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Literature summary extracted from

  • Maita, N.; Tsukimura, T.; Taniguchi, T.; Saito, S.; Ohno, K.; Taniguchi, H.; Sakuraba, H.
    Human alpha-L-iduronidase uses its own N-glycan as a substrate-binding and catalytic module (2013), Proc. Natl. Acad. Sci. USA, 110, 14628-14633.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.2.1.76 structure analysis of enzyme-substrate complex, PDB IDs 3W81 and 3W82 Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.76 additional information deglycosylation of the enzyme with endoglycosidase H, but not peptide-N-glycosidase F, reduces the enzyme's activity Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.2.1.76 lysosome
-
 Homo sapiens 5764
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.1.76 additional information Homo sapiens the enzyme hydrolyses the glycosidic bond between the terminal L-iduronic acid and the second sugar of N-acetylgalactosamine-4-sulfate/N-sulfo-D-glucosamine-6-sulfate, which are the major components of dermatan/heparan sulfate ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.76 Homo sapiens
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.2.1.76 glycoprotein N-glycosylation at N110, N190, N336, N372, N415, and N451 in subunit A, and at N110, N190, N336, N372, N415, and N451 in subunit B, glycan structures, overview. The enzyme uses its own N-glycan as a substrate binding and catalytic module. The mannose residue of the N-glycan attached to N372 constitutes a part of the substrate-binding pocket and interacts directly with a substrate. The kinetics of native and deglycosylated hIDUA suggest that the N-glycan is also involved in catalytic processes. Deglycosylation of the enzyme with endoglycosidase H, but not peptide-N-glycosidase F, reduces the enzyme's activity. Concanavalin A pull-down assay shows that PNGase F-resistant N-glycans are essential for the enzyme activity Homo sapiens

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.2.1.76 commercial preparation recombinant enzyme expressed in CHO cells Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.76 4-methylumbelliferyl-alpha-L-iduronide + H2O
-
 Homo sapiens 4-methylumbelliferol + alpha-L-iduronic acid
-
 ?
3.2.1.76 additional information the enzyme hydrolyses the glycosidic bond between the terminal L-iduronic acid and the second sugar of N-acetylgalactosamine-4-sulfate/N-sulfo-D-glucosamine-6-sulfate, which are the major components of dermatan/heparan sulfate Homo sapiens ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.76 alpha-L-iduronidase
-
 Homo sapiens
3.2.1.76 hIDUA
-
 Homo sapiens

General Information

EC Number General Information Comment Organism
3.2.1.76 evolution the enzyme belongs to glycoside hydrolase family 39, GH39 Homo sapiens
3.2.1.76 malfunction enzyme dysfunction causes accumulation of dermatan/heparan sulfate leading to mucopolysaccharidosis type I. The defect of the enzyme leads to excess storage of dermatan/heparan sulfate and causes a systemic disorder, MPS I, involving progressive mental retardation, gross facial features, an enlarged and deformed skull, a small stature, corneal opacities, hepatosplenomegaly, valvular heart defects, thick skin, joint contractures, and hernias Homo sapiens
3.2.1.76 additional information the enzyme uses its own N-glycan as a substrate binding and catalytic module. The mannose residue of the N-glycan attached to N372 constitutes a part of the substrate-binding pocket and interacts directly with a substrate. The kinetics of native and deglycosylated hIDUA suggest that the N-glycan is also involved in catalytic processes. Concanavalin A pull-down assay shows that PNGase F-resistant N-glycans are essential for the enzyme activity. Enzyme and substrate binding site structures and enzyme-substrate interaction analysis, overview Homo sapiens