3.1.6.13: iduronate-2-sulfatase

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For detailed information about iduronate-2-sulfatase, go to the full flat file.

Reaction

Synonyms

2-sulfo-L-iduronate 2-sulfatase, chondroitinsulfatase, elaprase, Hunter corrective factor, I2S, IDS, IDS-Like, IDS-like enzyme, iduronate 2-sulfatase, iduronate 2-sulfate sulfatase-like, iduronate 2-sulfate-like enzyme, iduronate sulfatase, iduronate sulfate sulfatase, iduronate-2-sulfatase, iduronate-2-sulfate sulfatase, iduronate-2-sulphatase, iduronide-2-sulfate sulfatase, idurono-2-sulfatase, idursulfase, L-iduronate 2-sulfate sulfatase, L-idurono sulfate sulfatase, sulfatase, L-idurono-, sulfo-L-iduronate sulfatase, sulfoiduronate sulfohydrolase

ECTree

     3 Hydrolases

         3.1 Acting on ester bonds

             3.1.6 Sulfuric-ester hydrolases

                3.1.6.13 iduronate-2-sulfatase

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Results	in table
1	Activating Compound
91	AA Sequence
32	Application
1	CAS Registry Number
22	Cloned(Commentary)
2	Crystallization (Commentary)
1431	Disease/ Diagnostics
8	Expression
15	General Information
3	General Stability
37	Inhibitors
17	KM Value [mM]
20	Localization
2	Metals/Ions
25	Molecular Weight [Da]
47	Natural Substrates/ Products (Substrates)
52	Organism
3	Pathway
2	PDB ID
9	pH Optimum
3	pH Stability
1	pI Value
8	Posttranslational Modification
46	Protein Variants
10	Purification (Commentary)
1	Reaction
1	Reaction Type
52	Reference
68	Source Tissue
10	Specific Activity [micromol/min/mg]
4	Storage Stability
83	Substrates and Products (Substrate)
10	Subunits
51	Synonyms
1	Systematic Name
2	Temperature Optimum [°C]
6	Temperature Stability [°C]

Crystallization

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Crystallization on EC 3.1.6.13 - iduronate-2-sulfatase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

structural models of the wild type and mutant IDS proteins resulting from 131 missense mutations identified in patients with mucopolysaccharidosis MPS II. The amino acid substitutions causing MPS II are widely spread over the enzyme molecule and the structural changes of the enzyme protein are generally larger in the severe group than in the attenuated one. The structural changes influence the disease progression

Homo sapiens

P22304

751950

structure with a covalently bound sulfate ion in the active site, to 2.3 A resolution

Homo sapiens

P22304

751660