The enzyme, found in plants and animals, participates in the processing of N-glycans in the Golgi apparatus. It removes two mannosyl residues, one linked by alpha1,3 linkage, and the other linked by alpha1,6 linkage, both of which are removed by the same catalytic site. The enzyme is sensitive to swainsonine.
mannosidase ii, jack bean alpha-mannosidase, man2a1, alpha-mannosidase iix, dgmii, manii, alpha-mii, drosophila gmii, alpha-d-mannosidase ii, afams1, more
The enzyme, found in plants and animals, participates in the processing of N-glycans in the Golgi apparatus. It removes two mannosyl residues, one linked by alpha1,3 linkage, and the other linked by alpha1,6 linkage, both of which are removed by the same catalytic site. The enzyme is sensitive to swainsonine.
Man II catalyzes the final hydrolytic step in the N-glycan maturation pathway acting as the committed step in the conversion of high mannose to complex type structures
Man II catalyzes the final hydrolytic step in the N-glycan maturation pathway acting as the committed step in the conversion of high mannose to complex type structures
MII and alpha-mannosidase IIx function in N-glycan processing in a similar manner. Alpha-mannosidase IIx shows no reactivity to high-mannose-type carbohydrates
Man II catalyzes the final hydrolytic step in the N-glycan maturation pathway acting as the committed step in the conversion of high mannose to complex type structures
Man II catalyzes the final hydrolytic step in the N-glycan maturation pathway acting as the committed step in the conversion of high mannose to complex type structures
alpha-mannosidase II deficiency has a minimal effect on N-glycan maturation in most cell types due to the compensation by alpha-mannosidase IIx, ablation of alpha-MII impairs the maturation of N-glycans in intestinal epithelial cells. alpha-mannosidase II (DELTA intestinal epithelial cell) mice are less susceptible to dextran sulfate sodium-induced colitis compared with control littermates. Neutrophil infiltration in the colonic mucosa is attenuated in alpha-mannosidase II (DELTA intestinal epithelial cell) mice. Gene expression levels of neutrophil-attracting chemokines are downregulated in the colonic tissue
the enzyme plays a crucial, but not exclusive, role in the maturation of N-glycans. Intestinal epithelial cell alpha-mannosidase II promotes intestinal inflammation by facilitating chemokine expression
MII/alpha-mannosidase IIx double knockout mice, completely lack complex-type N-glycans, some double-nulls die between embryonic days 15.5 and 18.5, but most survive until shortly after birth and die of respiratory failure. Alpha-mannosidase IIx-null mice are mainly complex-type and also contain high-mannose-type but not significant levels of hybrid-type N-glycans. In contrast, MII-null embryos show high levels of hybrid-type N-glycans and reduced levels of complex-type N-glycans
cDNA fragments encoding full-length enzymes subcloned into the pcDNA3.1 mammalian expression vector. cDNA fragments encoding soluble forms of enzymes subcloned into pcDNA-HSH. Full-length alpha-mannosidase IIx expressed in MII/alpha-mannosidase IIx double-null fibroblasts. Soluble recombinant alpha-mannosidase IIx expressed in COS cells
alpha-mannosidase IIx is an isozyme of MII. Either MII or alpha-mannosidase IIx can biochemically compensate for the deficiency of the other in vivo, and either of two is required for late embryonic and early postnatal development
Isolation, characterization, and expression of cDNAs encoding murine alpha-mannosidase II, a Golgi enzyme that controls conversion of high mannose to complex N-glycans
J. Cell Biol.
115
1521-1534
1991
Homo sapiens, Mus musculus (P27046), Mus musculus, Rattus norvegicus