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Literature summary for 2.4.2.3 extracted from

  • Roosild, T.P.; Castronovo, S.; Villoso, A.; Ziemba, A.; Pizzorno, G.
    A novel structural mechanism for redox regulation of uridine phosphorylase 2 activity (2011), J. Struct. Biol., 176, 229-237.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
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Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
two crystallographic structures of human isoform UPP2 in distinctly active and inactive conformations, to 2.0 and 1.54 A resolution, respectively. The structures reveal that a conditional intramolecular disulfide bridge can form within the protein that dislocates critical phosphate-coordinating arginine residue R100 away from the active site, disabling the enzyme. The state of the disulfide bridge has further structural consequences for one face of the enzyme that suggest UPP2 may have additional functions in sensing and initiating cellular responses to oxidative stress Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens O95045
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-

Synonyms

Synonyms Comment Organism
UPP2
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Homo sapiens