IngredientsSulfatases (also written sulphatases) are a large, evolutionarily ancient superfamily of hydrolytic enzymes defined by their capacity to cleave sulfate ester (C–O–S) and sulfamate (C–N–S) bonds from a wide variety of biological molecules. Sulfatases are hydrolytic enzymes that can cut sulfate groups from sulfate esters (CO–S) and sulfamates (CN–S). They are not a single compound but a family of related proteins sharing conserved structural and mechanistic features, each with its own substrate specificity.
Sulfatases are enzymes that catalyze the removal of sulfate from biological substances, and currently 17 human sulfatases have been identified. Their classification extends well beyond the human genome. Surprisingly, there are over 37,000 sulfatase genes in algae, accounting for approximately 90% of all sulfatase genes in the SulfAtlas Database.
The enzyme class is assigned Enzyme Commission number EC 3.1.6.– (sulfuric ester hydrolases), with individual subtypes holding specific EC numbers. For example, steroid sulfatase carries EC 3.1.6.2, and arylsulfatase A carries EC 3.1.6.8. In nature, sulfatases comprise a class of enzymes (EC 3.1.5.6) that are highly conserved sequentially, structurally, and mechanistically across both prokaryotic and eukaryotic species, having functions such as cell development and detoxification, sulfur scavenging, degradation of compounds, and osmoprotection.
Sulfatases occur in virtually all domains of life. In humans and other mammals, they are endogenous enzymes synthesized in the liver, placenta, adrenal glands, skin fibroblasts, lysosomes, and numerous other tissues. Sulfatases are expressed in various cellular compartments such as the lysosome, the endoplasmic reticulum, and the Golgi apparatus.
The marine environment represents by far the richest natural reservoir of sulfatase gene diversity. Sulphated polysaccharides such as carrageenan, fucoidan, and ulvan are predominantly produced by algae as structural components of their cell walls and represent one of the largest and most diverse sinks of organic carbon in the ocean. The sulphate esters are hypothesised to be an adaptation to marine life, as these modifications are far less common in land-based plants, yet in the ocean they can constitute up to 40% of the dry weight of these polymers.
Among microorganisms, sulfatases are prominently found in gut-dwelling bacteria. Arylsulfatases are involved in the degradation of sulfated compounds and have been purified from Clostridium perfringens. Glycosulfatase enzymes are also involved in the degradation of sulfated compounds and have been described primarily in the intestinal Prevotella and Bacteroides fragilis and have also been identified in the stomach Helicobacter pylori.
Without exception, newly described sulfatase activities have been S1 family sulfatases originating from bacteria and specific for complex carbohydrates (polysaccharides or proteoglycans). This is a significant change in trend, since most sulfatases were previously studied in humans and animals. Moreover, all the studied microorganisms were isolated from either human gut microbiota or marine environments.
Sulfatases are not consumed as dietary constituents in the conventional sense; they are endogenous enzymes. However, they appear in three distinct practical contexts relevant to health and medicine:
Natural sulfatases are typically large proteins that often comprise more than 500 amino acid residues, including up to about 800 amino acid residues for some eukaryotic sulfatases.
Sulfatases as biochemically defined enzymes were not recognised until the 20th century; accordingly, there is no recorded traditional or ethnobotanical history of sulfatases per se as isolated preparations. The concept of an enzyme did not exist in pre-modern medicine, and no documented traditional medical system identified or deliberately prepared sulfatase-containing substances for therapeutic use.
What does appear in historical and traditional contexts are sulfur-rich foods and preparations — including cruciferous vegetables, alliums, eggs, and seafood — whose health properties are now partially understood through the lens of sulfur biochemistry. Dietary sulfur, primarily derived from various natural sources, plays a crucial role in numerous physiological processes, including brain function. Natural sources of sulfur-rich substances include isothiocyanates, sulforaphane, glutathione, taurine, sulfated polysaccharides, allyl sulfides, and sulfur-containing amino acids, all of which have neuroprotective properties. However, these are sulfur compounds acted upon by or related to sulfatases, not sulfatase enzymes themselves.
The scientific identification of individual human sulfatases and their roles began with biochemical investigations in the mid-20th century. The first inborn errors of sulfatase metabolism — notably metachromatic leukodystrophy and mucopolysaccharidoses — were described clinically in the early 20th century, but their enzymatic bases were not elucidated until the 1960s through 1990s. The structure of steroid sulfatase and its role in estrogen metabolism was an active area of biochemical investigation from the 1970s onward, and the cloning of the STS gene and other human sulfatases proceeded through the 1980s and 1990s.
