Beta-mannosidase

Beta-mannosidase is a lysosomal exoglycosidase enzyme belonging to the glycoside hydrolase family 2 (GH2)[4][3][6]. It catalyzes the hydrolysis of terminal, non-reducing β-D-mannose residues from β-D-mannosides, playing a key role as the final exoglycosidase in the lysosomal pathway for N-linked glycoprotein oligosaccharide catabolism[4]. The human enzyme is encoded by the MANBA gene and is essential for the degradation of complex carbohydrates in glycoproteins and hemicellulose-derived polysaccharides. Structural studies reveal a (β/α)_8_ barrel catalytic domain and multiple auxiliary domains, forming a trimeric or dimeric protein depending on the organism[2][5][3]. Deficiency of beta-mannosidase activity leads to the lysosomal storage disorder beta-mannosidosis, characterized by neurological impairment and accumulation of oligosaccharides in tissues[4][5]. Several experimental inhibitors are described, providing insight into the enzyme’s mechanism and potential for targeted intervention in disease or biotechnology[2].

Other names

β-mannosidasebeta-mannosidaseβ-D-mannosidaseβ-mannoside mannohydrolaseexo-β-D-mannanaselysosomal beta A mannosidasemannanasemannase

Competitive inhibition of enzymatic activity (by inhibitors such as mannoimidazole, noeuromycin, DNP-2FM); Glycosyl-enzyme intermediate formation and slow turnover (mechanism-based inhibition by DNP-2FM)