| T99K variant of glycosylasparaginase shows a new structural mechanism of the genetic disease aspartylglucosaminuria | The T99K variant of glycosylasparaginase shows a new structural mechanism of the genetic disease aspartylglucosaminuria.
Pande S, Guo HC., Free PMC Article | 04/11/2020 |
| Determination a 1.6 A-resolution structure of the Finnish AGU model and building of an enzyme-substrate complex to provide a structural basis for analyzing the negative effects of the point mutation on KM and kcat of the mature enzyme. | Biochemical and structural insights into an allelic variant causing the lysosomal storage disorder - aspartylglucosaminuria.
Pande S, Bizilj W, Guo HC., Free PMC Article | 06/15/2019 |
| 1.8A resolution crystal structure of mature G172D mutant of a model missense GA corresponding to a Canadian aspartylglucosaminuria allele; studied the effect of its single amino acid change on substrate processing | Crystal structure of a mutant glycosylasparaginase shedding light on aspartylglycosaminuria-causing mechanism as well as on hydrolysis of non-chitobiose substrate.
Pande S, Lakshminarasimhan D, Guo HC., Free PMC Article | 03/17/2018 |
| We show that gene-silenced cells show specifically reduced AGA activity and store globotriaosylceramide. In gene-silenced cells, release of the neurotransmitter acetylcholine is significantly reduced, demonstrating that this model may be used to study specific neuronal functions such as neurotransmitter release in Fabry disease | Development of a model system for neuronal dysfunction in Fabry disease.
Kaneski CR, Brady RO, Hanover JA, Schueler UH., Free PMC Article | 12/9/2017 |
| 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 | Aspartylglucosaminuria: unusual neonatal presentation in Qatari twins with a novel aspartylglucosaminidase gene mutation and 3 new cases in a Turkish family.
Opladen T, Ebinger F, Zschocke J, Sengupta D, Ben-Omran T, Shahbeck N, Moog U, Fischer C, Bürger F, Haas D, Ruef P, Harting I, Al-Rifai H, Hoffmann GF. | 10/18/2014 |
| [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. activity. | Expanding targets for a metabolic therapy of cancer: L-asparaginase.
Covini D, Tardito S, Bussolati O, Chiarelli LR, Pasquetto MV, Digilio R, Valentini G, Scotti C. | 09/15/2012 |
| Increased AGA plasma activity, although a consistent finding in congenital disorders of glycosylation patients, is not specific to this group of disorders. | Plasma lysosomal enzyme activities in congenital disorders of glycosylation, galactosemia and fructosemia.
Michelakakis H, Moraitou M, Mavridou I, Dimitriou E. | 01/21/2010 |
| The amino acid substitutions in aspartylglucosaminidase responsible for aspartylglucosaminuria were classified and divided in three groups. | Structural basis of aspartylglucosaminuria.
Saito S, Ohno K, Sugawara K, Suzuki T, Togawa T, Sakuraba H. | 01/21/2010 |
| Molecular mechanism for the autoproteolytic activation of aspartylglucosaminidase. | Autoproteolytic activation of human aspartylglucosaminidase.
Saarela J, Oinonen C, Jalanko A, Rouvinen J, Peltonen L., Free PMC Article | 01/21/2010 |
| 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. | A novel aspartylglucosaminuria mutation affects translocation of aspartylglucosaminidase.
Saarela J, von Schantz C, Peltonen L, Jalanko A. | 01/21/2010 |
| aspartylglucosaminidase may have a role in development of congenital disorders of glycosylation type I | Elevation of plasma aspartylglucosaminidase is a useful marker for the congenital disorders of glycosylation type I (CDG I).
Jackson M, Clayton P, Grunewald S, Keir G, Mills K, Mills P, Winchester B, Worthington V, Young E. | 01/21/2010 |