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.

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).

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.

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.


Key Publications
- Kleczkowski LA, Igamberdiev AU (2020) Optimization of nucleotide sugar supply for polysaccharide formation via thermodynamic buffering. Biochemical Journal 477: 341-356.
- Decker D, Kleczkowski LA (2019) UDP-sugar producing pyrophosphorylases – distinct and essential enzymes with overlapping substrate specificities, providing de novo precursors for glycosylation reactions. Frontiers in Plant Science 9:1822.
- Decker D, Kleczkowski LA (2017) Substrate specificity and inhibitor sensitivity of plant UDP-sugar producing pyrophosphorylases. Frontiers in Plant Science 8: 1610.
- Decker D, Öberg C, Kleczkowski LA (2017) Identification and characterization of inhibitors of UDP-glucose and UDP-sugar pyrophosphorylases for in vivo studies. Plant Journal 90: 1093–1107.
- Kleczkowski LA, Geisler M, Fitzek E, Wilczynska M (2011) A common structural blueprint for plant UDP-sugar producing pyrophosphorylases. Biochemical Journal 439: 375-379
CV Dr. Leszek A. Kleczkowski
- 1977: MSci, University of Warsaw, Poland
- 1977-1981: Junior Researcher, Agriculture University, Warsaw, Poland
- 1981-1985: PhD in biochemistry, University of Missouri, USA
- 1985-1986: Postdoc, University of Missouri, USA
- 1986-1987: Researcher, Agriculture University, Warsaw, Polan
- 1987-1988: Assistant Professor, Agriculture University, Warsaw, Poland
- 1988-1990: Postdoc, Washington State University, Pullman, USA
- 1990-1994: Project leader, Norwegian Research Council, Aas, Norway
- 1993: Habilitation thesis in plant biology, University of Warsaw, Poland
- 1994-2003: Associate Professor, Umeå University
- 2003-present: Professor, Umeå University
Publication list
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Magnesium Signaling in Plants
Int J Mol Sci. 2021, 22(3):1159 -
Optimization of nucleotide sugar supply for polysaccharide formation via thermodynamic buffering
Biochem J. 2020, 477(2):341-356 -
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 -
Thermodynamic buffering, stable non-equilibrium and establishment of the computable structure of plant metabolism
Prog Biophys Mol Biol. 2018, 146:23-26
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The structure-activity relationship of the salicylimide derived inhibitors of UDP-sugar producing pyrophosphorylases
Plant Signaling & Behavior 2018, 13(8):e1507406 -
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 -
Substrate Specificity and Inhibitor Sensitivity of Plant UDP-Sugar-Producing Pyrophosphorylases
Frontiers Plant Sciences 2017, 8:1610 -
Identification and characterization of inhibitors of UDP-glucose and UDP-sugar pyrophosphorylases for in vivo studies
Plant J. 2017, 90(6):1093-1107
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Defense responses in aspen with altered pectin methylesterase activity reveal the hormonal inducers of tyloses
Plant Physiol. 2017, 173(2):1409-1419
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The redox control of photorespiration: from biochemical and physiological aspects to biotechnological considerations
Plant Cell Environ. 2017, 40 (4):553-569
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Sugar activation for production of nucleotide sugars as substrates for glycosyltransferases in plants
J Appl Glycoscience 2015, 62(2):25-36 -
Hexokinase 1 is required for glucose-induced repression of bZIP63, At5g22920, and BT2 in Arabidopsis
Front Plant Sci. 2015, 6:525 -
Optimization of ATP synthase function in mitochondria and chloroplasts via the adenylate kinase equilibrium
Front. Plant Sci. 2015, 6:10
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Functional Dissection of Sugar Signals Affecting Gene Expression in Arabidopsis thaliana
PLoS One. 2014 Jun 20;9(6):e100312 -
A luminescence-based assay of UDP-sugar producing pyrophosphorylases
Anal. Methods, 2014, 6(1):57-61 -
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
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A common structural blueprint for plant UDP-sugar-producing pyrophosphorylases
Biochemical Journal: 2011, 439:375–379 -
Magnesium and cell energetics in plants under anoxia
Biochemical Journal: 2011, 437:373-379 -
Kleczkowski LA, Decker D, Wilczynska M
UDP-sugar pyrophosphorylase: a new old mechanism for sugar activation
Plant Physiology: 2011 156:3-10
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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
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Igamberdiev AU, Kleczkowski LA
Optimization of CO2 fixation in photosynthetic cells via thermodynamic buffering
Biosystems: 2011 103:224-229
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Kleczkowski LA, Kunz S, Wilczynska M
Mechanisms of UDP-glucose synthesis in plants
Critical Reviews in Plant Sciences: 2010 29:191-203
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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
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Igamberdiev AU, Kleczkowski LA
Metabolic systems maintain stable non-equilibrium via thermodynamic buffering
BioEssays: 2009 31:1091-1099
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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
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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
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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
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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
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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
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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
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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
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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 -
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 -
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 -
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 -
Kleczkowski LA, Martz F, Wilczynska M
Factors affecting oligomerization status of UDP-glucose pyrophosphorylase.
Phytochemistry: 2005 66:2815-2821
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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 -
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 -
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 -
Kleczkowski LA, Geisler M, Ciereszko I, Johansson H
UDP-glucose pyrophosphorylase. An old protein with new tricks
Plant Physiol: 2004 134:912-918 -
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 -
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 -
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 -
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 -
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 -
