Research in my group is focused on elucidating mechanisms leading to formation of nucleotide- sugars (especially UDP-sugars), which are direct precursors to polysaccharides (e.g. sucrose, cellulose, hemicellulose). The function of relevant enzymes is elucidated both in vivo, using transgenic plants, but also wt plants with the use of specific inhibitors, and by studying purified proteins. Structure/ function properties of key enzymes are investigated, using site-directed mutagenesis, domain deletion approaches, specific inhibitors, etc.
Leszek Kleczkowski 1150

UDP-sugars are used in hundreds of glycosylation reactions (e.g. those forming sucrose, cell wall polysaccharides, etc.), and they represent the most important precursors for biomass production in nature. Thus, mechanisms of UDP-sugar formation, together with selected glycosyltransferases, may represent primary targets for biotechnological approaches aiming at increased biomass production for needs of agriculture, forestry and other industries. We are studying both genes and proteins responsible for UDP-sugar production, including those for UDP-Glc pyrophosphorylase (UGPase), sucrose synthase and, recently, UDP-sugar pyrophosphorylase (USPase) and UDP-N-acetylglucosamine pyrophosphorylase (UAGPase).

Some roles of UDP-sugars in  plants (Decker and Kleczkowski, 2019)Some roles of UDP-sugars in plants (Decker and Kleczkowski, 2019)

We are using transgenic plants with impaired expression of a given protein to elucidate its physiological role. Parameters studied include growth/development of transgenics, metabolite contents, physiological properties, co-expressed gene networks, etc. At the protein level, purified plant pyrophosphorylases are investigated with respect to molecular determinants of their substrate specificity and regulation, including effects of oligomerization and post-translational modifications. The enzymes differ in specificity for sugar and nucleotide portions of their substrates, and may be involved in distinct metabolic pathways.

Substrate specificity of UDP-sugar producing enzymes (Decker and Kleczkowski, 2019)Substrate specificity of UDP-sugar producing enzymes (Decker and Kleczkowski, 2019)

Properties of the enzymes are modified via site-directed mutagenesis and domain swapping. We have also identified several inhibitors of pyrophosphorylases, using a chemical library developed at the Department of Chemistry, Umeå University. Inhibitors are used to study the role of the target protein in selected physiological/ developmental processes in plant tissues/ cells (reverse chemical-genetics approach) and, possibly, as potential drugs against human protozoan pathogens (e.g. Leishmania, Trypanosoma). Since sugars are essential for UDP-sugar synthesis, we also investigate sugar-mediated regulation of plant gene expression, using both cell culture, pollen germination test, and whole plants.

Structures of plant UDP-sugar producing pyrophosphorylases (Kleczkowski et al., 2011)Structures of plant UDP-sugar producing pyrophosphorylases (Kleczkowski et al., 2011)
sweden_greySvensk samanfattning

Publication list

  1. Magnesium Signaling in Plants
    Int J Mol Sci. 2021, 22(3):1159
  2. Optimization of nucleotide sugar supply for polysaccharide formation via thermodynamic buffering
    Biochem J. 2020, 477(2):341-356
  3. UDP-Sugar Producing Pyrophosphorylases: Distinct and Essential Enzymes With Overlapping Substrate Specificities, Providing de novo Precursors for Glycosylation Reactions
    Front. Plant Sci. 2019, 9:1822
  4. Thermodynamic buffering, stable non-equilibrium and establishment of the computable structure of plant metabolism
    Prog Biophys Mol Biol. 2018, 146:23-26
  5. The structure-activity relationship of the salicylimide derived inhibitors of UDP-sugar producing pyrophosphorylases
    Plant Signaling & Behavior 2018, 13(8):e1507406
  6. The glycerate and phosphorylated pathways of serine synthesis in plants: the branches of plant glycolysis linking carbon and nitrogen metabolism
    Frontiers in Plant Science 2018, 9: 318
  7. Substrate Specificity and Inhibitor Sensitivity of Plant UDP-Sugar-Producing Pyrophosphorylases
    Frontiers Plant Sciences 2017, 8:1610
  8. Identification and characterization of inhibitors of UDP-glucose and UDP-sugar pyrophosphorylases for in vivo studies
