The DOI matches its Crossref record; 52 of the 52 references it cites were found in a registry or an index.
Human sulfatases: A structural perspective to catalysis
Open accessAbstract
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.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“STS is a membrane-bound enzyme on the luminal side of the endoplasmic reticulum (Ghosh, 2007) and ubiquitously expressed in all human tissues (Reed et al., 2005).”
From Intracrine androgen biosynthesis, metabolism and action revisited (2018) · cites this paper as Ghosh, 2007
Citations
Cites
Steroid sulfatase: molecular biology, regulation, and inhibition
Reed, M. J., Purohit, A., Woo, L. W. L., Newman, S. P., & Potter, B. V. L. (2005) · Endocrine Reviews · doi:10.1210/er.2004-0003 · Cited by 524
Dierks, T., Schmidt, B., Borissenko, L. V., Peng, J., Preusser-Kunze, A., Mariappan, M., & FIGURA, K. V. (2003) · Cell · doi:10.1016/s0092-8674(03)00347-7 · Cited by 384
Cosma, M. P., Pepe, S., Annunziata, I., Newbold, R. F., Grompe, M., Parenti, G., & Ballabio, A. (2003) · Cell · doi:10.1016/s0092-8674(03)00348-9 · Cited by 364
A novel amino acid modification in sulfatases that is defective in multiple sulfatase deficiency
Schmidt, B., Selmer, T., Ingendoh, A., & von Figurat, K. (1995) · Cell · doi:10.1016/0092-8674(95)90314-3 · Cited by 361
Lukatela, G., Krauß, N., Theis, K. W., Selmer, T., Gieselmann, V., FIGURA, K. V., & Saenger, W. (1998) · Biochemistry · doi:10.1021/bi9714924 · Cited by 326
Structure of a human lysosomal sulfatase
Bond, C. S., Clements, P. R., Ashby, S., Collyer, C. A., Harrop, S. J., Hopwood, J. J., & Guss, J. M. (1997) · Structure · doi:10.1016/s0969-2126(97)00185-8 · Cited by 297
Stanway, S. J., Purohit, A., Woo, L. W. L., Sufi, S., Vigushin, D. M., Ward, R. E., Wilson, R. H., Stanczyk, F. Z., Dobbs, N. A., Kulinskaya, E., et al. (2006) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-05-1996 · Cited by 244
Dierks, T., Dickmanns, A., Preusser-Kunze, A., Schmidt, B., Mariappan, M., FIGURA, K. V., Ficner, R., & Rudolph, M. G. (2005) · Cell · doi:10.1016/j.cell.2005.03.001 · Cited by 195
Estrogen sulfotransferase and steroid sulfatase in human breast carcinoma.
Suzuki, T., Nakata, T., Miki, Y., Kaneko, C., Moriya, T., Ishida, T., Akinaga, S., Hirakawa, H., Kimura, M., & Sasano, H. (2003) · PubMed · Cited by 185
Boltes, I., Czapinska, H., Kahnert, A., von Bülow, R., Dierks, T., Schmidt, B., FIGURA, K. V., Kertesz, M. A., & Usón, I. (2001) · Structure · doi:10.1016/s0969-2126(01)00609-8 · Cited by 174
Cited by
Sorted by citations
Braulke, T., & Bonifacino, J. S. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2008.10.016 · Cited by 811
RadicalS-Adenosylmethionine Enzymes
Broderick, J. B., Duffus, B. R., Duschene, K. S., & Shepard, E. M. (2014) · Chemical Reviews · doi:10.1021/cr4004709 · Cited by 843
The Regulation of Steroid Action by Sulfation and Desulfation
Mueller, J. W., Gilligan, L. C., Idkowiak, J., Arlt, W., & Foster, P. A. (2015) · Endocrine Reviews · doi:10.1210/er.2015-1036 · Cited by 419
Intracrine androgen biosynthesis, metabolism and action revisited
Schiffer, L., Arlt, W., & Storbeck, K.-H. (2018) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2017.08.016 · Cited by 217
“STS is a membrane-bound enzyme on the luminal side of the endoplasmic reticulum (Ghosh, 2007) and ubiquitously expressed in all human tissues (Reed et al., 2005).”
The structural biology of oestrogen metabolism
THOMAS, M. P., & Potter, B. V. L. (2013) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2012.12.014 · Cited by 181
Metadata
- Authors
- Ghosh, D.
- Affiliations
- Hauptman-Woodward Medical Research Institute (US)
- Corresponding author
- Ghosh, D.
- ORCID
- Ghosh, D.
- Venue
- Cellular and Molecular Life Sciences
- Published
- 2007-06-11
- Volume
- 64
- Issue
- 15
- Pages
- 2013-2022
- ISSN
- 1420-682X (ISSN-L)
- 1420-9071
- 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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
