intact chloroplasts. Plant Physiol. 1983 Jun;72(2):415–419. doi: 10.1104/pp.72.2.415. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Murray A. J., Blackwell R. D., Lea P. J. Metabolism of Hydroxypyruvate in a Mutant of Barley Lacking NADH-Dependent Hydroxypyruvate Reductase, an Important Photorespiratory Enzyme Activity. Plant Physiol. 1989 Sep;91(1):395–400. doi: 10.1104/pp.91.1.395. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. STAFFORD H. A., MAGALDI A., VENNESLAND B. The enzymatic reduction of hydroxypyruvic acid to D-glyceric acid in higher plants. J Biol Chem. 1954 Apr;207(2):621–629. [PubMed] [Google Scholar]
  15. Thompson C. M., Whittingham C. P. Intracellular localisation of phosphoglycollate phosphatase and glyoxalate reductase. Biochim Biophys Acta. 1967;143(3):642–644. doi: 10.1016/0005-2728(67)90074-6. [DOI] [PubMed] [Google Scholar]
  16. Tolbert N. E., Yamazaki R. K., Oeser A. Localization and properties of hydroxypyruvate and glyoxylate reductases in spinach leaf particles. J Biol Chem. 1970 Oct 10;245(19):5129–5136. [PubMed] [Google Scholar]
  17. Yu C., Huang A. H. Conversion of serine to glycerate in intact spinach leaf peroxisomes: role of malate dehydrogenase. Arch Biochem Biophys. 1986 Feb 15;245(1):125–133. doi: 10.1016/0003-9861(86)90196-7. [DOI] [PubMed] [Google Scholar]
  18. ZELITCH I., GOTTO A. M. Properties of a new glyoxylate reductase from leaves. Biochem J. 1962 Sep;84:541–546. doi: 10.1042/bj0840541. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. ZELITCH I. The isolation and action of crystalline glyoxylic acid reductase from tobacco leaves. J Biol Chem. 1955 Oct;216(2):553–575. [PubMed] [Google Scholar]

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