A common structural blueprint for plant UDP-sugar-producing pyrophosphorylases. Kleczkowski, L. A., Geisler, M., Fitzek, E., & Wilczynska, M. Biochemical Journal, 439(3):375–381, November, 2011. Paper doi abstract bibtex 1 download 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.
@article{kleczkowski_common_2011,
title = {A common structural blueprint for plant {UDP}-sugar-producing pyrophosphorylases},
volume = {439},
issn = {0264-6021, 1470-8728},
url = {https://portlandpress.com/biochemj/article/439/3/375/45641/A-common-structural-blueprint-for-plant},
doi = {10/dm53gk},
abstract = {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.},
language = {en},
number = {3},
urldate = {2021-06-08},
journal = {Biochemical Journal},
author = {Kleczkowski, Leszek A. and Geisler, Matt and Fitzek, Elisabeth and Wilczynska, Malgorzata},
month = nov,
year = {2011},
pages = {375--381},
}
Downloads: 1
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