AGA
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Official Full Name
aspartylglucosaminidase
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Overview
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. -
Synonyms
AGA; aspartylglucosaminidase; N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase; ASRG; glycosylasparaginase; AGU; Aspartylglucosylamine deaspartylase; Aspartylglycosaminuria; ASPG_HUMAN; GA; Glycosylasparaginase beta chain; N4 (N acetyl beta glucosaminyl) L asparagine amidase; N4-(N-acetyl-beta-glucosaminyl)-L-asparagine amidase;
- Recombinant Proteins
- Cell & Tissue Lysates
- Protein Pre-coupled Magnetic Beads
- Chicken
- Cynomolgus Monkey
- Human
- Mouse
- Rat
- Zebrafish
- E.coli
- HEK293
- Human Cell
- In Vitro Cell Free System
- Insect Cell
- Mammalian Cell
- Wheat Germ
- GST
- His
- His (Fc)
- Avi
- His|SUMO
- SUMO
- N/A
- Involved Pathway
- Protein Function
- Interacting Protein
- AGA Related Articles
AGA involved in several pathways and played different roles in them. We selected most pathways AGA participated on our site, such as Integrated Pancreatic Cancer Pathway, L-asparagine degradation III (mammalian), Lysosome, which may be useful for your reference. Also, other proteins which involved in the same pathway with AGA were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
| Pathway Name | Pathway Related Protein |
|---|---|
| Integrated Pancreatic Cancer Pathway | FKBP1B;TOP1;BRF1;RB1CC1;CST3;CD82;FST;AGA;NOXA1 |
| L-asparagine degradation III (mammalian) | |
| Lysosome | CTSA;CTSZ;ATP6V1H;PSAP;NEU1;SCARB2;AP1G2;LAMP2;ACP5A |
| Other glycan degradation | MAN2B1;HEXB;GLB1;HEXA;ENGASE;AGA;FUCA1;NEU3.2;NEU3.3 |
| asparagine degradation |
AGA has several biochemical functions, for example, N4-(beta-N-acetylglucosaminyl)-L-asparaginase activity, peptidase activity, protein self-association. Some of the functions are cooperated with other proteins, some of the functions could acted by AGA itself. We selected most functions AGA had, and list some proteins which have the same functions with AGA. You can find most of the proteins on our site.
| Function | Related Protein |
|---|---|
| N4-(beta-N-acetylglucosaminyl)-L-asparaginase activity | |
| peptidase activity | UFSP2;TMPRSS7;HM13;THSD4;GZMF;MCPT9;USPL1;HE2;CTSSB.1 |
| protein self-association | CTSB;SVIP;EPB49;TRIM32;PCSK9;CCDC88C;CCL5;LDB1;DYRK1A |
AGA has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with AGA here. Most of them are supplied by our site. Hope this information will be useful for your research of AGA.
q81kn9_bacan; ALB
- Q&As
- Reviews
Q&As (20)
Ask a questionThe AGA protein is found in lysosomes, which are cell organelles involved in breaking down cellular waste.
Researchers used the PhosphoSitePlus tool and molecular dynamics simulations to analyze AGA protein phosphorylation.
Research investigates how AGA protein’s specificity for aspartylglucosamine residues influences substrate interactions.
AGA protein’s role contributes to maintaining lysosomal homeostasis and overall cellular health.
Deficiency of the AGA protein leads to Aspartylglucosaminuria, a rare genetic disorder characterized by the buildup of glycoproteins in the body.
The C163S mutant AGA protein exhibited increased hydrogen bonds and greater compactness compared to the wild type.
Yes, AGA protein’s activity might play a role in maintaining optimal lysosomal pH for enzymatic activity.
AGA protein’s role may include participating in lysosomal enzyme trafficking to enhance degradation processes.
Phosphorylated AGA forms (Y178-p, T215-p, T324-p) showed increased intramolecular hydrogen bonds and greater compactness.
Yes, AGA protein’s function impacts lysosomal enzyme activity and contributes to efficient degradation.
The AGA protein catalyzes the hydrolysis of N-linked glycoproteins, breaking them down into smaller components.
The AGA protein plays a role in the metabolism of glycoproteins.
Yes, AGA protein’s activity can be influenced by cellular conditions and the presence of its substrates.
Research aims to uncover how AGA protein’s function mitigates cellular responses to glycoprotein accumulation.
Yes, AGA protein’s role directly influences glycoprotein metabolism and turnover within cells.
Yes, AGA protein’s involvement can extend to lysosomal exocytosis and the release of lysosomal contents.
Research investigates AGA protein’s role in lysosomal storage disorders, aiding in understanding disease mechanisms.
In AGU, insufficient AGA activity leads to the buildup of glycoproteins, causing chronic neurodegeneration.
AGA protein’s function could impact cellular responses to lysosomal stressors and maintain lysosomal function.
Yes, AGA protein’s malfunction can lead to lysosomal storage disorders, disrupting glycoprotein degradation.
Customer Reviews (5)
Write a reviewThe product’s adaptability to various buffers contributed to its stable and consistent performance.
The consistent performance of the product simplified data interpretation.
Our research was fortified by the product’s consistent behavior, fostering robust results.
The high-quality Protein AGA enabled precise quantification of target proteins.
Our assays showed a significant increase in enzyme activity using Ag5.
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