| IED ID | IndEnz0002014348 |
| Enzyme Type ID | protease014348 |
| Protein Name |
N 4 - beta-N-acetylglucosaminyl -L-asparaginase EC 3.5.1.26 Aspartylglucosaminidase Glycosylasparaginase N4- N-acetyl-beta-glucosaminyl -L-asparagine amidase Cleaved into: Glycosylasparaginase alpha chain; Glycosylasparaginase beta chain |
| Gene Name | AGA |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MARKSNLPVLLVPFLLCQALVRCSSPLPLVVNTWPFKNATEAAWRALASGGSALDAVESGCAMCEREQCDGSVGFGGSPDELGETTLDAMIMDGTTMDVGAVGDLRRIKNAIGVARKVLEHTTHTLLVGESATTFAQSMGFINEDLSTTASQALHSDWLARNCQPNYWRNVIPDPSKYCGPYKPPGILKQDIPIHKETEDDRGHDTIGMVVIHKTGHIAAGTSTNGIKFKIHGRVGDSPIPGAGAYADDTAGAAAATGNGDILMRFLPSYQAVEYMRRGEDPTIACQKVISRIQKHFPEFFGAVICANVTGSYGAACNKLSTFTQFSFMVYNSEKNQPTEEKVDCI |
| Enzyme Length | 346 |
| Uniprot Accession Number | P20933 |
| Absorption | |
| Active Site | ACT_SITE 206; /note=Nucleophile; /evidence=ECO:0000269|PubMed:8846222 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=H2O + N(4)-(beta-N-acetyl-D-glucosaminyl)-L-asparagine = H(+) + L-aspartate + N-acetyl-beta-D-glucosaminylamine; Xref=Rhea:RHEA:11544, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15947, ChEBI:CHEBI:29991, ChEBI:CHEBI:58080; EC=3.5.1.26; Evidence={ECO:0000269|PubMed:1703489, ECO:0000269|PubMed:1904874, ECO:0000269|PubMed:2401370}; |
| DNA Binding | |
| EC Number | 3.5.1.26 |
| Enzyme Function | FUNCTION: Cleaves the GlcNAc-Asn bond which joins oligosaccharides to the peptide of asparagine-linked glycoproteins. {ECO:0000269|PubMed:1703489, ECO:0000269|PubMed:1904874, ECO:0000269|PubMed:2401370}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (15); Chain (2); Disulfide bond (4); Glycosylation (2); Helix (10); Modified residue (1); Natural variant (15); Region (2); Sequence conflict (3); Signal peptide (1); Turn (5) |
| Keywords | 3D-structure;Autocatalytic cleavage;Direct protein sequencing;Disease variant;Disulfide bond;Glycoprotein;Hydrolase;Lysosome;Protease;Reference proteome;Signal |
| Interact With | O60333-2; P07196; O76024 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Lysosome. |
| Modified Residue | MOD_RES 24; /note=Blocked amino end (Ser) |
| Post Translational Modification | PTM: Cleaved into an alpha and beta chain by autocatalysis; this activates the enzyme. The N-terminal residue of the beta subunit is responsible for the nucleophile hydrolase activity. {ECO:0000269|PubMed:1281977, ECO:0000269|PubMed:1703489, ECO:0000269|PubMed:1904874}.; PTM: N-glycosylated. {ECO:0000269|PubMed:2401370}. |
| Signal Peptide | SIGNAL 1..23; /evidence="ECO:0000269|PubMed:2011603, ECO:0007744|PubMed:25944712" |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 1APY; 1APZ; |
| Mapped Pubmed ID | 14616088; 15174051; 15365992; 16435229; 18992224; 19100247; 20711500; 21854356; 23271757; 27471012; 2775174; 28457719; 29993127; 30901125; 8692836; |
| Motif | |
| Gene Encoded By | |
| Mass | 37,208 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:11544 |
| Cross Reference Brenda | 3.5.1.26; |