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Literature summary for 3.5.1.26 extracted from

  • Saarela, J.; von Schantz, C.; Peltonen, L.; Jalanko, A.
    A novel aspartylglucosaminuria mutation affects translocation of aspartylglucosaminidase (2004), Hum. Mutat., 24, 350-351.
    View publication on PubMed
Search for more literature for 3.5.1.26

Cloned(Commentary)

Cloned (Comment) Organism
DNA sequence determination and analysis, overexpression of mutant L15R in BHK and COS-1 cells, low expression level in endoplasmic reticulum, the recombinant active enzyme does not reach the lysosomes Homo sapiens

Protein Variants

Protein Variants Comment Organism
L15R naturally occuring L15R, mutating the signal sequence, causes aspartylglucosaminuria and affects translocation of aspartylglucosaminidase Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
lysosome
-
 Homo sapiens 5764
-
additional information L15R causes aspartylglucosaminuria and affects translocation of aspartylglucosaminidase Homo sapiens
-
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Homo sapiens aspartylglucosaminuria, a lysosomal storage disease caused by mutation L15R, is enriched in the Finnish population ?
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens P20933 AGA; gene AGA
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification the enzyme contains a subcellular targeting signal sequence Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information aspartylglucosaminuria, a lysosomal storage disease caused by mutation L15R, is enriched in the Finnish population Homo sapiens ?
-
 ?

Synonyms

Synonyms Comment Organism
AGA
-
 Homo sapiens
aspartylglucosaminidase
-
 Homo sapiens