PMID: 23959878

 

    Legend: Gene, Sites

Title : Human α -L-iduronidase uses its own N-glycan as a substrate-binding and catalytic module

Abstract :

1. N-glycosylation is a major posttranslational modification that endows proteins with various functions
2. It is established that N-glycans are essential for the correct folding and stability of some enzymes; however, the actual effects of N-glycans on their activities are poorly understood
3. Here, we show that human α -l-iduronidase ( hIDUA ), of which a dysfunction causes accumulation of dermatan/heparan sulfate leading to mucopolysaccharidosis type I, uses its own N-glycan as a substrate binding and catalytic module
4. Structural analysis revealed that the mannose residue of the N-glycan attached to N372 constituted a part of the substrate-binding pocket and interacted directly with a substrate
5. A deglycosylation study showed that enzyme activity was highly correlated with the N-glycan attached to N372
6. The kinetics of native and deglycosylated hIDUA suggested that the N-glycan is also involved in catalytic processes
7. Our study demonstrates a previously unrecognized function of N-glycans

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

• 4. attached, , -, the N-glycan, N372
• 5. attached, , -, the N-glycan, N372
• 6. deglycosylated, , hIDUA, -, -

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

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

• 4. -L-iduronidase, the N-glycan, N372
• 5. -L-iduronidase, the N-glycan, N372

 

Protein	NCBI ID	SENTENCE INDEX
-L-iduronidase	3425	0
hIDUA	3425	3,6
-l-iduronidase	3425	3