Human sulfatases comprise 17 genes, 10 of which are involved in congenital disorders, including lysosomal storage disorders, while the function of the remaining seven is still unclear. The principal members with established functions are listed below by their substrates and cellular locations:
ARSH, ARSI, ARSG, and ARSK are novel sulfatases that were identified through bioinformatics analysis, and they remain to be fully characterized.
All mammalian sulfatases share a unique and essential post-translational activation step. Sulfatases are enzymes that catalyze the removal of sulfate from biological substances, an essential process for the homeostasis of the body. They are commonly activated by the unusual amino acid formylglycine, which is formed from cysteine at the catalytic center, mediated by a formylglycine-generating enzyme as a post-translational modification.
These enzymes are activated by the formylglycine-generating enzyme (FGE), which is encoded by the sulfatase modifying factor 1 (SUMF1) gene. The catalytic mechanism itself relies on this formylglycine residue. Based on the crystal structures of several natural sulfatases, two reaction mechanisms that prominently utilize the α-formylglycine residue for catalysis have been proposed. In one proposed mechanism, the α-formylglycine residue, in its aldehyde form, is nucleophilically attacked by one of the sulfate group oxygen atoms within the substrate to form a sulfate diester. The alcohol conjugate is then released through the action of a nucleophile, such as an activated water molecule, to form a sulfate hemiacetal. Subsequent attack by the alcohol of the nucleophilic center within the sulfate hemiacetal causes the release of the sulfate molecule from the active site, regenerating the enzyme for future catalysis.
All known natural hydrolytic sulfatases contain two highly homologous amino acid motifs that have been previously identified as sulfatase signature sequences I and II, both of which are found in the N-terminal sequence region.
The substrates of mammalian sulfatases are sulfolipids, glycosaminoglycans, and steroid hormones. These enzymes maintain neuronal function in both the central and the peripheral nervous system, chondrogenesis and cartilage in the connective tissue, detoxification from xenobiotics and pharmacological compounds in the liver, steroid hormone inactivation in the placenta, and the proper regulation of skin humidification.
Sulfatases, which cleave sulfate esters in biological systems, play a key role in regulating the sulfation states that determine the function of many physiological molecules. Sulfatase substrates range from small cytosolic steroids, such as estrogen sulfate, to complex cell-surface carbohydrates, such as the glycosaminoglycans. The transformation of these molecules has been linked with important cellular functions, including hormone regulation, cellular degradation, and modulation of signaling pathways.
Many proteoglycans, glycoproteins, and glycolipids contain sulfated carbohydrates, which are sulfatase substrates. Sulfatases operate as decoding factors for a large amount of biological information contained in the structures of the sulfated sugar chains that are covalently linked to proteins and lipids. Modifications to these sulfate groups have pivotal roles in modulating specific signaling pathways and cell metabolism in mammals.
The sulfonation of carbohydrates leads to glycosaminoglycans with hydrogel-like properties that are necessary for the proper maintenance of cartilage and connective tissues. In the liver, sulfonation detoxifies xenobiotics and certain pharmaceutical compounds, such as acetaminophen, by increasing their hydrophobicity to eliminate them in the urine. Sulfonation also inactivates several biological products induced by hormones and neurotransmitters, maintaining the homeostasis of the body. Thus, improper control of this process disturbs biological systems.
Steroid sulfatase (STS; EC 3.1.6.2; also called arylsulfatase C) has been one of the most intensely studied members of the sulfatase family due to its central role in regulating estrogen availability, particularly in hormone-dependent cancers.
Steroid sulfatase (STS) is responsible for the hydrolysis of aryl and alkyl steroid sulfates and therefore has a pivotal role in regulating the formation of biologically active steroids. STS hydrolyzes steroid sulfates, such as estrone sulfate and dehydroepiandrosterone sulfate (DHEAS), to estrone and DHEA, which can be converted to steroids with potent estrogenic properties — that is, estradiol and androstenediol, respectively.
One important feature responsible for the tumoral production of estradiol (E2) is the desulfation of the inactive estrone sulfate (E1-S) by the steroid sulfatase (STS), an enzyme ubiquitously expressed in many organs and particularly in breast carcinoma tissue. E1-S is the most abundant circulating estrogen in postmenopausal women and its levels are 7 to 11 times higher in tumor tissues than in circulation.
