Cited by 127Enzyme Structure and FunctionLysosomal Storage Disorders ResearchProtein Structure and Dynamics

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Human sulfatases: A structural perspective to catalysis

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Ghosh, D.·2007·Cellular and Molecular Life Sciences

DOI 10.1007/s00018-007-7175-yPMC PMC11136368

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Abstract

The sulfatase family of enzymes catalyzes hydrolysis of sulfate ester bonds of a wide variety of substrates. Seventeen genes have been identified in this class of sulfatases, many of which are associated with genetic disorders leading to reduction or loss of function of the corresponding enzymes. Amino acid sequence homology suggests that the enzymes have similar overall folds, mechanisms of action, and bivalent metal ion-binding sites. A catalytic cysteine residue, strictly conserved in prokaryotic and eukaryotic sulfatases, is post-translationally modified into a formylglycine. Hydroxylation of the formylglycine residue by a water molecule forming the activated hydroxylformylglycine (a formylglycine hydrate or a gem-diol) is a necessary step for the enzyme's sulfatase activity. Crystal structures of three human sulfatases, arylsulfatases A and B(ARSA and ARSB), and estrone/dehydroepiandrosterone sulfatase or steroid sulfatase (STS), also known as arylsulfatase C, have been determined. While ARSA and ARSB are water-soluble enzymes, STS has a hydrophobic domain and is an integral membrane protein of the endoplasmic reticulum. In this article, we compare and contrast sulfatase structures and revisit the proposed catalytic mechanism in light of available structural and functional data. Examination of the STS active site reveals substrate-specific interactions previously identified as the estrogen-recognition motif. Because of the proximity of the catalytic cleft of STS to the membrane surface, the lipid bilayer has a critical role in the constitution of the active site, unlike other sulfatases.

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Authors: Ghosh, D.
Affiliations: Hauptman-Woodward Medical Research Institute (US)
Corresponding author: Ghosh, D.
ORCID: Ghosh, D.
Venue: Cellular and Molecular Life Sciences
Publisher: Springer Science and Business Media LLC
Published: 2007-06-11
Volume: 64
Issue: 15
Pages: 2013-2022
ISSN: 1420-682X (ISSN-L)
1420-9071
DOI: 10.1007/s00018-007-7175-y
PMC: PMC11136368
OpenAlex: W2007796873
Cited by: 123
References: 52
Citations by year: 2026: 3 · 2025: 2 · 2024: 5 · 2023: 8 · 2022: 4 · 2021: 3 · 2020: 9 · 2019: 5 · 2018: 5 · 2017: 2 · 2016: 8 · 2015: 7 · 2014: 12 · 2013: 11 · 2012: 5
FWCI: 4.97
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.springer.com/tdm (tdm)
Locations: Cellular and Molecular Life Sciences (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Institute of General Medical Sciences (R01GM062794, GM62794)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
Health Sciences › Medicine › Genetics (clinical) › Lysosomal Storage Disorders Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Keywords: sulfatase, enzyme mechanism, formylglycine, arylsulfatase A, arylsulfatase B, steroid sulfatase, estrone sulfatase, arylsulfatase C, crystal structure, active site, endoplasmic reticulum membrane protein, lipid bilayers, genetic disorders
MeSH terms: Amino Acids, Breast Neoplasms, Catalysis, Cerebroside-Sulfatase, Female, Humans, Male, Models, Molecular, Pregnancy, Prostatic Neoplasms, Sulfatases, Protein Structure, Tertiary, Crystallography, X-Ray, N-Acetylgalactosamine-4-Sulfatase, Catalytic Domain, Steryl-Sulfatase, Static Electricity, In Vitro Techniques

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Human sulfatases: A structural perspective to catalysis

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