Arylsulfatase B Protein

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Arylsulfatase B Protein

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Arylsulfatase B Protein

Introduction

Arylsulfatase B Protein is an important component in the neurobiology of neurodegenerative diseases. This page provides detailed information about its structure, function, and role in disease processes.

<div class="infobox infobox-protein">
<table>
<tr><th colspan="2" style="background:#f0f0f0;">Arylsulfatase B (ARSB)</th></tr>
<tr><td><strong>Protein Name</strong></td><td>Arylsulfatase B</td></tr>
<tr><td><strong>Gene</strong></td><td>[ARSB](/genes/arsb)</td></tr>
<tr><td><strong>UniProt ID</strong></td><td>[P15884](https://www.uniprot.org/uniprot/P15884)</td></tr>
<tr><td><strong>PDB IDs</strong></td><td>1FSH, 2GUJ, 3BBO</td></tr>
<tr><td><strong>Molecular Weight</strong></td><td>55.8 kDa (precursor), 42 kDa (mature)</td></tr>
<tr><td><strong>Subcellular Localization</strong></td><td>Lysosome</td></tr>
<tr><td><strong>Protein Family</strong></td><td>Sulfatase family</td></tr>
</table>
</div>

Overview

Arylsulfatase B (ARSB) is a lysosomal hydrolase enzyme that catalyzes the removal of sulfate groups from glycosaminoglycans (GAGs), specifically dermatan sulfate and chondroitin sulfate. This enzyme is essential for the normal degradation and recycling of these complex carbohydrates within lysosomes.

Structure

Domain Architecture

Signal Peptide: 21 amino acids for ER targeting
Propeptide: 24 amino acids removed during processing
Sulfatase Domain: ~400 amino acids containing the catalytic site
Formylglycine Cofactor: Unusual post-translational modification essential for catalytic activity

...

Arylsulfatase B Protein

Introduction

Arylsulfatase B Protein is an important component in the neurobiology of neurodegenerative diseases. This page provides detailed information about its structure, function, and role in disease processes.

<div class="infobox infobox-protein">
<table>
<tr><th colspan="2" style="background:#f0f0f0;">Arylsulfatase B (ARSB)</th></tr>
<tr><td><strong>Protein Name</strong></td><td>Arylsulfatase B</td></tr>
<tr><td><strong>Gene</strong></td><td>[ARSB](/genes/arsb)</td></tr>
<tr><td><strong>UniProt ID</strong></td><td>[P15884](https://www.uniprot.org/uniprot/P15884)</td></tr>
<tr><td><strong>PDB IDs</strong></td><td>1FSH, 2GUJ, 3BBO</td></tr>
<tr><td><strong>Molecular Weight</strong></td><td>55.8 kDa (precursor), 42 kDa (mature)</td></tr>
<tr><td><strong>Subcellular Localization</strong></td><td>Lysosome</td></tr>
<tr><td><strong>Protein Family</strong></td><td>Sulfatase family</td></tr>
</table>
</div>

Overview

Arylsulfatase B (ARSB) is a lysosomal hydrolase enzyme that catalyzes the removal of sulfate groups from glycosaminoglycans (GAGs), specifically dermatan sulfate and chondroitin sulfate. This enzyme is essential for the normal degradation and recycling of these complex carbohydrates within lysosomes.

Structure

Domain Architecture

Signal Peptide: 21 amino acids for ER targeting
Propeptide: 24 amino acids removed during processing
Sulfatase Domain: ~400 amino acids containing the catalytic site
Formylglycine Cofactor: Unusual post-translational modification essential for catalytic activity

Crystal Structure

The enzyme adopts a sulfatase fold characteristic of all sulfatases
Active site contains a conserved cysteine/formylglycine
Two N-glycosylation sites for proper folding and stability
Dimeric in the active form

Post-Translational Modifications

Formylglycine (FGly) Modification: Catalytic residue generated from a cysteine at position 51
N-linked Glycosylation: Multiple sites for carbohydrate attachment
Phosphorylation: Some regulatory phosphorylation sites identified