Quantitative data show that the 'sulfatase pathway', which transforms estrogen sulfates into the bioactive unconjugated E2, is 100–500 times higher than the 'aromatase pathway', which converts androgens into estrogens. This finding has significant clinical implications: while most endocrine therapy for breast cancer has targeted the aromatase pathway, the sulfatase pathway may be quantitatively more important in local estrogen production within tumors.
Data suggest that steroid sulfatase (STS) activity is much higher than aromatase activity in breast tumors, and high levels of STS mRNA expression in tumors are associated with a poor prognosis.
Clinical evidence: A phase I/II clinical trial evaluated STX64, a potent irreversible STS inhibitor, in postmenopausal women with estrogen receptor–positive metastatic breast cancer. The drug recently completed the first-ever trial of this new type of therapy in postmenopausal women with estrogen receptor–positive metastatic breast cancer. STX64, tested at 5-mg and 20-mg doses, was able to almost completely block STS activity in peripheral blood lymphocytes and tumor tissues. Inhibition of STS activity was associated with significant reductions in serum concentrations of androstenediol and estrogens. Unexpectedly, serum androstenedione concentrations also decreased by up to 86%. Of eight patients who completed therapy, five showed evidence of stable disease for up to 7.0 months.
Evidence strength: The body of evidence on STS in breast cancer is substantial from molecular and biochemical standpoints, and preclinical evidence is robust. However, clinical evidence from completed trials remains preliminary; only small early-phase studies have been reported. STS inhibitors have not yet achieved regulatory approval as cancer treatments, and larger, controlled trials are needed.
Steroid sulfatase is critical for normal skin barrier function and desquamation (shedding of skin cells). X-linked ichthyosis (XLI) is defined as a condition inherited in an X-linked recessive manner, resulting from a deficiency of steroid sulfatase due to mutations in the STS gene. Although X-linked ichthyosis equally affects all ethnic groups and races worldwide, the condition predominantly affects males rather than females. With an incidence of 1 in 2,500 to 1 in 6,000 males, X-linked ichthyosis is the second most common type of ichthyosis, after ichthyosis vulgaris.
Affected patients can normally produce skin cells but cannot shed them correctly, leading to dry skin that accumulates in the form of polygonal scales. X-linked ichthyosis (XLI), which results from steroid sulfatase deficiency, is caused by mutation or deletion of the STS gene (300747) on chromosome Xp22. Most patients (90%) have deletions of the STS gene.
X-linked ichthyosis is characterized by cutaneous manifestations at birth, including pink or red skin with large, translucent scales, and is associated with an increased risk of cryptorchidism and ocular abnormalities. STS is a 62 kDa microsomal enzyme responsible for hydrolyzing the 3β-sulfate esters from both cholesterol sulfate and sulphated steroid hormones, generating their non-sulfated counterparts.
There is no approved enzyme replacement therapy for X-linked ichthyosis; current management is symptomatic, aimed at reducing skin dryness. Gene therapy approaches remain experimental.
Deficiencies in individual lysosomal sulfatases directly cause a group of inherited metabolic disorders known as mucopolysaccharidoses (MPS), characterized by progressive accumulation of undegraded glycosaminoglycans (GAGs) in cells and tissues. Enzyme deficiencies that prevent glycosaminoglycan breakdown cause accumulation of glycosaminoglycan fragments in lysosomes and cause extensive bone, soft tissue, and central nervous system changes.
Lysosomal sulfatases play a critical role in the degradation of macromolecules like sulfated glycosaminoglycans (GAGs), namely heparan sulfate (HS), chondroitin sulfate (CS), dermatan sulfate (DS) and keratan sulfate (KS), as well as a class of sulfolipids, also known as sulfatides.
Mucopolysaccharidosis VI (MPS VI) is a lysosomal storage disease with progressive multisystem involvement, associated with a deficiency of arylsulfatase B leading to the accumulation of dermatan sulfate. The characteristic skeletal dysplasia includes short stature and degenerative joint disease. Other manifestations include cardiac disease, impaired pulmonary function, ophthalmological complications, hepatosplenomegaly, sinusitis, otitis, hearing loss and sleep apnea. Intellectual impairment is generally absent. Clinical manifestation is typically by two or three years of age; however, slowly progressive cases may not present until adulthood.
