AF031: Enolase

List allergens from this family:

Routes of exposure:
Include only IUIS approved allergens.

Biochemical properties

Enolases (2-phospho-D-glycerate hydrolases) are essential glycolytic enzymes that catalyze the interconversion of 2-phosphoglycerate and phosphoenolpyruvate [1].

Allergens from this family

Enolases are important allergens from various molds and some plants. They were shown to exhibit cross-reactivity to other fungal and plant enolases [2, 3, 4].



  1. Zhang E, Brewer JM, Minor W, Carreira LA, Lebioda L:
    Mechanism of enolase: the crystal structure of asymmetric dimer enolase-2-phospho-D-glycerate/enolase-phosphoenolpyruvate at 2.0 A resolution.
    Biochemistry 1997, 36, 12526-34. [PubMed] [Full Text]
  2. Simon-Nobbe B, Probst G, Kajava AV, Oberkofler H, Susani M, Crameri R, Ferreira F, Ebner C, Breitenbach M:
    IgE-binding epitopes of enolases, a class of highly conserved fungal allergens.
    J Allergy Clin Immunol 2000, 106, 887-95. [PubMed] [Full Text]
  3. Lai HY, Tam MF, Tang RB, Chou H, Chang CY, Tsai JJ, Shen HD:
    cDNA cloning and immunological characterization of a newly identified enolase allergen from Penicillium citrinum and Aspergillus fumigatus.
    Int Arch Allergy Immunol 2002, 127, 181-90. [PubMed] [Full Text]
  4. Wagner S, Breiteneder H, Simon-Nobbe B, Susani M, Krebitz M, Niggemann B, Brehler R, Scheiner O, Hoffmann-Sommergruber K:
    Hev b 9, an enolase and a new cross-reactive allergen from hevea latex and molds. Purification, characterization, cloning and expression.
    Eur J Biochem 2000, 267, 7006-14. [PubMed]


Links to Pfam

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

Pfam domain Pfam clan
PF00113 Enolase, C-terminal TIM barrel domain CL0256 Enolase like TIM barrel
PF03952 Enolase, N-terminal domain CL0227 Enolase N-terminal domain-like superfamily

Links to Wikipedia


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