Lectins and glucanases exhibit the common property of reversibly binding to specific complex carbohydrates. The lectins/glucanases are a diverse group of proteins found in a wide range of species from prokaryotes to humans. The different family members all contain a concanavalin A-like domain, which consists of a sandwich of 12-14 beta strands in two sheets with a complex topology. Members of this family are diverse, and include the lectins: legume lectins, cereal lectins, viral lectins, and animal lectins. Plant lectins function in the storage and transport of carbohydrates in seeds, the binding of nitrogen-fixing bacteria to root hairs, the inhibition of fungal growth or insect feeding, and in hormonally regulated plant growth [1]. Protein members include concanavalin A (Con A), favin, isolectin I, lectin IV, soybean agglutinin and lentil lectin. Animal lectins include the galectins, which are S-type lactose-binding and IgE-binding proteins such as S-lectin, CLC protein, galectin1, galectin2, galectin3 CRD, and Congerin I [2].

Other members with a Con A-like domain include the glucanases. Bacterial and fungal beta-glucanases, such as Bacillus 1-3,1-4-beta-glucanse, carry out the acid catalysis of beta-glucans found in microorganisms and plants [3]. Similarly, kappa-Carrageenase degrades kappa-carrageenans from marine red algae cell walls [4].

1. The crystal structure of Canavalia brasiliensis lectin suggests a correlation between its quaternary conformation and its distinct biological properties from Concanavalin A. FEBS Lett. 405, 114-8
2. Charcot-Leyden crystal protein (galectin-10) is not a dual function galectin with lysophospholipase activity but binds a lysophospholipase inhibitor in a novel structural fashion. J. Biol. Chem. 277, 14859-68
3. Crystal structure of Bacillus licheniformis 1,3-1,4-beta-D-glucan 4-glucanohydrolase at 1.8 A resolution. FEBS Lett. 374, 221-4
4. The kappa-carrageenase of P. carrageenovora features a tunnel-shaped active site: a novel insight in the evolution of Clan-B glycoside hydrolases. Structure 9, 513-25

Lectins and glucanases exhibit the common property of reversibly binding to specific complex car
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