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Literature summary for 5.3.1.1 extracted from

  • Aparicio, R.; Ferreira, S.T.; Polikarpov, I.
    Closed conformation of the active site loop of rabbit muscle triosephosphate isomerase in the absence of substrate: evidence of conformational heterogeneity (2003), J. Mol. Biol., 334, 1023-1041.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop vapor diffusion method, apo-enzyme structure, refined to 1.5 A resolution, in which the active site loop is either in the open or in the closed conformation in different subunits of the enzyme. The observation of both open and closed lid conformations in triosephosphate isomerase crystals might by related to a persistent conformational heterogeneity of the protein in solution Oryctolagus cuniculus

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus P00939
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Source Tissue

Source Tissue Comment Organism Textmining