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.
Publication types
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Animals
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Humans
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Nucleotidyltransferases / biosynthesis*
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Nucleotidyltransferases / chemistry*
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Nucleotidyltransferases / physiology
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Phylogeny
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Plant Extracts / chemistry*
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Plant Extracts / metabolism
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Plant Proteins / biosynthesis*
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Plant Proteins / chemistry*
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Plant Proteins / physiology
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Structural Homology, Protein*
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UTP-Glucose-1-Phosphate Uridylyltransferase / biosynthesis
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UTP-Glucose-1-Phosphate Uridylyltransferase / chemistry
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UTP-Glucose-1-Phosphate Uridylyltransferase / physiology
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Uridine Diphosphate Sugars / biosynthesis*
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Uridine Diphosphate Sugars / chemistry*
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Uridine Diphosphate Sugars / physiology
Substances
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Plant Extracts
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Plant Proteins
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Uridine Diphosphate Sugars
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Nucleotidyltransferases
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UDPacetylglucosamine pyrophosphorylase
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UTP-Glucose-1-Phosphate Uridylyltransferase