Function
Glycosylasparaginase or aspartylglucosaminidase (AGA) hydrolyzes a number of β-aspartyl amides including asparagine. AGA contains α and β subunits which derive from a precursor (PAGA) which is cleaved post-translationally. Mammalian AGA substrate is the protein-sugar bond of Asn-GlcNac.
Disease
AGA deficiency is the cause of the human lysosomal disease aspartylglycosaminuria.
Relevance
Structural highlights
3D structures of glycosylasparaginase
Updated on 16-June-2014
AGA α+β subunits
1ayy, 2gaw – EmAGA α+β subunits – Elizabethkingia meningoseptica
1apy – hAGA + Nag + β-mannose - human
1apz – hAGA + Nag + β-mannose + Asp
2gl9 – EmAGA α+β (mutant) subunits + Nag + Asn<br /
AGA precursor
2gac - EmPAGA (mutant)
9gaa, 1p4k – EmPAGA (mutant)
9gac, 9gaf, 1p4v, 3ljq – EmPAGA (mutant) + glycine
References