    Plant J. 2017, 90(6):1093-1107
  9. Defense responses in aspen with altered pectin methylesterase activity reveal the hormonal inducers of tyloses
    Plant Physiol. 2017, 173(2):1409-1419
  10. The redox control of photorespiration: from biochemical and physiological aspects to biotechnological considerations
    Plant Cell Environ. 2017, 40 (4):553-569
  11. Sugar activation for production of nucleotide sugars as substrates for glycosyltransferases in plants
    J Appl Glycoscience 2015, 62(2):25-36
  12. Hexokinase 1 is required for glucose-induced repression of bZIP63, At5g22920, and BT2 in Arabidopsis
    Front Plant Sci. 2015, 6:525
  13. Optimization of ATP synthase function in mitochondria and chloroplasts via the adenylate kinase equilibrium
    Front. Plant Sci. 2015, 6:10
  14. Functional Dissection of Sugar Signals Affecting Gene Expression in Arabidopsis thaliana
    PLoS One. 2014 Jun 20;9(6):e100312
  15. A luminescence-based assay of UDP-sugar producing pyrophosphorylases
    Anal. Methods, 2014, 6(1):57-61
  16. Decker D, Meng M, Gornicka A, Hofer A, Wilczynska M, Kleczkowski LA
    Substrate kinetics and substrate effects on the quaternary structure of barley UDP-glucose pyrophosphorylase

    Phytochemistry 2012 79:39-45
  17. A common structural blueprint for plant UDP-sugar-producing pyrophosphorylases
    Biochemical Journal: 2011, 439:375–379
  18. Magnesium and cell energetics in plants under anoxia
    Biochemical Journal: 2011, 437:373-379
  19. Kleczkowski LA, Decker D, Wilczynska M
    UDP-sugar pyrophosphorylase: a new old mechanism for sugar activation
    Plant Physiology: 2011 156:3-10
  20. Granado-Yela C, Garcia-Verdugo C, Carrillo K, Rubio de Dasas R, Kleczkowski LA, Balaguer L
    Temporal matching among diurnal photosynthetic patterns within the crown of the evergreen sclerophyll Olea europaea L.
    Plant, Cell & Environment: 2011 34:800-810
  21. Igamberdiev AU, Kleczkowski LA
    Optimization of CO2 fixation in photosynthetic cells via thermodynamic buffering
    Biosystems: 2011 103:224-229
  22. Kleczkowski LA, Kunz S, Wilczynska M
    Mechanisms of UDP-glucose synthesis in plants
    Critical Reviews in Plant Sciences: 2010 29:191-203
  23. Meng M, Fitzek E, Gajowniczek A, Wilczynska M, Kleczkowski LA
    Domain-specific determinants of catalysis/substrate binding and the oligomerization status of barley UDP-glucose pyrophosphorylase
    Biochimica et Biophysica Acta - Proteins and Proteomics: 2009 1794:1734-1742
  24. Igamberdiev AU, Kleczkowski LA
    Metabolic systems maintain stable non-equilibrium via thermodynamic buffering

    BioEssays: 2009 31:1091-1099
  25. Meng M, Geisler M, Johansson H, Harholt J, Scheller HV, Mellerowicz E, Kleczkowski LA
    UDP-glucose pyrophosphorylase is not rate limiting, but is essential in Arabidopsis
    Plant Cell Physiology: 2009 50: 998-1011
  26. Jiménez MD, Pardos M, Puértolas J, Kleczkowski LA, Parados JA
    Deep shade alters the acclimation response to moderate water stress in Quercus suber L.
    Forestry: 2009 82:285-298
  27. Timm S, Nunes-Nesi A, Pärnik T, Morgenthal K, Wienkoop S, Keerberg O, Weckwerth W, Kleczkowski LA, Fernie AR, Bauwe H
    A cytosolic pathway for the conversion of hydroxypyruvate to glycerate during photorespiration in Arabidopsis
    The Plant Cell: 2008 20:2848-2859
  28. Meng M, Wilczynska M, Kleczkowski LA
    Molecular and kinetic characterization of two UDP-glucose pyrophosphorylases, products of distinct genes, from Arabidopsis
    Biochimica et Biophysica Acta - Proteins and Proteomics: 2008 1784:967-972
  29. Meng M, Geisler M, Johansson H, Mellerowicz EJ, Karpinski S, Kleczkowski LA
    Differential tissue/organ-dependent expression of two sucrose- and cold-responsive genes for UDP-glucose pyrophosphorylase in Populus
    Gene: 2007 389:186-195
  30. Meng M, Geisler M, Johansson H, Mellerowicz EJ, Karpinski S, Kleczkowski LA
    Differential tissue/organ-dependent expression of two sucrose- and cold-responsive genes for UDP-glucose pyrophosphorylase in Populus
    Gene: 2007 389:186-195
  31. Ciereszko I, Kleczkowski LA 
    Phosphate deficiency-dependent upregulation of UDP-glucose pyrophosphorylase genes is insensitive to ABA and ethylene status in Arabidopsis leaves.
