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AGA

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
1APY, 1APZ

Identifiers

Aliases

AGA, Aga, AW060726, AGU, ASRG, GA, aspartylglucosaminidase

External IDs

OMIM: 613228 MGI: 104873 HomoloGene: 13 GeneCards: AGA

Gene location (Human)

Chr.	Chromosome 4 (human)^[1]

Band	4q34.3	Start	177,430,774 bp^[1]
Band	4q34.3	End	177,442,437 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 8 (mouse)^[2]

Band	8\|8 B1.3	Start	53,964,762 bp^[2]
Band	8\|8 B1.3	End	53,976,456 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

corpus epididymis

stromal cell of endometrium

oral cavity

islet of Langerhans

parotid gland

kidney tubule

hair follicle

bone marrow cells

human penis

thymus

Top expressed in

calvaria

ascending aorta

otolith organ

utricle

pituitary gland

aortic valve

islet of Langerhans

supraoptic nucleus

seminal vesicula

interventricular septum

More reference expression data

BioGPS


More reference expression data

Gene ontology
Molecular function	protein self-association peptidase activity hydrolase activity N4-(beta-N-acetylglucosaminyl)-L-asparaginase activity
Cellular component	lysosome endoplasmic reticulum extracellular region extracellular space azurophil granule lumen cytoplasm
Biological process	protein maturation protein deglycosylation proteolysis neutrophil degranulation
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


175


11593

Ensembl


ENSG00000038002


ENSMUSG00000031521

UniProt


P20933


Q64191

RefSeq (mRNA)


NM_000027 NM_001171988


NM_001005847 NM_001205054

RefSeq (protein)


NP_000018 NP_001165459


NP_001005847 NP_001191983

Location (UCSC)

Chr 4: 177.43 – 177.44 Mb

Chr 8: 53.96 – 53.98 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase is an enzyme that in humans is encoded by the AGA gene.^[5]

Aspartylglucosaminidase is an amidohydrolase enzyme 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.^[5]

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Transcription

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000038002 - Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000031521 - Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ ^a ^b "Entrez Gene: AGA aspartylglucosaminidase".

External links

Human AGA genome location and AGA gene details page in the UCSC Genome Browser.

