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Human α-L-iduronidase Uses Its Own N-glycan as a Substrate-Binding and Catalytic Module

Human α-L-iduronidase Uses Its Own N-glycan as a Substrate-Binding and Catalytic Module

Nobuo Maita, Takahiro Tsukimura, Takako Taniguchi, Seiji Saito, Kazuki Ohno, Hisaaki Taniguchi, Hitoshi Sakuraba

Proc Natl Acad Sci U S A. 2013 Sep 3;110(36):14628-33.

PMID: 23959878

Abstract:

N-glycosylation is a major posttranslational modification that endows proteins with various functions. 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. 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. 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. A deglycosylation study showed that enzyme activity was highly correlated with the N-glycan attached to N372. The kinetics of native and deglycosylated hIDUA suggested that the N-glycan is also involved in catalytic processes. Our study demonstrates a previously unrecognized function of N-glycans.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
IAR42415183	α-L-Iduronidase human			Price

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