A common structural blueprint for plant UDP-sugar-producing pyrophosphorylases

Kleczkowski LA, Geisler M, Fitzek E, Wilczynska M (2011)
Biochemical Journal 439(3): 375-381.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
 
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DOI
URN
urn:nbn:de:0070-pub-29208988
Autor*in
Kleczkowski, Leszek A.; Geisler, Matt; Fitzek, ElisabethUniBi; Wilczynska, Malgorzata
Einrichtung
Fakultät für Biologie > Computational Biology
Abstract / Bemerkung
Plant pyrophosphorylases that are capable of producing UDP-sugars, key precursors for glycosylation reactions, include UDP-glucose pyrophosphorylases (A- and B-type), UDP-sugar pyrophosphorylase and UDP-N-acetylglucosamine pyrophosphorylase. Although not sharing significant homology at the amino acid sequence level, the proteins share a common structural blueprint. Their structures are characterized by the presence of the Rossmann fold in the central (catalytic) domain linked to enzyme-specific N-terminal and C-terminal domains, which may play regulatory functions. Molecular mobility between these domains plays an important role in substrate binding and catalysis. Evolutionary relationships and the role of (de)oligomerization as a regulatory mechanism are discussed.
Stichworte
oligomerization; protein structure; sugar activation; UDP-sugar synthesis
Erscheinungsjahr
2011
Zeitschriftentitel
Biochemical Journal
Band
439
Ausgabe
3
Seite(n)
375-381
ISSN
0264-6021
eISSN
1470-8728
Page URI
https://pub.uni-bielefeld.de/record/2920898

Zitieren

Kleczkowski LA, Geisler M, Fitzek E, Wilczynska M. A common structural blueprint for plant UDP-sugar-producing pyrophosphorylases. Biochemical Journal. 2011;439(3):375-381.
Kleczkowski, L. A., Geisler, M., Fitzek, E., & Wilczynska, M. (2011). A common structural blueprint for plant UDP-sugar-producing pyrophosphorylases. Biochemical Journal, 439(3), 375-381. doi:10.1042/bj20110730
Kleczkowski, Leszek A., Geisler, Matt, Fitzek, Elisabeth, and Wilczynska, Malgorzata. 2011. “A common structural blueprint for plant UDP-sugar-producing pyrophosphorylases”. Biochemical Journal 439 (3): 375-381.
Kleczkowski, L. A., Geisler, M., Fitzek, E., and Wilczynska, M. (2011). A common structural blueprint for plant UDP-sugar-producing pyrophosphorylases. Biochemical Journal 439, 375-381.
Kleczkowski, L.A., et al., 2011. A common structural blueprint for plant UDP-sugar-producing pyrophosphorylases. Biochemical Journal, 439(3), p 375-381.
L.A. Kleczkowski, et al., “A common structural blueprint for plant UDP-sugar-producing pyrophosphorylases”, Biochemical Journal, vol. 439, 2011, pp. 375-381.
Kleczkowski, L.A., Geisler, M., Fitzek, E., Wilczynska, M.: A common structural blueprint for plant UDP-sugar-producing pyrophosphorylases. Biochemical Journal. 439, 375-381 (2011).
Kleczkowski, Leszek A., Geisler, Matt, Fitzek, Elisabeth, and Wilczynska, Malgorzata. “A common structural blueprint for plant UDP-sugar-producing pyrophosphorylases”. Biochemical Journal 439.3 (2011): 375-381.
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11 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

