Crystallization (Comment) | Organism |
---|---|
structure analysis of enzyme-substrate complex, PDB IDs 3W81 and 3W82 | Homo sapiens |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
additional information | deglycosylation of the enzyme with endoglycosidase H, but not peptide-N-glycosidase F, reduces the enzyme's activity | Homo sapiens |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
lysosome | - |
Homo sapiens | 5764 | - |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
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 | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
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 | Comment | Organism | Textmining |
---|---|---|---|
commercial preparation | recombinant enzyme expressed in CHO cells | Homo sapiens | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
4-methylumbelliferyl-alpha-L-iduronide + H2O | - |
Homo sapiens | 4-methylumbelliferol + alpha-L-iduronic acid | - |
? | |
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 | Comment | Organism |
---|---|---|
alpha-L-iduronidase | - |
Homo sapiens |
hIDUA | - |
Homo sapiens |
General Information | Comment | Organism |
---|---|---|
evolution | the enzyme belongs to glycoside hydrolase family 39, GH39 | Homo sapiens |
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 |
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 |