    Acta Physiologiae Plantarum: 2006 28:387-393
  32. Igamberdiev AU, Kleczkowski LA
    Equilibration of adenylates in the mitochondrial intermembrane space maintains respiration and regulates cytosolic metabolism
    Journal Of Experimental Botany: 2006 57:2133-2141
  33. Geisler M, Kleczkowski LA, Karpinski S
    A universal algorithm for genome-wide in silicio identification of biologically significant gene promoter putative cis-regulatory-elements, identification of new elements for reactive oxygen species and sucrose signaling in Arabidopsis
    Plant J: 2006 45:384-398
  34. Goulas E, Schubert M, Kieselbach T, Kleczkowski LA, Gardestrom P, Schroder W, Hurry V
    The chloroplast lumen and stromal proteomes of Arabidopsis thaliana show differential sensitivity to short- and long-term exposure to low temperature
    Plant Journal: 2006 47:720-734
  35. Geisler-Lee J, Geisler M, Coutinho PM, Segerman B, Nishikubo N, Takahashi J, Aspeborg H, Djerbi S, Master E, Andersson-Gunneras S, Sundberg B, Karpinski S, Teeri TT, Kleczkowski LA, Henrissat B, Mellerowicz EJ
    Poplar carbohydrate-active enzymes. Gene identification and expression analyses
    Plant Physiology: 2006 140:946-962
  36. Kleczkowski LA, Martz F, Wilczynska M 
    Factors affecting oligomerization status of UDP-glucose pyrophosphorylase
    Phytochemistry: 2005 66:2815-2821
  37. Ciereszko I, Kleczkowski LA
    Expression of several genes involved in sucrose/starch metabolism as affected by different strategies to induce phosphate deficiency in Arabidopsis
    Acta Physiologiae Plantarum: 2005 27:147-155
  38. Ciereszko I, Johansson H, Kleczkowski LA
    Interactive effects of phosphate deficiency, sucrose and light/dark conditions on gene expression of UDP-glucose pyrophosphory lase in Arabidopsis
    Journal of Plant Physiology: 2005 162:343-353
  39. Geisler M, Wilczynska M, Karpinski S, Kleczkowski LA
    Toward a blueprint for UDP-glucose pyrophosphorylase structure/function properties: homology-modeling analyses
    Plant Mol Biol: 2004 56:783-794
  40. Kleczkowski LA, Geisler M, Ciereszko I, Johansson H
    UDP-glucose pyrophosphorylase. An old protein with new tricks
    Plant Physiol: 2004 134:912-918
  41. Igamberdiev AU, Kleczkowski LA
    Membrane potential, adenylate levels and Mg2+ are interconnected via adenylate kinase equilibrium in plant cells
    Biochimica Et Biophysica Acta-Bioenergetics: 2003 1607:111-119
  42. Siedlecka A, Ciereszko I, Mellerowicz E, Martz Fo, Chen J, Kleczkowski LA
    The small subunit ADP-glucose pyrophosphorylase ( ApS) promoter mediates okadaic acid-sensitive uidA expression in starch-synthesizing tissues and cells in Arabidopsis
    Planta: 2003 217:184-192
  43. Martz Fo, Wilczynska M, Kleczkowski LA
    Oligomerization status, with the monomer as active species, defines catalytic efficiency of UDP-glucose pyrophosphorylase
    Biochem J: 2002 367:295-300
  44. Ciereszko I, Kleczkowski LA
    Effects of phosphate deficiency and sugars on expression of rab18 in Arabidopsis: hexokinase-dependent and okadaic acid-sensitive transduction of the sugar signal
    Biochimica Et Biophysica Acta-Gene Structure and Expression: 2002 1579:43-49
  45. Johansson H, Sterky F, Amini B, Lundeberg J, Kleczkowski LA
    Molecular cloning and characterization of a cDNA encoding poplar UDP-glucose dehydrogenase, a key gene of hemicellulose/pectin formation
    Biochimica Et Biophysica Acta-Gene Structure and Expression: 2002 1576:53-58
  46. Ciereszko I, Kleczkowski LA
    Glucose and mannose regulate the expression of a major sucrose synthase gene in Arabidopsis via hexokinase-dependent mechanisms
    Plant Physiology and Biochemistry: 2002 40:907-911
  47. Ciereszko I, Johansson H, Kleczkowski LA
    Sucrose and light regulation of a cold-inducible UDP-glucose pyrophosphorylase gene via a hexokinase-independent and abscisic acid-insensitive pathway in Arabidopsis
