TY  - JOUR
AB  - 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.
DA  - 2011
DO  - 10.1042/bj20110730
KW  - oligomerization
KW  - protein structure
KW  - sugar activation
KW  - UDP-sugar synthesis
LA  - eng
IS  - 3
M2  - 375
PY  - 2011
SN  - 0264-6021
SP  - 375-381
T2  - Biochemical Journal
TI  - A common structural blueprint for plant UDP-sugar-producing pyrophosphorylases
UR  - https://nbn-resolving.org/urn:nbn:de:0070-pub-29208988
Y2  - 2024-11-22T12:21:53
ER  -