UDP-Sugar Producing Pyrophosphorylases: Distinct and Essential Enzymes With Overlapping Substrate Specificities, Providing de novo Precursors for Glycosylation Reactions.
Decker D, Kleczkowski LA., Front Plant Sci 9(), 2018
PMID: 30662444
The structure-activity relationship of the salicylimide derived inhibitors of UDP-sugar producing pyrophosphorylases.
Decker D, Öberg C, Kleczkowski LA., Plant Signal Behav 13(8), 2018
PMID: 30125142
Identification and characterization of inhibitors of UDP-glucose and UDP-sugar pyrophosphorylases for in vivo studies.
Decker D, Öberg C, Kleczkowski LA., Plant J 90(6), 2017
PMID: 28273406
Substrate Specificity and Inhibitor Sensitivity of Plant UDP-Sugar Producing Pyrophosphorylases.
Decker D, Kleczkowski LA., Front Plant Sci 8(), 2017
PMID: 28970843
A quaternary mechanism enables the complex biological functions of octameric human UDP-glucose pyrophosphorylase, a key enzyme in cell metabolism.
Führing JI, Cramer JT, Schneider J, Baruch P, Gerardy-Schahn R, Fedorov R., Sci Rep 5(), 2015
PMID: 25860585
Overexpression of UDP-glucose pyrophosphorylase from Larix gmelinii enhances vegetative growth in transgenic Arabidopsis thaliana.
Li N, Wang L, Zhang W, Takechi K, Takano H, Lin X., Plant Cell Rep 33(5), 2014
PMID: 24408396
N-acetylglucosamine-1-P uridylyltransferase 1 and 2 are required for gametogenesis and embryo development in Arabidopsis thaliana.
Chen YH, Shen HL, Hsu PJ, Hwang SG, Cheng WH., Plant Cell Physiol 55(11), 2014
PMID: 25231969
Octamerization is essential for enzymatic function of human UDP-glucose pyrophosphorylase.
Führing J, Damerow S, Fedorov R, Schneider J, Münster-Kühnel AK, Gerardy-Schahn R., Glycobiology 23(4), 2013
PMID: 23254995
Genetic and structural validation of Aspergillus fumigatus UDP-N-acetylglucosamine pyrophosphorylase as an antifungal target.
Fang W, Du T, Raimi OG, Hurtado-Guerrero R, Urbaniak MD, Ibrahim AF, Ferguson MA, Jin C, van Aalten DM., Mol Microbiol 89(3), 2013
PMID: 23750903
Structure of the inositol-1-phosphate cytidylyltransferase from Thermotoga maritima.
Kurnasov OV, Luk HJ, Roberts MF, Stec B., Acta Crystallogr D Biol Crystallogr 69(pt 9), 2013
PMID: 23999304
Molecular insights into how a deficiency of amylose affects carbon allocation--carbohydrate and oil analyses and gene expression profiling in the seeds of a rice waxy mutant.
Zhang MZ, Fang JH, Yan X, Liu J, Bao JS, Fransson G, Andersson R, Jansson C, Åman P, Sun C., BMC Plant Biol 12(), 2012
PMID: 23217057

49 References

Daten bereitgestellt von Europe PubMed Central.

Biochemical genetics of nucleotide sugar interconversion reactions.
Reiter WD., Curr. Opin. Plant Biol. 11(3), 2008
PMID: 18486535

AUTHOR UNKNOWN, 0
Molecular cloning and characterization of a cDNA encoding poplar UDP-glucose dehydrogenase, a key gene of hemicellulose/pectin formation.
Johansson H, Sterky F, Amini B, Lundeberg J, Kleczkowski LA., Biochim. Biophys. Acta 1576(1-2), 2002
PMID: 12031484

