TreeGrafter-generated GO annotations
Combined Automated Annotation using Multiple IEA Methods
The eukaryotic UDP-N-acetylglucosamine pyrophosphorylases. Gene cloning, protein expression, and catalytic mechanism.
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Fungal and human UAP1 proteins have directly measured UDP-GlcNAc pyrophosphorylase activity and complement a yeast UAP1 deficiency.
"All the recombinant ScUap1p,
CaUap1p, and HsUap1p possessed UDP-N-acetylglucosamine pyrophosphorylase
activities in vitro."
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The founding UAP1 study establishes the N-acetylglucosamine phosphosugar substrate, distinguishing it from UDP-glucose pyrophosphorylase.
"The yeast Uap1p utilized N-acetylglucosamine-1-phosphate as
the substrate"
Frog-human UAP1 sequence and nucleotide-sugar contact mapping
UniProt record identifying the UDP-glucose pyrophosphorylase donor
Frozen exact-input ProtNLM output and UniProt sequence for Q6DCZ6
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.
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Human UAP1 structures establish nucleotide-sugar contacts and isoform-dependent architecture; conservation is mapped explicitly to frog Uap1.S.
"we
have solved the crystal structures of AGX1 and AGX2 in complexes with UDPGlcNAc"