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 -
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 -
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 -
Kleczkowski LA
A new player in the starch field
Plant Physiology and Biochemistry: 2001 39:759-761 -
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 -
Kleczkowski LA
Is leaf ADP-glucose pyrophosphorylase an allosteric enzyme?
Biochimica Et Biophysica Acta-Protein Structure and Molecular Enzymology: 2000 1476:103-108 -
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 -
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 -
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 -
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 -
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 -
Luo C, Kleczkowski LA
Expression of barley ADP-glucose pyrophosphorylase in Escherichia coli: processing and regulatory considerations
Phytochemistry: 1999 50:209-214 -
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 -
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 -
Igamberdiev AU, Bykova NV, Kleczkowski LA
Origins and metabolism of formate in higher plants
Plant Physiology and Biochemistry: 1999 37:503-513 -
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 -
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 -
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 -
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 -
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
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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 -
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 -
Sokolov L, Dejardin A, Kleczkowski LA
Sugar-mediated regulation of ADP-glucose pyrophosphorylase genes in Arabidopsis
Plant Physiology: 1997 114:1294-1294 -
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 -
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 -
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 -
Eimert K, Villand P, Kleczkowski LA
Molecular characterization of UDP-glucose pyrophosphorylase from barley
Plant Physiology: 1996 111:119-119 -
Kleczkowski LA
Back to the drawing board: Redefining starch synthesis in cereals
Trends in Plant Science: 1996 1:363-364 -
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
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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 -
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 -
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 -
Villand P, Kleczkowski LA
Is there an alternative pathway for starch biosynthesis in cereal seeds?
Zeitschrift für Naturforschung: 1994 49c:215-219
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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
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Kleczkowski LA
Inhibitors of Photosynthetic Enzymes/Carriers and Metabolism
Annual Review of Plant Physiology and Plant Molecular Biology: 1994 45:339-367 -
Kleczkowski LA
Glucose Activation and Metabolism through Udp-Glucose Pyrophosphorylase in Plants
Phytochemistry: 1994 37:1507-1515 -
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
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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 -
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 -
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 -
Villand P, Olsen O-A, Kilian A, Kleczkowski LA
ADP-glucose pyrophosphorylase large subunit cDNA from barley endosperm.
Plant Physiology: 1992 100:1617-1618
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Kleczkowski LA, Edwards GE, Randall DD
Effects of oxalate on the reduction of hydroxypyruvate and glyoxylate in leaves.
Phytochemistry: 1992 31:51-54
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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 -
Givan CV, Kleczkowski LA
The Enzymatic Reduction of Glyoxylate and Hydroxypyruvate in Leaves of Higher-Plants
Plant Physiology: 1992 100:552-556 -
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 -
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 -
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 -
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 -
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
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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
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Kleczkowski LA, Edwards GE
Hysteresis and reversible cold inactivation of maize phosphoenolpyruvate carboxylase.
Zeitschrift für Naturforschung: 1990 45c:42-46
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Kleczkowski LA, Edwards GE
Identification of hydroxypyruvate and glyoxylate reductases in maize leaves.
Plant Physiology: 1989 91:278-286
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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.
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Kleczkowski LA, Loboda T, Nalborczyk E
Determination of photorespiration in higher plants (in Polish).
Wiadomosci Botaniczne: 1988 32:227-240
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Kleczkowski LA, Givan CV
Serine formation in leaves by mechanisms other than the glycolate pathway.
Journal of Plant Physiology: 1988 132:641-652
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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
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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
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Kleczkowski LA, Randall DD
Development of adenylate kinase activity upon greening of etiolated seedlings of C3 and C4 species.
Photosynthetica: 1988 22:112-115
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Kleczkowski LA, Randall DD
Purification and characterization of D-glycerate-3-kinase from maize leaves.
Planta: 1988 173:221-229
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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 -
Kleczkowski LA, Randall DD
Substrate Stereospecificity of Leaf Glycerate Kinase from C-3 and C-4 Plants
Phytochemistry: 1988 27:1269-1273 -
Givan CV, Joy KW, Kleczkowski LA
A decade of photorespiratory nitrogen cycling
Trends Biochem Sci: 1988 13:433-437 -
Kleczkowski LA
Rubisco activase and carboxyarabinitol phosphate - keys to photosynthesis? (in Polish).
Postepy Biochemii: 1987 33:629-633
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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
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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
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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 -
Kleczkowski LA, Randall DD
Maize leaf adenylate kinase: purification and partial characterization.
Plant Physiology: 1986 81:1110-1114
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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 -
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 -
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
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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