Clinical evidence (ERT with galsulfase): The pivotal clinical study was a phase III, randomized, multicenter, placebo-controlled, double-blind study that evaluated the efficacy and safety of galsulfase in people with MPS VI. A total of 39 participants were included. Participants were over seven years of age with biochemical or genetic proof of MPS VI and the ability to walk without assistance at least five meters but no more than 270 meters in the first six minutes.
The results of one small study demonstrated that galsulfase is more effective than placebo in people with MPS VI, with significant improvements in the 12-minute walk test and a reduction in urinary glycosaminoglycans. There were no significant changes in cardiac or pulmonary functions, liver or spleen volume, overnight apnea-hypopnea, height and weight, quality of life and adverse effects. Further studies are needed to obtain more information on the long-term effectiveness and safety of enzyme replacement therapy with galsulfase.
Long-term observational data reinforce the signal of benefit. Data collected in a clinical surveillance program over 15 years provide real-world evidence for sustained improvements in endurance and pulmonary function among patients with MPS VI treated with ERT, with no new safety concerns identified. These results further support and confirm observations from the clinical trials and previous findings from the surveillance program.
In a Taiwanese case series, after 6.2 to 11.2 years of galsulfase treatment, six patients experienced improvement over baseline in the 6-minute walk test by a mean of 150 meters (59% change over time), and three patients also increased the 3-minute stair climb test by a mean of 60 steps (46%). Treatment reduced urinary GAG and had positive effects on a wide range of clinical functional assessments including endurance, mobility, joint function, pulmonary function, liver and spleen size, cardiac hypertrophy and diastolic dysfunction.
Galsulfase has been approved by the Food and Drug Administration in 2005 and by the European Medicines Agency in 2006.
Evidence strength: Moderate to good for galsulfase in MPS VI. The pivotal RCT was small (n=39) due to the rarity of the disease, but post-marketing surveillance over 15 years consistently confirms functional benefits and acceptable tolerability. The Cochrane review (2021) noted the limitation of evidence from a single small RCT.
Mucopolysaccharidosis type II (MPS II; also known as Hunter syndrome) is a rare, inherited lysosomal storage disease. The disease is caused by deficiency of the lysosomal enzyme iduronate-2-sulphatase (I2S) due to mutations in the IDS gene, which leads to accumulation of glycosaminoglycans (GAGs). Life-long enzyme replacement therapy with idursulfase (recombinant human I2S) is the current standard of care.
With pathogenic variants of the IDS gene, the activity of iduronate-2-sulfatase (IDS) is reduced or lost, causing the inability to degrade glycosaminoglycans (GAGs) in cells and influencing cell function, eventually resulting in multisystemic manifestations, such as a coarse face, dysostosis multiplex, recurrent respiratory tract infections, and hernias.
Despite MPS II being the most variable and wide-ranging of the MPS types, MPS II is often described as either an attenuated or "non-neuronopathic" phenotype, or a severe, progressive, "neuronopathic" phenotype involving central nervous system dysfunction.
MPS IIIA is inherited in an autosomal recessive manner and is caused by a deficiency in the lysosomal enzyme sulfamidase, which is required for the degradation of heparan sulfate. The sulfamidase is produced by the N-sulphoglucosamine sulphohydrolase (SGSH) gene. In MPS IIIA patients, the excess of lysosomal storage of heparan sulfate often leads to mental retardation, hyperactive behavior, and connective tissue impairments.
Sulfatide degradation is dependent on a single lysosomal sulfatase as reflected by the severe lysosomal storage disease metachromatic leukodystrophy resulting from deficiency of arylsulfatase A. Metachromatic leukodystrophy (MLD) is an inherited, autosomal recessive disorder of lipid metabolism characterized by deficient activity of the lysosomal enzyme arylsulfatase A (ASA), which results in progressive accumulation of galactosylceramide-3-O-sulfate (cerebroside sulfate or sulfatide) and a cytotoxic metabolite of sulfatide.
A clinical trial for intrathecal administration of arylsulfatase A in MLD has been investigated. A clinical trial has demonstrated that intrathecal administration of recombinant human heparan-N-sulfatase, which is well tolerated in individuals with MPS IIIA, results in consistent decrease of heparan sulfate in the CSF. The blood-brain barrier remains a major obstacle for intravenous delivery of sulfatases to the CNS.
