This enzyme's substrate is extracted from membranes by the activator protein SAP-3.
The beta-subunit of this enzyme has aspartate-452 and leucine-453 residues rather than the corresponding asparagine and arginine residues in its alpha subunit. Those changes cause this enzyme's beta subunit not to show any activity despite having active sites, as the changes make the beta subunit inflexible. Bacterial analogs of this enzyme suggest that it proceeds via the formation of an oxazolinium intermediate, and its R-247-W and R-249-W mutations in humans are its two known pseudo-deficient forms. This enzyme's substrate is extracted from membranes by the activator protein SAP-3. This enzyme's main activity is to cleave N-acetyl-galactosamine from certain oligo-saccharides. The zero-variant of this enzyme, in which the beta-subunit is affected, results in Sandhoff's disease. It is localized to the lysosome, and mutations that make it unable to hydrolyze GM2 ganglioside lead to a buildup of fat in nerve cells. For 10 points, name this enzyme that is faulty in patients suffering from Tay-Sachs disease.
The beta-subunit of this enzyme has aspartate-452 and leucine-453 residues rather than the corresponding asparagine and arginine residues in its alpha subunit.
hexosaminidase [accept beta-hexosaminidase A or beta-N-acetyl-hexosaminidase or N- acetyl-beta-glucosaminidase or HEXA or TSD]