    Biochem J: 2001 354:67-72
  48. Igamberdiev AU, Kleczkowski LA
    Implications of adenylate kinase-governed equilibrium of adenylates on contents of free magnesium in plant cells and compartments
    Biochem J: 2001 360:225-231
  49. Kleczkowski LA
    A new player in the starch field
    Plant Physiology and Biochemistry: 2001 39:759-761
  50. Ciereszko I, Johansson H, Hurry V, Kleczkowski LA
    Phosphate status affects the gene expression, protein content and enzymatic activity of UDP-glucose pyrophosphorylase in wild-type and pho mutants of Arabidopsis
    Planta: 2001 212:598-605
  51. Kleczkowski LA
    Is leaf ADP-glucose pyrophosphorylase an allosteric enzyme?
    Biochimica Et Biophysica Acta-Protein Structure and Molecular Enzymology: 2000 1476:103-108
  52. Thorbjornsen T, Villand P, Ramstad VE, Kleczkowski LA, Olsen OA, Opsahl-Ferstad HG
    Nucleotide sequence of the ADP-glucose pyrophosphorylase gene (Accession No. AJ239130) of barley (Hordeum vulgare L.), a gene involved in endosperm starch formation (PGR00-051)
    Plant Physiology: 2000 122:1457-1457
  53. Igamberdiev AU, Kleczkowski LA
    Capacity for NADPH/NADP turnover in the cytosol of barley seed endosperm: The role of NADPH-dependent hydroxypyruvate reductase
    Plant Physiology and Biochemistry: 2000 38:747-753
  54. Krupa Z, Siedlecka A, Kleczkowski LA
    Cadmium-affected level of inorganic phosphate in rye leaves influences Rubisco subunits
    Acta Physiologiae Plantarum: 1999 21:257-261
  55. Dejardin A, Sokolov LN, Kleczkowski LA
    Sugar/osmoticum levels modulate differential abscisic acid-independent expression of two stress-responsive sucrose synthase genes in Arabidopsis
    Biochemical Journal: 1999 344:503-509
  56. Kleczkowski LA
    A phosphoglycerate to inorganic phosphate ratio is the major factor in controlling starch levels in chloroplasts via ADP-glucose pyrophosphorylase regulation
    FEBS Lett: 1999 448:153-156
  57. Luo C, Kleczkowski LA
    Expression of barley ADP-glucose pyrophosphorylase in Escherichia coli: processing and regulatory considerations
    Phytochemistry: 1999 50:209-214
  58. Ito H, Sokolov LN, Kleczkowski LA, Okita TW
    The Arabidopsis thaliana ADP glucose pyrophosphorylase large subunit gene, adg2 (Accession No: AB022891). (PGR99-051)
    Plant Physiology: 1999 119:1568-1568
  59. Sterky F, Lundeberg J, Kleczkowski LA
    Cloning of a cDNA Encoding Soluble Inorganic Pyrophosphatase (Accession No. AF149116) From Cambium of Poplar (Populus tremula x tremuloides). (PGR99-095)
    Plant Physiology: 1999 120:934-934
  60. Igamberdiev AU, Bykova NV, Kleczkowski LA
    Origins and metabolism of formate in higher plants
    Plant Physiology and Biochemistry: 1999 37:503-513
  61. Kleczkowski LA, Sokolov LN, Luo C, Villand P
    Molecular cloning and spatial expression of an ApL1 cDNA for the large subunit of ADP-glucose pyrophosphorylase from Arabidopsis thaliana
    Zeitschrift Fur Naturforschung C-a Journal of Biosciences: 1999 54:353-358
  62. Siedlecka A, Gardestrom P, Samuelsson G, Kleczkowski LA, Krupa Z
    A relationship between carbonic anhydrase and rubisco in response to moderate cadmium stress during light activation of photosynthesis
    Zeitschrift Fur Naturforschung C-a Journal of Biosciences: 1999 54:759-763
  63. Sokolov LN, Dejardin A, Kleczkowski LA
    Sugars and light/dark exposure trigger differential regulation of ADP-glucose pyrophosphorylase genes in Arabidopsis thaliana (thale cress)
    Biochemical Journal: 1998 336:681-687
  64. Sterky F, Sievertzon M, Kleczkowski LA
    Molecular Cloning of a cDNA Encoding a Cytosolic Form of Phosphoglucomutase (Accession No. AF097938) From Cambium of Poplar (Populus tremula x tremuloides) (PGR98-205)
    Plant Physiology: 1998 118:1535-1535
  65. Igamberdiev AU, Kleczkowski LA 
    Glyoxylate metabolism during photorespiration - a cytosol connection.