Because all sulfatases require FGE for activation, mutations in SUMF1 cause simultaneous failure of all 17 known human sulfatases — a condition termed Multiple Sulfatase Deficiency. Multiple sulfatase deficiency (MSD) is an ultra-rare neurodegenerative disorder that results in defective sulfatase post-translational modification. Sulfatases in the body are activated by a unique protein, formylglycine-generating enzyme (FGE), encoded by SUMF1. When FGE is absent or insufficient, all 17 known human sulfatases are affected, including the enzymes associated with metachromatic leukodystrophy (MLD), several mucopolysaccharidoses (MPS II, IIIA, IIID, IVA, VI), chondrodysplasia punctata, and X-linked ichthyosis.
Individuals with MSD and their families encounter a complex range of health problems and challenges that are unique even among lysosomal storage diseases. The primary issues arise from a combination of neurologic disease, including developmental delay and regression, and extraneurologic manifestations such as cardiopulmonary complications and skeletal anomalies.
Based on the onset and severity of the disease, MSD has been traditionally divided into several forms: neonatal, severe late infantile, mild infantile, and juvenile. The severity of the disorder is thought to be dependent on the stability and degree of residual enzymatic activity of dysfunctional FGE resulting in variable levels of residual sulfatase activities. Unfortunately, as is true for most lysosomal storage disorders, there are currently no curative options for individuals with MSD.
Two extracellular sulfatases — Sulf-1 and Sulf-2 — regulate growth factor availability at the cell surface and have significant roles in cancer biology. Once presented on the cell surface, heparan sulfate proteoglycans (HSPGs) are further modified by two extracellular 6-O-endosulfatase enzymes, Sulf-1 and Sulf-2, which catalyze subtle but consequential changes within growth factor-binding regions of the glycan chains by removing glucosamine 6-O-sulfates. Despite being closely related isoforms, systems-level biological studies indicate specific roles for each Sulf. In cancer specifically, over-expression of Sulf-1 can be anti-oncogenic, while overexpression of Sulf-2 is generally pro-oncogenic, leading to increased tumorigenesis.
Evidence strength: Preclinical and mechanistic evidence is robust; Sulf-1/Sulf-2 are active research targets, but no approved therapies specifically targeting these enzymes exist as of the current literature.
Bacterial sulfatases in the gut microbiome play essential roles in nutrient access and intestinal colonization. Sulfatases are essential to the utilization of distal colonic mucin O-glycans by the human gut symbiont Bacteroides thetaiotaomicron. Humans have co-evolved with a dense community of microbial symbionts that inhabit the lower intestine. In the colon, secreted mucus creates a barrier that separates these microorganisms from the intestinal epithelium. Some gut bacteria are able to utilize mucin glycoproteins, the main mucus component, as a nutrient source.
Sulfatases are essential to the utilization of colonic mucin O-glycans by the human gut symbiont Bacteroides thetaiotaomicron. The activity of 12 different sulfatases encoded by this species shows that these enzymes collectively are active on all of the known sulfate linkages in colonic O-glycans.
Sulfatase activity is likely to be a keystone step in bacterial mucin degradation, and inhibition of these enzymes may therefore represent a viable therapeutic path for treatment of IBD and other diseases.
Evidence strength: Predominantly preclinical (in vitro and animal model studies). Clinical implications for IBD therapy are conceptually supported but not yet tested in human trials. This is an active area of investigation.
Given the prevalence of sulfated polysaccharides like agar, carrageenans, fucoidans, and ulvans in seaweeds, many marine microbes possess the metabolic machinery needed for the utilization of these biopolymers, thus playing crucial roles in the marine carbon cycle. While numerous enzymes active on such polysaccharides originating from marine microorganisms and environments have been characterized, information regarding marine polysaccharide-specific sulfatases remains limited. Nevertheless, the significance of these enzymes is evident, particularly in industrial processing of carrageenans, where targeted removal of sulfate groups and the production of new carrageenan structures can generate new functional properties and potential bioactivities.
Carrageenans are sulfated polysaccharides found in the cell wall of certain red seaweeds. They are widely used in the food industry for their gelling and stabilizing properties. In nature, carrageenans undergo enzymatic modification and degradation by marine organisms. Characterizing these enzymes is crucial for understanding carrageenan utilization and may eventually enable the development of targeted processes to modify carrageenans for industrial applications.
