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Literature summary extracted from

  • Salinas, S.R.; Petruk, A.A.; Brukman, N.G.; Bianco, M.I.; Jacobs, M.; Marti, M.A.; Ielpi, L.
    Binding of the substrate UDP-glucuronic acid induces conformational changes in the xanthan gum glucuronosyltransferase (2016), Protein Eng. Des. Sel., 29, 197-207.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.4.1.264 in silico-built models of GumK complexed with UDP-GlcA as well as its analogs UDP-glucose and UDP-galacturonic acid. UDP-GlcA binding to GumK triggers a change in the GumK tertiary structure, affecting N-terminal hydrophobic residues to generate or improve the lipid-derived acceptor substrate site, while UDP-GlcA accommodates the transfer reaction Xanthomonas campestris

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.264 Xanthomonas campestris Q8GCH2
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.264 additional information GumK undergoes a conformational change upon donor substrate binding, likely bringing the two Rossmann fold domains closer together and triggering a change in the N-terminal domain, with consequent generation of the acceptor substrate binding site Xanthomonas campestris ?
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 ?
2.4.1.264 UDP-alpha-D-glucuronate + D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphoundecaprenol
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 Xanthomonas campestris UDP + GlcA-beta-(1->2)-D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphoundecaprenol
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 ?

Synonyms

EC Number Synonyms Comment Organism
2.4.1.264 gumK
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 Xanthomonas campestris