Alpha-mannosidase (Jack bean) (JBM)

Jack bean alpha-mannosidase is a zinc-dependent glycosyl hydrolase (EC 3.2.1.24) purified from the seeds of the Jack bean plant, Canavalia ensiformis (UniProt: P80033). It belongs to the Glycosyl Hydrolase Family 38 (GH38) and is characterized by its ability to hydrolyze terminal, non-reducing alpha-D-mannose residues from various glycoconjugates (CAZy Database). In the field of glycobiology, this enzyme is a standard tool for the structural analysis and sequencing of N-linked oligosaccharides due to its broad substrate specificity. Although it is a plant-derived enzyme, it serves as a primary biochemical model for human alpha-mannosidases, which are involved in glycoprotein maturation and lysosomal degradation. It is frequently used in drug discovery as a surrogate target to screen for inhibitors like swainsonine, which are investigated for their anti-tumor and immunomodulatory properties (PMID: 1566718). These inhibitors typically act by mimicking the transition state of the mannosyl residue, thereby competitively blocking the enzyme's active site (PMID: 8413645). Consequently, Jack bean alpha-mannosidase plays a vital role in understanding the pharmacology of glycomimetics intended for treating cancer, viral infections, and metabolic disorders.

Other names

Alpha-D-mannoside mannohydrolaseJack bean alpha-mannosidaseCanavalia ensiformis alpha-mannosidaseAlpha-mannosidase 1

Competitive inhibition of the catalytic site by transition-state analogs, preventing the cleavage of terminal alpha-mannosyl residues from glycoproteins (PMID: 8413645).