PMID: 8846222

 

    Legend: Gene, Sites

Title : Three-dimensional structure of human lysosomal aspartylglucosaminidase

Abstract :

1. The high resolution crystal structure of human lysosomal aspartylglucosaminidase ( AGA ) has been determined
2. This lysosomal enzyme is synthesized as a single polypeptide precursor , which is immediately post-translationally cleaved into alpha- and beta- subunits
3. Two alpha- and beta- chains are found to pack together forming the final heterotetrameric structure
4. The catalytically essential residue , the N-terminal threonine of the beta- chain is situated in the deep pocket of the funnel-shaped active site
5. On the basis of the structure of the enzyme-product complex we present a catalytic mechanism for this lysosomal enzyme with an exceptionally high pH optimum
6. The three-dimensional structure also allows the prediction of the structural consequences of human mutations resulting in aspartylglucosaminuria (AGU), a lysosomal storage disease

Output (sent_index, trigger, protein, sugar, site):

Output(Part-Of) (sent_index, protein, site):

• 4. chain, residue
• 4. chain, threonine

*Output_Site_Fusion* (sent_index, protein, sugar, site):

 

Protein	NCBI ID	SENTENCE INDEX