AUTHOR UNKNOWN, 0
UDP-sugar pyrophosphorylase with broad substrate specificity toward various monosaccharide 1-phosphates from pea sprouts.
Kotake T, Yamaguchi D, Ohzono H, Hojo S, Kaneko S, Ishida HK, Tsumuraya Y., J. Biol. Chem. 279(44), 2004
PMID: 15326166
Properties and physiological functions of UDP-sugar pyrophosphorylase in Arabidopsis.
Kotake T, Hojo S, Yamaguchi D, Aohara T, Konishi T, Tsumuraya Y., Biosci. Biotechnol. Biochem. 71(3), 2007
PMID: 17341835
Biosynthesis of UDP-glucuronic acid in developing soybean embryos: possible role of UDP-sugar pyrophosphorylase
Litterer LynnA, Plaisance KathrynL, Schnurr JudyA, Storey KathleenK, Jung Hans-JoachimG, Gronwald JohnW, Somers DavidA., Physiol Plant 128(2), 2006
PMID: IND43835961
Characterization and expression of Arabidopsis UDP-sugar pyrophosphorylase.
Litterer LA, Schnurr JA, Plaisance KL, Storey KK, Gronwald JW, Somers DA., Plant Physiol. Biochem. 44(4), 2006
PMID: 16757173
Leishmania UDP-sugar pyrophosphorylase: the missing link in galactose salvage?
Damerow S, Lamerz AC, Haselhorst T, Fuhring J, Zarnovican P, von Itzstein M, Routier FH., J. Biol. Chem. 285(2), 2009
PMID: 19906649
Identification of a novel UDP-sugar pyrophosphorylase with a broad substrate specificity in Trypanosoma cruzi.
Yang T, Bar-Peled M., Biochem. J. 429(3), 2010
PMID: 20482518
UDP-sugar pyrophosphorylase: a new old mechanism for sugar activation.
Kleczkowski LA, Decker D, Wilczynska M., Plant Physiol. 156(1), 2011
PMID: 21444645
Identification and modification of the uridine-binding site of the UDP-GalNAc (GlcNAc) pyrophosphorylase.
Wang-Gillam A, Pastuszak I, Stewart M, Drake RR, Elbein AD., J. Biol. Chem. 275(2), 2000
PMID: 10625695
Crystal structures of two human pyrophosphorylase isoforms in complexes with UDPGlc(Gal)NAc: role of the alternatively spliced insert in the enzyme oligomeric assembly and active site architecture.
Peneff C, Ferrari P, Charrier V, Taburet Y, Monnier C, Zamboni V, Winter J, Harnois M, Fassy F, Bourne Y., EMBO J. 20(22), 2001
PMID: 11707391
Identification and characterization of a strict and a promiscuous N-acetylglucosamine-1-P uridylyltransferase in Arabidopsis.
Yang T, Echols M, Martin A, Bar-Peled M., Biochem. J. 430(2), 2010
PMID: 20557289
A phosphoglycerate to inorganic phosphate ratio is the major factor in controlling starch levels in chloroplasts via ADP-glucose pyrophosphorylase regulation.
Kleczkowski LA., FEBS Lett. 448(1), 1999
PMID: 10217430
Molecular cloning of the Leishmania major UDP-glucose pyrophosphorylase, functional characterization, and ligand binding analyses using NMR spectroscopy.
Lamerz AC, Haselhorst T, Bergfeld AK, von Itzstein M, Gerardy-Schahn R., J. Biol. Chem. 281(24), 2006
PMID: 16611637
Structure and dynamics of UDP-glucose pyrophosphorylase from Arabidopsis thaliana with bound UDP-glucose and UTP.
McCoy JG, Bitto E, Bingman CA, Wesenberg GE, Bannen RM, Kondrashov DA, Phillips GN Jr., J. Mol. Biol. 366(3), 2006
PMID: 17178129
Crystal structure of uridine-diphospho-N-acetylglucosamine pyrophosphorylase from Candida albicans and catalytic reaction mechanism.
