Mannosidase alpha class 2B member 2 (MAN2B2)

Mannosidase alpha class 2B member 2 (MAN2B2) is a lysosomal enzyme responsible for the cleavage of alpha-1,6-mannose residues during the degradation of N-linked glycoproteins. MAN2B2 acts as a core-specific alpha-1,6-mannosidase and functions alongside other lysosomal mannosidases to break down glycoproteins into monosaccharides, which are salvaged for further use in glycan biosynthesis. Mutations in MAN2B2 can cause abnormal glycosylation, leading to congenital disorders of glycosylation (CDG) presenting as immune deficiency, developmental delay, and neurodevelopmental abnormalities. Inhibition of this enzyme is possible with compounds such as swainsonine and mannostatin A. MAN2B2 is related to metabolic pathways in glycosaminoglycan metabolism, and aberrations in its activity represent a novel cause of CDG and lysosomal dysfunction in humans[1][2][3].

Other names

Epididymis-specific alpha-mannosidaseMAN2B2KIAA0935EpMANAlpha-1,6-mannosidaseCore-specific lysosomal alpha-1,6-mannosidaseCDG1EEEpididymis secretory sperm binding protein

Inhibition of lysosomal alpha-mannosidase activity, specifically cleavage of alpha-1,6-mannose residues of N-linked glycans[2]