There are numerous mutations that lead to hexosaminidase deficiency including gene deletions, nonsense mutations, and missense mutations.
 Tay–Sachs disease occurs when hexosaminidase A loses its ability to function.
People with Tay–Sachs disease are unable to remove the GalNAc residue from the GM2 ganglioside, and as a result, they end up storing 100 to 1000 times more  GM2 gangliosides in the brain than the normal person.
 Over 100 different mutations have been discovered just in infantile cases of Tay–Sachs disease alone.

The most common mutation, which occurs in over 80 percent of Tay–Sachs patients, results from a four base pair addition (TATC) in exon 11 of the Hex A gene.
 This insertion leads to an early stop codon, which causes the Hex A deficiency.

Children born with Tay–Sachs usually die between two and four years of age from aspiration and pneumonia.
 Tay–Sachs causes cerebral degeneration and blindness.
 Patients also experience flaccid extremities and seizures.
 At this point in time, there has been no cure or effective treatment of Tay–Sachs disease.

NAG-thiazoline, NGT, acts as mechanism based inhibitor of hexosaminidase A.  In patients with Tay–Sachs disease (misfolded hexosaminidase A), NGT acts as a molecular chaperone by binding in the active site of hexosaminidase A which helps create a properly folded hexosaminidase A. The stable dimer conformation of hexosaminidase A has the ability to leave the endoplasmic reticulum and is directed to the lysosome where it can perform the degradation of GM2 gangliosides.
The two subunits of hexosaminidase A are shown below:
There are numerous mutations that lead to hexosaminidase deficiency including gene deletions, nonsense mutations, and missense mutations.  Tay–Sachs disease occurs when hexosaminidase A loses its ability to function. People with Tay–Sachs disease are unable to remove the GalNAc residue from the GM2 ganglioside, and as a result, they end up storing 100 to 1000 times more  GM2 gangliosides in the brain than the normal person.  Over 100 different mutations have been discovered just in infantile cases of Tay–Sachs disease alone.
The most common mutation, which occurs in over 80 percent of Tay–Sachs patients, results from a four base pair addition (TATC) in exon 11 of the Hex A gene.  This insertion leads to an early stop codon, which causes the Hex A deficiency.
Children born with Tay–Sachs usually die between two and four years of age from aspiration and pneumonia.  Tay–Sachs causes cerebral degeneration and blindness.  Patients also experience flaccid extremities and seizures.  At this point in time, there has been no cure or effective treatment of Tay–Sachs disease.
NAG-thiazoline, NGT, acts as mechanism based inhibitor of hexosaminidase A.  In patients with Tay–Sachs disease (misfolded hexosaminidase A), NGT acts as a molecular chaperone by binding in the active site of hexosaminidase A which helps create a properly folded hexosaminidase A. The stable dimer conformation of hexosaminidase A has the ability to leave the endoplasmic reticulum and is directed to the lysosome where it can perform the degradation of GM2 gangliosides. The two subunits of hexosaminidase A are shown below:
Hexosaminidase