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Literature summary for 5.3.1.1 extracted from

  • Alahuhta, M.; Salin, M.; Casteleijn, M.G.; Kemmer, C.; El-Sayed, I.; Augustyns, K.; Neubauer, P.; Wierenga, R.K.
    Structure-based protein engineering efforts with a monomeric TIM variant: the importance of a single point mutation for generating an active site with suitable binding properties (2008), Protein Eng. Des. Sel., 21, 257-266.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
monomeric enzyme variant with an engineered binding groove, m18bTIM, and the V233A mutant of this variant in complex with citrate, 2-phosphoglycolate, and glycerol 3-phosphate, to 1.89, 1.6, 2.3 and 2.0 A resolution, respectively Trypanosoma brucei

Protein Variants

Protein Variants Comment Organism
additional information introduction of mutation V233A into a monomeric enzyme variant with an engineered binding groove, m18bTIM. Mutation V233A restores the structural properties of loop-7, the binding site of a conserved water molecule between loop-7 and loop-8 and the binding site of the phosphate moiety of wild-type in the m18bTIM background. The active site of the V233A mutant can bind transition state analogs and suicide inhibitors competently, the catalytic efficiency of the V233A mutant is too low to be detected Trypanosoma brucei

Organism

Organism UniProt Comment Textmining
Trypanosoma brucei P04789
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