Article
An alpha-subunit loop structure is required for GM2 activator protein binding by beta-hexosaminidase A.
Biochemical and biophysical research communications - 19 Nov 2004
Zarghooni Maryam, Bukovac Scott, Tropak Michael, Callahan John, Mahuran Don
Abstract excerpt
The alpha- and/or beta-subunits of human beta-hexosaminidase A (alphabeta) and B (betabeta) are approximately 60% identical. In vivo only beta-hexosaminidase A can utilize GM2 ganglioside as a substrate, but requires the GM2 activator protein to bind GM2 ganglioside and then interact with the enzyme, placing the terminal GalNAc residue in the active site of the alpha-subunit. A model for this interaction suggests...
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