Ikonen E, Peltonen L (1993). "Mutations causing aspartylglucosaminuria (AGU): a lysosomal accumulation disease". Hum. Mutat. 1 (5): 361–5. doi:10.1002/humu.1380010503. PMID 1301945. S2CID 24301019.
Mononen I, Fisher KJ, Kaartinen V, Aronson NN (1993). "Aspartylglycosaminuria: protein chemistry and molecular biology of the most common lysosomal storage disorder of glycoprotein degradation". FASEB J. 7 (13): 1247–56. doi:10.1096/fasebj.7.13.8405810. PMID 8405810. S2CID 21771613.
Enomaa N, Heiskanen T, Halila R, et al. (1992). "Human aspartylglucosaminidase. A biochemical and immunocytochemical characterization of the enzyme in normal and aspartylglucosaminuria fibroblasts". Biochem. J. 286 ( Pt 2) (Pt 2): 613–8. doi:10.1042/bj2860613. PMC 1132942. PMID 1530592.
Ikonen E, Baumann M, Grön K, et al. (1991). "Aspartylglucosaminuria: cDNA encoding human aspartylglucosaminidase and the missense mutation causing the disease". EMBO J. 10 (1): 51–8. doi:10.1002/j.1460-2075.1991.tb07920.x. PMC 452610. PMID 1703489.
Morris C, Heisterkamp N, Groffen J, et al. (1992). "Chromosomal localization of the human glycoasparaginase gene to 4q32-q33". Hum. Genet. 88 (3): 295–7. doi:10.1007/BF00197262. PMID 1733831. S2CID 8805853.
Ikonen E, Enomaa N, Ulmanen I, Peltonen L (1992). "In vitro mutagenesis helps to unravel the biological consequences of aspartylglucosaminuria mutation". Genomics. 11 (1): 206–11. doi:10.1016/0888-7543(91)90120-4. PMID 1765378.
Park H, Fisher KJ, Aronson NN (1991). "Genomic structure of human lysosomal glycosylasparaginase". FEBS Lett. 288 (1–2): 168–72. doi:10.1016/0014-5793(91)81027-6. PMID 1840528. S2CID 26680929.
Mononen T, Mononen I, Matilainen R, Airaksinen E (1991). "High prevalence of aspartylglycosaminuria among school-age children in eastern Finland". Hum. Genet. 87 (3): 266–8. doi:10.1007/BF00200902. PMID 1864600. S2CID 8240322.
Fisher KJ, Aronson NN (1991). "Characterization of the mutation responsible for aspartylglucosaminuria in three Finnish patients. Amino acid substitution Cys163----Ser abolishes the activity of lysosomal glycosylasparaginase and its conversion into subunits". J. Biol. Chem. 266 (18): 12105–13. doi:10.1016/S0021-9258(18)99071-X. PMID 1904874.
Mononen I, Heisterkamp N, Kaartinen V, et al. (1991). "Aspartylglycosaminuria in the Finnish population: identification of two point mutations in the heavy chain of glycoasparaginase". Proc. Natl. Acad. Sci. U.S.A. 88 (7): 2941–5. Bibcode:1991PNAS...88.2941M. doi:10.1073/pnas.88.7.2941. PMC 51356. PMID 2011603.
Halila R, Baumann M, Ikonen E, et al. (1991). "Human leucocyte aspartylglucosaminidase. Evidence for two different subunits in a more complex native structure". Biochem. J. 276 ( Pt 1) (Pt 1): 251–6. doi:10.1042/bj2760251. PMC 1151172. PMID 2039475.
Fisher KJ, Tollersrud OK, Aronson NN (1991). "Cloning and sequence analysis of a cDNA for human glycosylasparaginase. A single gene encodes the subunits of this lysosomal amidase". FEBS Lett. 276 (1–2): 232. doi:10.1016/0014-5793(90)80551-S. PMID 2265705. S2CID 221417722.
Fisher KJ, Tollersrud OK, Aronson NN (1990). "Cloning and sequence analysis of a cDNA for human glycosylasparaginase. A single gene encodes the subunits of this lysosomal amidase". FEBS Lett. 269 (2): 440–4. doi:10.1016/0014-5793(90)81211-6. PMID 2401370. S2CID 8210082.
Tollersrud OK, Aronson NN (1989). "Purification and characterization of rat liver glycosylasparaginase". Biochem. J. 260 (1): 101–8. doi:10.1042/bj2600101. PMC 1138631. PMID 2775174.
Hreidarsson S, Thomas GH, Valle DL, et al. (1983). "Aspartylglucosaminuria in the United States". Clin. Genet. 23 (6): 427–35. doi:10.1111/j.1399-0004.1983.tb01977.x. PMID 6883788. S2CID 46703938.
Enomaa NE, Lukinmaa PL, Ikonen EM, et al. (1993). "Expression of aspartylglucosaminidase in human tissues from normal individuals and aspartylglucosaminuria patients". J. Histochem. Cytochem. 41 (7): 981–9. doi:10.1177/41.7.7685790. PMID 7685790.
McCormack AL, Mononen I, Kaartinen V, Yates JR (1995). "Localization of the disulfide bond involved in post-translational processing of glycosylasparaginase and disrupted by a mutation in the Finnish-type aspartylglycosaminuria". J. Biol. Chem. 270 (7): 3212–5. doi:10.1074/jbc.270.7.3212. PMID 7852406.
Tollersrud OK, Heiskanen T, Peltonen L (1994). "Human leucocyte glycosylasparaginase is an alpha/beta-heterodimer of 19 kDa alpha-subunit and 17 and 18 kDa beta-subunit". Biochem. J. 300 ( Pt 2) (Pt 2): 541–4. doi:10.1042/bj3000541. PMC 1138195. PMID 8002961.

v t e PDB gallery
1apy: HUMAN ASPARTYLGLUCOSAMINIDASE 1apz: HUMAN ASPARTYLGLUCOSAMINIDASE COMPLEX WITH REACTION PRODUCT

External links

Aspartylglucosylaminase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

v t e Hydrolases: carbon-nitrogen non-peptide (EC 3.5)
3.5.1: Linear amides / Amidohydrolases	Asparaginase Glutaminase Urease Biotinidase Aminoacylase ACY1 Aspartoacylase(ACY2) ACY3 Ceramidase Aspartylglucosaminidase Fatty acid amide hydrolase Histone deacetylase Sirtuin
3.5.2: Cyclic amides/ Amidohydrolases	Barbiturase Beta-lactamase Dihydroorotase
3.5.3: Linear amidines/ Ureohydrolases	Arginase Agmatinase Protein-arginine deiminase
3.5.4: Cyclic amidines/ Aminohydrolases	Guanine deaminase Adenosine deaminase AMP deaminase Inosine monophosphate synthase DCMP deaminase GTP cyclohydrolase I Cytidine deaminase AICDA Activation-induced cytidine deaminase
3.5.5: Nitriles/ Aminohydrolases	Nitrilase
3.5.99: Other	Riboflavinase Thiaminase II

v t e Metabolism: carbohydrate metabolism · glycoprotein enzymes
Anabolism	Dolichol kinase GCS1 Oligosaccharyltransferase
Catabolism	Neuraminidase Beta-galactosidase Hexosaminidase mannosidase alpha-Mannosidase beta-mannosidase Aspartylglucosaminidase Fucosidase NAGA
Transport	SLC17A5
M6P tagging	N-acetylglucosamine-1-phosphate transferase

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This page was last edited on 11 March 2024, at 19:56

Aspartylglucosaminidase

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Transcription

References

External links

Further reading

External links