AF032: Triosephosphate isomerase

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Biochemical properties

Triosephosphate isomerase (TIM) is the glycolytic enzyme that catalyzes the reversible interconversion of glyceraldehyde 3-phosphate and dihydroxyacetone phosphate. TIM plays an important role in several metabolic pathways and is essential for efficient energy production. It is a dimer of identical subunits, each of which is made up of about 250 amino acid residues and folds into an eight-stranded β-barrel (the TIM barrel), a wide-spread fold found in many enzyme families [1].

Allergens from this family

A TIM from wheat was identified as a minor allergen for patients with baker's asthma [2]. Allergenic TIMs were also detected in shrimps and mites [3].

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References

  1. Wierenga RK:
    The TIM-barrel fold: a versatile framework for efficient enzymes.
    FEBS Lett 2001, 492, 193-8. [PubMed]
  2. Rozynek P, Sander I, Appenzeller U, Crameri R, Baur X, Clarke B, Bruning T, Raulf-Heimsoth M:
    TPIS--an IgE-binding wheat protein.
    Allergy 2002, 57, 463. [PubMed]
  3. Bauermeister K, Wangorsch A, Garoffo LP, Reuter A, Conti A, Taylor SL, Lidholm J, Dewitt AM, Enrique E, Vieths S, Holzhauser T, Ballmer-Weber B, Reese G:
    Generation of a comprehensive panel of crustacean allergens from the North Sea Shrimp Crangon crangon.
    Mol Immunol 2011, 48, 1983-92. [PubMed] [Full Text]

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Links to Pfam

Family-defining Pfam domains (at least one of these domains is present in each family member):

Pfam domain Pfam clan
PF00121 Triosephosphate isomerase CL0036 Common phosphate binding-site TIM barrel superfamily

Links to Wikipedia

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