EC Number   |
Protein Variants |
Reference |
|---|
   3.5.1.26 | C140S |
the substitution is the causative mutation for enzyme deficiency. In addition to preventing the disulfide bond formation between C140 and C156, the C140S substitution also causes destabilization of the unique/longer loop structure in the human sequence and thus prevent dimerization of GA essential for autoproteolytic activation |
753573 |
| 3.5.1.26 | D151N |
mutation completely abolishes autoproteolysis, mutation eradicates the backbone distortion near the scissile peptide bond |
657367 |
| 3.5.1.26 | D200A |
87% of wild-type activity, study of folding, transport and catalytic kinetics of mutant AGA |
654537 |
| 3.5.1.26 | D201A |
93% of wild-type activity, study of folding, transport and catalytic kinetics of mutant AGA |
654537 |
| 3.5.1.26 | D205G |
essential for activation by autocatalytic proteolytic processing |
209048 |
| 3.5.1.26 | D70A |
44% of wild-type activity, study of folding, transport and catalytic kinetics of mutant AGA |
654537 |
| 3.5.1.26 | G172D |
naturally occuring mutation in Finnish population causing aspartylglucosaminuria (AGU) |
755339 |
| 3.5.1.26 | G172D |
site-directed mutagenesis, the mutation causes a local conformational change, which in turn disrupts the requisite autoprocessing step to generate metabolically functional mature hydrolase |
753573 |
| 3.5.1.26 | G172D |
the naturally occuring point mutation results in misprocessing of its precursor and is deficient in hydrolyzing glycoasparagines, the mutant can be stabilized by L-aspartic acid beta-hydroxamate for crystallization against proteolysis by other enzymes |
735290 |
| 3.5.1.26 | G203D |
naturally occuring mutation in Canadian population, causing aspartylglucosaminuria (AGU) |
753573 |