Maruyama D, Nishitani Y, Nonaka T, Kita A, Fukami TA, Mio T, Yamada-Okabe H, Yamada-Okabe T, Miki K., J. Biol. Chem. 282(23), 2007
PMID: 17392279
Open and closed structures of the UDP-glucose pyrophosphorylase from Leishmania major.
Steiner T, Lamerz AC, Hess P, Breithaupt C, Krapp S, Bourenkov G, Huber R, Gerardy-Schahn R, Jacob U., J. Biol. Chem. 282(17), 2007
PMID: 17303565
A chloroplastic UDP-glucose pyrophosphorylase from Arabidopsis is the committed enzyme for the first step of sulfolipid biosynthesis.
Okazaki Y, Shimojima M, Sawada Y, Toyooka K, Narisawa T, Mochida K, Tanaka H, Matsuda F, Hirai A, Hirai MY, Ohta H, Saito K., Plant Cell 21(3), 2009
PMID: 19286968
Structural basis for the broad substrate range of the UDP-sugar pyrophosphorylase from Leishmania major.
Dickmanns A, Damerow S, Neumann P, Schulz EC, Lamerz AC, Routier FH, Ficner R., J. Mol. Biol. 405(2), 2010
PMID: 21073876
Molecular and kinetic characterization of two UDP-glucose pyrophosphorylases, products of distinct genes, from Arabidopsis.
Meng M, Wilczynska M, Kleczkowski LA., Biochim. Biophys. Acta 1784(6), 2008
PMID: 18395530
UDP-sugar pyrophosphorylase is essential for pollen development in Arabidopsis.
Schnurr JA, Storey KK, Jung HJ, Somers DA, Gronwald JW., Planta 224(3), 2006
PMID: 16557401
Rice UDP-glucose pyrophosphorylase1 is essential for pollen callose deposition and its cosuppression results in a new type of thermosensitive genic male sterility.
Chen R, Zhao X, Shao Z, Wei Z, Wang Y, Zhu L, Zhao J, Sun M, He R, He G., Plant Cell 19(3), 2007
PMID: 17400897
UDP-glucose pyrophosphorylase is not rate limiting, but is essential in Arabidopsis.
Meng M, Geisler M, Johansson H, Harholt J, Scheller HV, Mellerowicz EJ, Kleczkowski LA., Plant Cell Physiol. 50(5), 2009
PMID: 19366709
UDP-glucose pyrophosphorylase is rate limiting in vegetative and reproductive phases in Arabidopsis thaliana.
Park JI, Ishimizu T, Suwabe K, Sudo K, Masuko H, Hakozaki H, Nou IS, Suzuki G, Watanabe M., Plant Cell Physiol. 51(6), 2010
PMID: 20435647
The LPB1 gene is important for acclimation of Chlamydomonas reinhardtii to phosphorus and sulfur deprivation.
Chang CW, Moseley JL, Wykoff D, Grossman AR., Plant Physiol. 138(1), 2005
PMID: 15849300
Evidence for function of UDP galactose pyrophosphorylase in mice with absent galactose-1-phosphate uridyltransferase.
Wehrli S, Reynolds R, Segal S., Mol. Genet. Metab. 91(2), 2007
PMID: 17433749
Uridine diphosphate glucose pyrophosphorylase. IV. Crystallization and properties of the enzyme from human liver.
Knop JK, Hansen RG., J. Biol. Chem. 245(10), 1970
PMID: 5427280
Toward a blueprint for UDP-glucose pyrophosphorylase structure/function properties: homology-modeling analyses.
Geisler M, Wilczynska M, Karpinski S, Kleczkowski LA., Plant Mol. Biol. 56(5), 2004
PMID: 15803415
Sequence comparison and protein structure prediction.
Dunbrack RL Jr., Curr. Opin. Struct. Biol. 16(3), 2006
PMID: 16713709
Crystal structure of human Pus10, a novel pseudouridine synthase.
McCleverty CJ, Hornsby M, Spraggon G, Kreusch A., J. Mol. Biol. 373(5), 2007
PMID: 17900615
MultiSeq: unifying sequence and structure data for evolutionary analysis.
Roberts E, Eargle J, Wright D, Luthey-Schulten Z., BMC Bioinformatics 7(), 2006
