EC Number   |
General Information |
Reference |
|---|
    3.2.1.24 | malfunction |
alpha-Man RNAi fruits are approximately two times firmer compared with the control and fruit deterioration is delayed by approximately 7 d. It is shown that silencing of alpha-Man enhances fruit shelf life due to the reduced degradation of N-glycoproteins which result in delayed softening |
715769 |
| 3.2.1.24 | malfunction |
alpha-mannosidase deficiency causes the rare lysosomal storage disease alpha-mannosidosis leading to intellectual disabilities, facial characteristics and hearing impairment |
730144 |
| 3.2.1.24 | malfunction |
enzyme deficiency leads to alpha-mannosidosis |
751574 |
| 3.2.1.24 | physiological function |
mutant PBL2025, that misses 50 genes (SSO3004-3050), including genes coding for a multitude of enzymes possibly involved in sugar degradation or metabolism, is complemented with one of the missing proteins, the alpha-mannosidase (SSO3006). The alpha-mannosidase complemented strain resembles the Sulfolobus solfataricus P2 behavior with respect to attachment of cells to glass and growth of cells in static biofilms. During expression of the alpha-mannosidase, glucose and mannose-containing extracellular polymeric substance levels changes in the recombinant strain during surface attachment and biofilm formation. alpha-Mannosidase might be involved in the modulation of the extracellular polymeric substance composition and/or in the de-mannosylation of the glycan tree, which is attached to extracellular glycosylated proteins in Sulfolobus solfataricus |
-, 724934 |
| 3.2.1.24 | physiological function |
the acid enzyme form alpha-mannosidase I plays a role in plasma membrane remodeling associated with sperm maturation. The neutral enzyme form alpha-mannosidase II acts as a receptor in the recognition and binding of the complementary carbohydrate moieties present on the zona pellucida |
730990 |
| 3.2.1.24 | physiological function |
the enzyme could be putatively involved in the turnover and/or the maturation of glycoprotein |
-, 714369 |
| 3.2.1.24 | physiological function |
the enzyme is perhaps functioning in the subsequent degradation of extracellular host glycans following their initial digestion by secreted glycosidases |
710392 |
