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Literature summary for 3.2.1.76 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
Search for more literature for 3.2.1.76

Crystallization (Commentary)

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

Inhibitors

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

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

Natural Substrates/ Products (Substrates)

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

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Posttranslational Modification

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

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

Substrates and Products (Substrate)

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

Synonyms Comment Organism
alpha-L-iduronidase
-
 Homo sapiens
hIDUA
-
 Homo sapiens

General Information

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