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 (2009)
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1794(12): 1734-1742.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
 
Download
Es wurden keine Dateien hochgeladen. Nur Publikationsnachweis!
DOI
Autor*in
Meng, Meng; Fitzek, ElisabethUniBi; Gajowniczek, Agnieszka; Wilczynska, Malgorzata; Kleczkowski, Leszek A.
Einrichtung
Fakultät für Biologie > Computational Biology
Erscheinungsjahr
2009
Zeitschriftentitel
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
Band
1794
Ausgabe
12
Seite(n)
1734-1742
ISSN
1570-9639
Page URI
https://pub.uni-bielefeld.de/record/2920900

Zitieren

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 (BBA) - Proteins and Proteomics. 2009;1794(12):1734-1742.
Meng, M., Fitzek, E., Gajowniczek, A., Wilczynska, M., & Kleczkowski, L. A. (2009). Domain-specific determinants of catalysis/substrate binding and the oligomerization status of barley UDP-glucose pyrophosphorylase. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 1794(12), 1734-1742. doi:10.1016/j.bbapap.2009.08.009
Meng, Meng, Fitzek, Elisabeth, Gajowniczek, Agnieszka, Wilczynska, Malgorzata, and Kleczkowski, Leszek A. 2009. “Domain-specific determinants of catalysis/substrate binding and the oligomerization status of barley UDP-glucose pyrophosphorylase”. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1794 (12): 1734-1742.
Meng, M., Fitzek, E., Gajowniczek, A., Wilczynska, M., and Kleczkowski, L. A. (2009). Domain-specific determinants of catalysis/substrate binding and the oligomerization status of barley UDP-glucose pyrophosphorylase. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1794, 1734-1742.
Meng, M., et al., 2009. Domain-specific determinants of catalysis/substrate binding and the oligomerization status of barley UDP-glucose pyrophosphorylase. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 1794(12), p 1734-1742.
M. Meng, et al., “Domain-specific determinants of catalysis/substrate binding and the oligomerization status of barley UDP-glucose pyrophosphorylase”, Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, vol. 1794, 2009, pp. 1734-1742.
Meng, M., Fitzek, E., Gajowniczek, A., Wilczynska, M., Kleczkowski, L.A.: Domain-specific determinants of catalysis/substrate binding and the oligomerization status of barley UDP-glucose pyrophosphorylase. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1794, 1734-1742 (2009).
Meng, Meng, Fitzek, Elisabeth, Gajowniczek, Agnieszka, Wilczynska, Malgorzata, and Kleczkowski, Leszek A. “Domain-specific determinants of catalysis/substrate binding and the oligomerization status of barley UDP-glucose pyrophosphorylase”. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1794.12 (2009): 1734-1742.

13 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
Crystal structure and insights into the oligomeric state of UDP-glucose pyrophosphorylase from sugarcane.
Cotrim CA, Soares JSM, Kobe B, Menossi M., PLoS One 13(3), 2018
PMID: 29494650
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
Identification and characterization of UDP-glucose pyrophosphorylase in cyanobacteria Anabaena sp. PCC 7120.
Kawano Y, Sekine M, Ihara M., J Biosci Bioeng 117(5), 2014
PMID: 24231376
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
Oligomerization, membrane association, and in vivo phosphorylation of sugarcane UDP-glucose pyrophosphorylase.
Soares JS, Gentile A, Scorsato V, Lima Ada C, Kiyota E, Dos Santos ML, Piattoni CV, Huber SC, Aparicio R, Menossi M., J Biol Chem 289(48), 2014
PMID: 25320091
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
The crystal structure of human UDP-glucose pyrophosphorylase reveals a latch effect that influences enzymatic activity.
Yu Q, Zheng X., Biochem J 442(2), 2012
PMID: 22132858
Identification of a UDP-glucose pyrophosphorylase from cotton (Gossypium hirsutum L.) involved in cellulose biosynthesis in Arabidopsis thaliana.
Wang Q, Zhang X, Li F, Hou Y, Liu X, Zhang X., Plant Cell Rep 30(7), 2011
PMID: 21373794
UDP-sugar pyrophosphorylase: a new old mechanism for sugar activation.
Kleczkowski LA, Decker D, Wilczynska M., Plant Physiol 156(1), 2011
PMID: 21444645
A common structural blueprint for plant UDP-sugar-producing pyrophosphorylases.
Kleczkowski LA, Geisler M, Fitzek E, Wilczynska M., Biochem J 439(3), 2011
PMID: 21992098

References

Daten bereitgestellt von Europe PubMed Central.

Export

Markieren/ Markierung löschen
Markierte Publikationen

Open Data PUB

Web of Science

Dieser Datensatz im Web of Science®
Quellen

PMID: 19683599
PubMed | Europe PMC

Suchen in

Google Scholar