| Symbol: | Glyco_hydro_38 |
| Glycosyl hydrolases family 38 N-terminal domain | |
| Pfam: | PF01074 |
| Pfam Clan: | CL0158 |
| Interpro: | IPR000602 |
| Scop: | 1o7d |
| Cazy: | GH38 |
| Membranome Superfamily: | 311 |
| Symbol: | Alpha-mann_mid |
| Alpha mannosidase, middle domain | |
| Pfam: | PF09261 |
| Interpro: | IPR015341 |
| Scop: | 1o7d |
| Symbol: | Glyco_hydro_38C |
| Glycosyl hydrolases family 38 C-terminal domain | |
| Pfam: | PF07748 |
| Pfam Clan: | CL0103 |
| Interpro: | IPR011682 |
| Scop: | 1o7d |
| Cazy: | GH38 |
In molecular biology, glycoside hydrolase family 38 is a family of glycoside hydrolases.
Glycoside hydrolases are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycoside hydrolases, based on sequence similarity, has led to the definition of >100 different families.[1] [2] [3] This classification is available on the CAZy web site,[4] [5] and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.[6] [7]
Glycoside hydrolase family 38 CAZY GH_38 comprises enzymes with only one known activity; alpha-mannosidase .
Lysosomal alpha-mannosidase is necessary for the catabolism of N-linked carbohydrates released during glycoprotein turnover. The enzyme catalyzes the hydrolysis of terminal, non-reducing alpha-D-mannose residues in alpha-D-mannosides, and can cleave all known types of alpha-mannosidic linkages. Defects in the gene cause lysosomal alpha-mannosidosis (AM), a lysosomal storage disease characterised by the accumulation of unbranched oligo-saccharide chains.
A domain, which is found in the central region adopts a structure consisting of three alpha helices, in an immunoglobulin/albumin-binding domain-like fold. The domain is predominantly found in the enzyme alpha-mannosidase.[8]