    In Handbook of Photosynthesis, Pessarakli M. ed., Marcel Dekker, Inc: 1997, pp. 269-279
  66. Eimert K, Luo C, Dejardin A, Villand P, Thorbjornsen T, Kleczkowski LA
    Molecular cloning and expression of the large subunit of ADP-glucose pyrophosphorylase from barley (Hordeum vulgare) leaves
    Gene: 1997 189:79-82
  67. Luo C, Dejardin A, Villand P, Kleczkowski LA
    Expression of homologues of barley ADP-glucose pyrophosphorylase in E-coli
    Plant Physiology: 1997 114:1215-1215
  68. Sokolov L, Dejardin A, Kleczkowski LA
    Sugar-mediated regulation of ADP-glucose pyrophosphorylase genes in Arabidopsis
    Plant Physiology: 1997 114:1294-1294
  69. Luo H, Dejardin A, Villand P, Doan DNP, Kleczkowski LA
    Differential processing of homologues of the small subunit of ADP-glucose pyrophosphorylase from barley (Hordeum vulgare) tissues
    Zeitschrift Fur Naturforschung C-a Journal of Biosciences: 1997 52:807-811
  70. Thorbjornsen T, Villand P, Kleczkowski LA, Olsen OA
    A single gene encodes two different transcripts for the ADP-glucose pyrophosphorylase small subunit from barley (Hordeum vulgare)
    Biochem J: 1996 313:149-154
  71. Eimert K, Villand P, Kilian A, Kleczkowski LA
    Cloning and characterization of several cDNAs for UDP-glucose pyrophosphorylase from barley (Hordeum vulgare) tissues
    Gene: 1996 170:227-232
  72. Eimert K, Villand P, Kleczkowski LA
    Molecular characterization of UDP-glucose pyrophosphorylase from barley
    Plant Physiology: 1996 111:119-119
  73. Kleczkowski LA
    Back to the drawing board: Redefining starch synthesis in cereals
    Trends in Plant Science: 1996 1:363-364
  74. Olsen O-A, Brown R, Kalla R, Kleczkowski LA, Lemmon B, Linnestad C, Nielsen PS, Potter R, Shimamoto K, Thorbjørnsen T, Villand P 
    Developmental regulation of gene expression during barley endosperm formation.
    Journal of Plant Physiology: 1995 145:587-591
  75. Kwiatkowski BA, Zielinskakwiatkowska AG, Migdalski A, Kleczkowski LA, Wasilewska LD
    Cloning of 2 Cdnas Encoding Calnexin-Like and Calreticulin-Like Proteins from Maize (Zea-Mays) Leaves - Identification of Potential Calcium-Binding Domains
    Gene: 1995 165:219-222
  76. Kleczkowski LA, Villand P, Eimert K
    A Possible Source of Ppi for the Sucrose to Starch Conversion in Cereal Seeds
    Plant Physiology: 1995 108:31-31
  77. Kleczkowski LA
    Kinetics and Regulation of the Nad(P)H-Dependent Glyoxylate-Specific Reductase from Spinach Leaves
    Zeitschrift Fur Naturforschung C-a Journal of Biosciences: 1995 50:21-28
  78. Villand P, Kleczkowski LA
    Is there an alternative pathway for starch biosynthesis in cereal seeds?
