Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Mucopolysaccharidosis type I, unique structure of accumulated heparan sulfate and increased N-sulfotransferase activity in mice lacking α-l-iduronidase.
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Idua-deficient mice accumulate heparan sulfate bearing a terminal iduronate-capped disaccharide at the non-reducing end, where no further degradation can occur without Idua, confirming IDUA's role in heparan sulfate/heparin catabolism.
"representing the terminal iduronic acid residue capping the non-reducing end of the HS chain, where no further degradation can occur in the absence of Idua."
In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine.
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IDUA was among ~900 proteins detected by shotgun proteomics of urinary prostatic-secretion exosomes, supporting its recovery in extracellular vesicles.
"In pooled EPS-urine exosome samples, ~900 proteins were detected."
Human α-L-iduronidase uses its own N-glycan as a substrate-binding and catalytic module.
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Crystal structure and enzymology of human IDUA showing that the N-glycan at Asn372 forms part of the substrate-binding pocket and is required for full L-iduronidase activity.
"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."
Insights into mucopolysaccharidosis I from the structure and action of α-L-iduronidase.
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Crystal structures of human IDUA bound to iduronate analogs define the catalytic mechanism (retaining double displacement; nucleophile Glu299, acid/base Glu182) and confirm exolytic removal of alpha-L-iduronate from heparan and dermatan sulfate.
"IDUA participates in the stepwise degradation of the glycosaminoglycans (GAGs) heparan sulphate and dermatan sulphate, by removing a single α-L-iduronyl residue from the non-reducing ends of these complex polysaccharides."
Immunopurification and characterization of human alpha-L-iduronidase with the use of monoclonal antibodies.
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Immunopurified human alpha-L-iduronidase from liver was active toward disaccharide substrates derived from both heparan sulfate and dermatan sulfate.
"activities towards disaccharide substrates derived from two glycosaminoglycan sources, heparan sulphate and dermatan sulphate."
IDUA cleaves iduronate from HS chain
IDUA hydrolyses the unsulfated alpha-L-iduronosidic link in DS
IDUA hydrolyses Heparan sulfate chain(6)
Defective IDUA does not hydrolyse Heparan sulfate chain(6)
Defective IDUA does not hydrolyse Heparan sulfate chain(1)
Defective IDUA does not hydrolyse the unsulfated alpha-L-iduronosidic link in DS
UniProtKB entry P35475 (IDUA_HUMAN)