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Aspartylglucosaminidase is involved in the catabolism of N-linked oligosaccharides of glycoproteins.
study reports 2 novel aspartylglucosaminidase gene mutations, one in Qatari twins with an early, perinatal presentation not previously described for aspartylglucosaminuria and the other in 3 Turkish children with newly diagnosed aspartylglucosaminuria and a more classical disease course
[review] Natural killer (NK) cell tumors, subtypes of myeloid leukemias and T-cell lymphomas respond to ASNase; ovarian carcinomas and other solid tumors have been proposed as additional targets for ASNase, with a potential role for glutaminase (show GLS ELISA Kits). activity.
Molecular mechanism for the autoproteolytic activation of aspartylglucosaminidase.
A new point mutation, c.44T>G, found in a Finnish compound heterozygote causes a L15R AA substitution in the signal sequence of the AGA enzyme, affecting AGA translocation by altering a critical hydrophobic core structure in the signal sequence.
aspartylglucosaminidase may have a role in development of congenital disorders of glycosylation type I
The amino acid substitutions in aspartylglucosaminidase responsible for aspartylglucosaminuria were classified and divided in three groups.
Increased AGA plasma activity, although a consistent finding in congenital disorders of glycosylation patients, is not specific to this group of disorders.
Aspartylglucosaminidase is involved in the catabolism of N-linked oligosaccharides of glycoproteins. It cleaves asparagine from N-acetylglucosamines as one of the final steps in the lysosomal breakdown of glycoproteins. The lysosomal storage disease aspartylglycosaminuria is caused by a deficiency in the AGA enzyme. Alternatively spliced transcript variants have been identified.
, N4-(N-acetyl-beta-glucosaminyl)-L-asparagine amidase
, aspartylglucosylamine deaspartylase