    Zeitschrift für Naturforschung: 1994 49c:215-219
  79. Kilian A, Kleinhofs A, Villand P, Thorbjørnsen T, Olsen O-A, Kleczkowski LA
    Mapping of ADP-glucose pyrophosphorylase genes from barley.
    Theoretical and Applied Genetics: 1994 87:869-871
  80. Kleczkowski LA
    Inhibitors of Photosynthetic Enzymes/Carriers and Metabolism
    Annual Review of Plant Physiology and Plant Molecular Biology: 1994 45:339-367
  81. Kleczkowski LA
    Glucose Activation and Metabolism through Udp-Glucose Pyrophosphorylase in Plants
    Phytochemistry: 1994 37:1507-1515
  82. Kleczkowski LA, Villand P, Olsen O-A 
    Hysteresis and reversible cold inactivation of ADP-glucose pyrophosphorylase from barley seed endosperm.
    Zeitschrift für Naturforschung: 1993  48c:457-460
  83. Kleczkowski LA, Villand P, Preiss J, Olsen OA
    Kinetic mechanism and regulation of ADP-glucose pyrophosphorylase from barley (Hordeum vulgare) leaves
    J Biol Chem: 1993 268:6228-6233
  84. Villand P, Olsen OA, Kleczkowski LA
    Molecular Characterization of Multiple Cdna Clones for Adp-Glucose Pyrophosphorylase from Arabidopsis-Thaliana
    Plant Molecular Biology: 1993 23:1279-1284
  85. Kleczkowski LA, Villand P, Luthi E, Olsen OA, Preiss J
    Insensitivity of Barley Endosperm Adp-Glucose Pyrophosphorylase to 3-Phosphoglycerate and Orthophosphate Regulation
    Plant Physiology: 1993 101:179-186
  86. Villand P, Olsen O-A, Kilian A, Kleczkowski LA
    ADP-glucose pyrophosphorylase large subunit cDNA from barley endosperm.
    Plant Physiology: 1992 100:1617-1618

  87. Kleczkowski LA, Edwards GE, Randall DD
    Effects of oxalate on the reduction of hydroxypyruvate and glyoxylate in leaves.
    Phytochemistry: 1992 31:51-54
  88. Villand P, Aalen R, Olsen OA, Luthi E, Lonneborg A, Kleczkowski LA
    Pcr Amplification and Sequences of Cdna Clones for the Small and Large Subunits of Adp-Glucose Pyrophosphorylase from Barley Tissues
    Plant Molecular Biology: 1992 19:381-389
  89. Givan CV, Kleczkowski LA
    The Enzymatic Reduction of Glyoxylate and Hydroxypyruvate in Leaves of Higher-Plants
    Plant Physiology: 1992 100:552-556
  90. Kleczkowski LA, Randall DD, Edwards GE
    Oxalate as a Potent and Selective Inhibitor of Spinach (Spinacia-Oleracea) Leaf Nadph-Dependent Hydroxypyruvate Reductase
    Biochemical Journal: 1991 276:125-127
  91. Kleczkowski LA, Randall DD
    Equilibration of Adenylates by Maize Leaf Adenylate Kinase - Effects of Magnesium on Apparent and True Equilibria
    Journal of Experimental Botany: 1991 42:537-540
  92. Kleczkowski LA, Edwards GE
    A Low Temperature-Induced Reversible Transition between Different Kinetic Forms of Maize Leaf Phosphoenolpyruvate Carboxylase
    Plant Physiology and Biochemistry: 1991 29:9-17
  93. Kleczkowski LA, Villand P, Lonneborg A, Olsen OA, Luthi E
    Plant Adp-Glucose Pyrophosphorylase - Recent Advances and Biotechnological Perspectives (a Review)
    Zeitschrift Fur Naturforschung C-a Journal of Biosciences: 1991 46:605-612
  94. Kleczkowski LA, Edwards GE, Blackwell RD, Lea PJ, Givan CV 
    Enzymology of the reduction of hydroxypyruvate and glyoxylate in a mutant of barley lacking peroxisomal hydroxypyruvate reductase.
    Plant Physiology: 1990 94:819-825
  95. Kleczkowski LA, Randall DD, Zahler WL 
    Adenylate kinase from maize leaves: true substrates, inhibition by P1,P5-di(adenosine-5')pentaphosphate, and kinetic mechanism.
    Zeitschrift für Naturforschung: 1990 45c:607-613
  96. Kleczkowski LA, Edwards GE 
    Hysteresis and reversible cold inactivation of maize phosphoenolpyruvate carboxylase.
