InterPro: IPR018120 Glycoside hydrolase, family 1, active site

Glycoside hydrolase family 1 GH1 comprises enzymes with a number of known activities; beta-glucosidase (EC:3.2.1.21); beta-galactosidase (EC:3.2.1.23); 6-phospho-beta-galactosidase (EC:3.2.1.85); 6-phospho-beta-glucosidase (EC:3.2.1.86); lactase-phlorizin hydrolase (EC:3.2.1.62), (EC:3.2.1.108); beta-mannosidase (EC:3.2.1.25); myrosinase (EC:3.2.1.147).

One of the conserved regions in these enzymes is centred on a conserved glutamic acid residue which has been shown in the beta-glucosidase from Agrobacterium, to be directly involved in glycosidic bond cleavage by acting as a nucleophile. We have used this region as a signature pattern. As a second signature pattern we selected a conserved region, found in the N-terminal extremity of these enzymes, this region also contains a glutamic acid residue. This pattern will pick up the last two domains of LPH; the first two domains, which are removed from the LPH precursor by proteolytic processing, have lost the active site glutamate and may therefore be inactive [1].