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Literature summary for 5.3.1.1 extracted from

  • Walden, H.; Taylor, G.L.; Lorentzen, E.; Pohl, E.; Lilie, H.; Schramm, A.; Knura, T.; Stubbe, K.; Tjaden, B.; Hensel, R.
    Structure and function of a regulated archaeal triosephosphate isomerase adapted to high temperature (2004), J. Mol. Biol., 342, 861-875.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
structure of both a hexagonal and an orthorhombic crystal form to resolutions of 2.5 A and 2.3 A. In both crystal forms the enzyme exists as a tetramer of the (betaalpha)8-barrel. Hexagonal crystal form (crystallisation conditions 0.1 M Hepes–KOH (pH 7.5), 0.8 M sodium potassium phosphate) diffracts to 2.5 A and belongs to spacegroup P6(5)22/P6(1)22 with cell dimensions a = b = 186.9 A, c = 287.8 A, alpha = beta = 90°, gamma = 120°, suggesting two tetramers in the asymmetric unit. Orthorhombic crystals with cell dimensions a = 154.1 A, b = 91.0 A, c = 141.2 A, alpha = beta = gamma = 90° are obtained in 0.1 M sodium acetate (pH 4.6), 0.2 M ammonium sulfate, with PEG4000 at any concentration between 20% and 30% (w/v). Crystals grew within 48 hours at 20°C Thermoproteus tenax

Organism

Organism UniProt Comment Textmining
Thermoproteus tenax Q8NKN9
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Purification (Commentary)

Purification (Comment) Organism
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Thermoproteus tenax

Subunits

Subunits Comment Organism
More in solution the enzyme exhibits an equilibrium between inactive dimers and active tetramers Thermoproteus tenax

Synonyms

Synonyms Comment Organism
Triosephosphate isomerase
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Thermoproteus tenax