Given the breadth of sulfatase substrates, these enzymes touch virtually every major body system:
Sulfatases as therapeutic agents are administered exclusively as injected recombinant proteins; they are not available as oral dietary supplements because proteins are digested in the gastrointestinal tract before reaching systemic circulation.
Nine Taiwanese patients with MPS VI were treated with weekly intravenous infusions of galsulfase at 1.0 mg/kg in 5 medical centers in Taiwan. This dose — 1.0 mg/kg body weight administered as a weekly intravenous infusion — is the standard approved dose cited across clinical studies.
International guidelines recommend enzyme replacement therapy (ERT) with galsulfase (Naglazyme®) in patients with MPS VI as soon as possible after a confirmed diagnosis.
STX64, tested at 5-mg and 20-mg doses, was able to almost completely block STS activity in peripheral blood lymphocytes and tumor tissues in the first-in-class early-phase clinical trial in postmenopausal women with ER-positive metastatic breast cancer.
Other methods of ERT administration, such as intrathecal injections, are effective in delivering ERT to normalize substrate storage in the CNS of MPS III animal models. A clinical trial has demonstrated that intrathecal administration of recombinant human heparan-N-sulfatase, which is well tolerated in individuals with MPS IIIA, results in consistent decrease of heparan sulfate in the CSF.
No dietary supplement product delivers active sulfatase enzyme. Products that claim to support "sulfation pathways" do not contain sulfatase proteins but may contain sulfur-donating nutrients (e.g., MSM, sulfur amino acids) that participate in related metabolic cycles.
Galsulfase was generally well tolerated with no new safety signals identified over 15 years of clinical surveillance. Most adverse events were MPS-related clinical manifestations and considered not related to galsulfase by investigators.
The pivotal clinical trials of galsulfase showed rapid and sustained reductions in urinary GAGs and significant and sustained improvements in endurance in the 6-min walk test and 3-min stair climb test, and in pulmonary function in treated patients, as well as an acceptable safety profile. The primary known safety concern with all enzyme replacement therapies — including galsulfase — is the risk of infusion-associated reactions and the development of anti-drug antibodies, which can attenuate efficacy over time. These are monitored in all treated patients per clinical guidelines.
Inherited sulfatase deficiencies — not sulfatase supplementation — are the principal safety concern with this enzyme class. Deficiencies in six lysosomal sulfatases lead to severe lysosomal storage diseases caused by accumulation of the corresponding sulfated substrate in the lysosome, resulting in the impairment of lysosomal function as well as the initiation of pathological cascades outside the lysosomes.
Common manifestations of MPS-type lysosomal storage diseases include coarse facial features, neurodevelopmental delays and regression, joint contractures, organomegaly, stiff hair, progressive respiratory insufficiency caused by airway obstruction and sleep apnea, cardiac valvular disease, skeletal changes, and cervical vertebral subluxation.
The crystal structure of steroid sulfatase has been resolved, but relatively little is known about what regulates its expression or activity. Research into the control and inhibition of this enzyme has been stimulated by its important role in supporting the growth of hormone-dependent tumors of the breast and prostate.
Steroid sulfatase has significant potential as a novel drug target in hormone-dependent cancers such as in the breast or prostate, and in conditions like endometriosis. From the early 1990s onwards, reversible (non-covalently bound) and time-dependent irreversible STS inhibitors have been under investigation. Any compound that substantially inhibits or augments endogenous steroid sulfatase activity could, in theory, alter circulating levels of bioactive estrogens, androgens, and DHEA — with potential downstream hormonal effects. This is relevant to the pharmacology of tamoxifen, aromatase inhibitors, and other endocrine therapies.
Antibiotics that deplete sulfatase-producing Bacteroides and Prevotella species from the gut could alter intestinal mucin glycan metabolism. The detailed mechanisms of the cross-talk between the gut microbiome and the human host are complex, dynamic, and still to be fully determined. While the mutually beneficial relationship of the host provides an environment and nutrients for the bacteria to thrive, the bacteria contribute to various aspects of human health. The specific clinical consequences of disrupted microbial sulfatase activity in humans have not been established in controlled clinical trials.
The field of sulfatase biology is rapidly evolving. Research areas of active investigation include:
In the last six years, 19 new sulfatase activities have been discovered, indicating an increase in the discovery rate. Almost all these studies have adopted the SulfAtlas classification and use it as a guide to select subfamilies with unknown substrate specificity.
Health conditions that Sulfatase may help support.
Body systems that Sulfatase may help support.
Go back