PMID: 16914055
Structural basis for subunit assembly in UDP-glucose pyrophosphorylase from Saccharomyces cerevisiae.
Roeben A, Plitzko JM, Korner R, Bottcher UM, Siegers K, Hayer-Hartl M, Bracher A., J. Mol. Biol. 364(4), 2006
PMID: 17010990
A 17-amino acid insert changes UDP-N-acetylhexosamine pyrophosphorylase specificity from UDP-GalNAc to UDP-GlcNAc.
Wang-Gillam A, Pastuszak I, Elbein AD., J. Biol. Chem. 273(42), 1998
PMID: 9765219
Domain-specific determinants of catalysis/substrate binding and the oligomerization status of barley UDP-glucose pyrophosphorylase.
Meng M, Fitzek E, Gajowniczek A, Wilczynska M, Kleczkowski LA., Biochim. Biophys. Acta 1794(12), 2009
PMID: 19683599
Expression in Escherichia coli of UDP-glucose pyrophosphorylase cDNA from potato tuber and functional assessment of the five lysyl residues located at the substrate-binding site.
Katsube T, Kazuta Y, Tanizawa K, Fukui T., Biochemistry 30(35), 1991
PMID: 1909568
Oligomerization status, with the monomer as active species, defines catalytic efficiency of UDP-glucose pyrophosphorylase.
Martz F, Wilczynska M, Kleczkowski LA., Biochem. J. 367(Pt 1), 2002
PMID: 12088504
Factors affecting oligomerization status of UDP-glucose pyrophosphorylase.
Kleczkowski LA, Martz F, Wilczynska M., Phytochemistry 66(24), 2005
PMID: 16289256
Analysis of the human protein interactome and comparison with yeast, worm and fly interaction datasets.
Gandhi TK, Zhong J, Mathivanan S, Karthick L, Chandrika KN, Mohan SS, Sharma S, Pinkert S, Nagaraju S, Periaswamy B, Mishra G, Nandakumar K, Shen B, Deshpande N, Nayak R, Sarker M, Boeke JD, Parmigiani G, Schultz J, Bader JS, Pandey A., Nat. Genet. 38(3), 2006
PMID: 16501559
UDP-glucose pyrophosphorylase. An old protein with new tricks.
Kleczkowski LA, Geisler M, Ciereszko I, Johansson H., Plant Physiol. 134(3), 2004
PMID: 15020755
Structural basis for the reaction mechanism of UDP-glucose pyrophosphorylase.
Kim H, Choi J, Kim T, Lokanath NK, Ha SC, Suh SW, Hwang HY, Kim KK., Mol. Cells 29(4), 2010
PMID: 20238176
Expression, purification, and characterization of a functionally active Mycobacterium tuberculosis UDP-glucose pyrophosphorylase.
Lai X, Wu J, Chen S, Zhang X, Wang H., Protein Expr. Purif. 61(1), 2008
PMID: 18621545
UDPglucose pyrophosphorylase from Xanthomonas spp. Characterization of the enzyme kinetics, structure and inactivation related to oligomeric dissociation.
Bosco MB, Machtey M, Iglesias AA, Aleanzi M., Biochimie 91(2), 2008
PMID: 18926872
Disease-associated carbohydrate-recognising proteins and structure-based inhibitor design.
von Itzstein M., Curr. Opin. Struct. Biol. 18(5), 2008
PMID: 18706999
Designing focused chemical libraries enriched in protein-protein interaction inhibitors using machine-learning methods.
Reynes C, Host H, Camproux AC, Laconde G, Leroux F, Mazars A, Deprez B, Fahraeus R, Villoutreix BO, Sperandio O., PLoS Comput. Biol. 6(3), 2010
PMID: 20221258

AUTHOR UNKNOWN, 0

Bates, Proteins 5(), 2001
VMD: visual molecular dynamics.
Humphrey W, Dalke A, Schulten K., J Mol Graph 14(1), 1996
PMID: 8744570
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