Normal Function

Enzymatic Activity

Catalyzes hydrolysis of sulfate ester bonds at the non-reducing end of GAGs
Specifically targets 4-sulfate groups on dermatan sulfate and chondroitin sulfate
Optimal activity at acidic pH (5.0-5.5) consistent with lysosomal environment
Requires metal ions (Ca²⁺) for structural stability

Role in GAG Catabolism

Final step in lysosomal degradation of dermatan sulfate
Completes the breakdown cascade initiated by other sulfatases
Prevents accumulation of partially degraded GAGs

Cellular Importance

Maintains lysosomal function and cellular homeostasis
Prevents accumulation of toxic GAG fragments
Essential for normal proteoglycan turnover

Role in Disease

Mucopolysaccharidosis Type VI (MPS VI)

Also known as Maroteaux-Lamy syndrome, MPS VI is caused by deficiency of Arylsulfatase B activity.

Pathogenesis:

Accumulation of dermatan sulfate in lysosomes
Progressive storage of GAGs in multiple tissues
Systemic clinical manifestations

Disease Progression:

Severe cases: rapid progression with early death
Attenuated cases: slower progression, longer survival
Neurological involvement varies by case

Therapeutic Targeting

Enzyme Replacement Therapy (ERT)

Galsulfase (Naglazyme®): FDA-approved recombinant human ARSB
Weekly intravenous infusions
Improves endurance and functional abilities
Does not cross the [blood-brain barrier](/entities/blood-brain-barrier)

Gene Therapy

AAV-mediated gene delivery in development
Potential for CNS-directed therapy
Challenges with blood-brain barrier penetration

Substrate Reduction Therapy

Small molecules reducing GAG synthesis
Being explored for MPS VI treatment

Key Publications

Bond CS, et al. (1997). "Structure of arylsulfatase B." Nat Struct Biol. PMID: 9278053(https://pubmed.ncbi.nlm.nih.gov/9278053/)

Roberts SH, et al. (2006). "Crystal structure of human arylsulfatase B." J Mol Biol. PMID: 16403646(https://pubmed.ncbi.nlm.nih.gov/16403646/)

Harmatz P, et al. (2018). "Enzyme replacement therapy for mucopolysaccharidosis VI: 10-year outcomes." Mol Genet Metab. PMID: 29428225(https://pubmed.ncbi.nlm.nih.gov/29428225/)

External Links

[UniProt: P15884](https://www.uniprot.org/uniprot/P15884)
[PDB: 1FSH](https://www.rcsb.org/structure/1FSH)
[RCSB: ARSB Structure](https://www.rcsb.org/structure/2GUJ)
[GeneReviews: MPS VI](https://www.ncbi.nlm.nih.gov/books/NBK148162)

Background

The study of Arylsulfatase B Protein has evolved significantly over the past decades. Research in this area has revealed important insights into the underlying mechanisms of neurodegeneration and continues to drive therapeutic development.

Historical context and key discoveries in this field have shaped our current understanding and will continue to guide future research directions.

References

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Related Entities

ARYLSULFATASEBPROTEIN

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📊 Evidence Profile

Evidence Balance

+0%

Certainty

45%

Debates

0

Incoming

9

Outgoing

10

0 supporting 0 contradicting 0 neutral

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📗 Cite This Artifact

Arylsulfatase B Protein

Arylsulfatase B Protein

Introduction

Overview

Structure

Domain Architecture

Arylsulfatase B Protein

Introduction

Overview

Structure

Domain Architecture

Crystal Structure

Post-Translational Modifications

Normal Function

Enzymatic Activity

Role in GAG Catabolism

Cellular Importance

Role in Disease

Mucopolysaccharidosis Type VI (MPS VI)

Therapeutic Targeting

Enzyme Replacement Therapy (ERT)

Gene Therapy

Substrate Reduction Therapy

Key Publications

See Also

External Links

Background

References

💬 Discussion