    Zeitschrift für Naturforschung: 1990 45c:42-46
  97. Kleczkowski LA, Edwards GE 
    Identification of hydroxypyruvate and glyoxylate reductases in maize leaves.
    Plant Physiology: 1989 91:278-286
  98. Loboda T, Kleczkowski LA, Tarlowski J, Nalborczyk E 
    A transient stimulation of net photosynthesis of rye leaves by α-hydroxy-2-pyridinemethane sulfonic acid (α-HPMS) due to inhibition of photorespiratory CO2 release.
    Journal of Experimental Botany: 1988 39:1765-1770.
  99. Kleczkowski LA, Loboda T, Nalborczyk E 
    Determination of photorespiration in higher plants (in Polish).
    Wiadomosci Botaniczne: 1988 32:227-240
  100. Kleczkowski LA, Givan CV 
    Serine formation in leaves by mechanisms other than the glycolate pathway.
    Journal of Plant Physiology: 1988 132:641-652
  101. Kleczkowski LA, Givan CV, Randall DD, Loboda T 
    Substrate specificity and activities of glyoxylate and hydroxypyruvate reductases from leaf extracts: differentiation by ammonium sulfate fractionation and by immunoprecipitation.
    Physiologia Plantarum: 1988 74:763-769
  102. Kleczkowski LA, Givan CV, Hodgson JM, Randall DD 
    Subcellular location of NADPH-dependent hydroxypyruvate reductase activity in leaf protoplasts of Pisum sativum L. and its role in photorespiratory metabolism.
    Plant Physiology: 1988 88:1182- 1185
  103. Kleczkowski LA, Randall DD 
    Development of adenylate kinase activity upon greening of etiolated seedlings of C3 and C4 species.
    Photosynthetica: 1988 22:112-115
  104. Kleczkowski LA, Randall DD 
    Purification and characterization of D-glycerate-3-kinase from maize leaves.
    Planta: 1988 173:221-229
  105. Kleczkowski LA, Randall DD
    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 250:145-152
  106. Kleczkowski LA, Randall DD
    Substrate Stereospecificity of Leaf Glycerate Kinase from C-3 and C-4 Plants
    Phytochemistry: 1988 27:1269-1273
  107. Givan CV, Joy KW, Kleczkowski LA
    A decade of photorespiratory nitrogen cycling
    Trends Biochem Sci: 1988 13:433-437
  108. Kleczkowski LA 
    Rubisco activase and carboxyarabinitol phosphate - keys to photosynthesis? (in Polish).
    Postepy Biochemii: 1987 33:629-633
  109. Kleczkowski LA, Zeiher CA, Randall DD 
    Extrachloroplastic site of synthesis of three chloroplast proteins in maize (Zea mays L.).
    Zeitschrift für Naturforschung: 1987 42c:1113-1115
  110. Kleczkowski LA, Randall DD, Blevins DG 
    Inhibition of spinach leaf NADPH(NADH)-glyoxylate reductase by acetohydroxamate, aminooxyacetate and glycidate.
    Plant Physiology: 1987 84:619-623
  111. Kleczkowski LA, Randall DD
    Immunologically Distinct Forms of Adenylate Kinase in Leaves - Comparison of Subunit Size of Adenylate Kinase from C-3 and C-4 Plants
    Journal of Experimental Botany: 1987 38:1440-1445
  112. Kleczkowski LA, Randall DD 
    Maize leaf adenylate kinase: purification and partial characterization.
    Plant Physiology: 1986 81:1110-1114
  113. Kleczkowski LA, Randall DD, Blevins DG
    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 239:653-659
  114. Kleczkowski LA, Randall DD
    Thiol-Dependent Regulation of Glycerate Metabolism in Leaf Extracts - the Role of Glycerate Kinase in C-4 Plants
    Plant Physiology: 1986 81:656-662
  115. Kleczkowski LA, Randall DD 
    Light and thiol activation of maize leaf glycerate kinase. The stimulating effect of reduced thioredoxins and ATP.
    Plant Physiology 1985 79:274-277
  116. Kleczkowski LA, Randall DD, Zahler WL
    The substrate specificity, kinetics, and mechanism of glycerate-3-kinase from spinach leaves
    Arch Biochem Biophys: 1985 236:185-194