Preliminary crystallographic studies of triosephosphate isomerase from the blood parasite Trypanosoma brucei brucei
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Structural Biology
Reference18 articles.
1. On the three-dimensional structure and catalytic mechanism of triose phosphate isomerase
2. Evolution of enzyme function and the development of catalytic efficiency
3. Primary Structure of Triosephosphate Isomerase from Bacillus stearothermophilus
4. Structure of chicken muscle triose phosphate isomerase determined crystallographically at 2.5Å resolution: using amino acid sequence data
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2. Sulfate ion interaction with ‘anion recognition’ short peptide motif at the N-terminus of an isolated helix: A conformational landscape;Journal of Structural Biology;2010-09
3. Crystal Structure of the K12M/G15A Triosephosphate Isomerase Double Mutant and Electrostatic Analysis of the Active Site;Biochemistry;1994-03-15
4. Overexpression of trypanosomal triosephosphate isomerase in Escherichia coli and characterisation of a dimer-interface mutant;European Journal of Biochemistry;1993-02
5. Structure of the complex between trypanosomal triosephosphate isomerase andN-hydroxy-4-phosphono-butanamide: Binding at the active site despite an “open” flexible loop conformation;Protein Science;1992-12
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