Formylglycine-generating enzyme (FGE) catalyzes the oxidation of a specific cysteine residue in nascent sulfatase polypeptides to formylglycine (FGly). This FGly is part of the active site of all sulfatases and is required for their catalytic activity. Here we demonstrate that residues 34-68 constitute an N-terminal extension of the FGE catalytic core that is dispensable for in vitro enzymatic activity of FGE but is required for its in vivo activity in the endoplasmic reticulum (ER), i.e. for generation of FGly residues in nascent sulfatases. In addition, this extension is needed for the retention of FGE in the ER. Fusing a KDEL retention signal to the C terminus of FGE is sufficient to mediate retention of an N-terminally truncated FGE but not sufficient to restore its biological activity. Fusion of FGE residues 1-88 to secretory proteins resulted in ER retention of the fusion protein. Moreover, when fused to the paralog of FGE (pFGE), which itself lacks FGly-generating activity, the FGE ...

Multiple sulfatase deficiency (MSD) is a rare disorder characterized by impaired activity of all known sulfatases. The gene mutated in this disease is SUMF1, which encodes a protein involved in a post-translational modification at the catalytic site of all sulfatases that is necessary for their function. SUMF1 strongly enhances the activity of sulfatases when coexpressed with sulfatase in Cos-7 cells. We performed a mutational analysis of SUMF1 in 20 MSD patients of different ethnic origin. The clinical presentation of these patients was variable, ranging from severe neonatal forms to mild phenotypes showing mild neurological involvement. A total of 22 SUMF1 mutations were identified, including missense, nonsense, microdeletion, and splicing mutations. We expressed all missense mutations in culture to study their ability to enhance the activity of sulfatases. Of the predicted amino acid changes, 11 (p.R349W, p.R224W, p.L20F, p.A348P, p.S155P, p.C218Y, p.N259I, p.A279V, p.R349Q, p.C336R, p.A177P)

C alpha-formylglycine (FGly) is the catalytic residue of sulfatases in eukaryotes. It is generated by a unique post-translational modification catalysed by the FGly-generating enzyme (FGE) in the endoplasmic reticulum. FGE oxidizes a cysteine residue within the conserved CxPxR sequence motif of nascent sulfatase polypeptides to FGly. Here we show that this oxidation is strictly dependent on molecular oxygen (O-2) and consumes 1 mol O-2 per mol FGly formed. For maximal activity FGE requires an O-2 concentration of 9% (105 mu M). Sustained FGE activity further requires the presence of a thiol-based reductant such as DTT. FGly is also formed in the absence of DTT, but its formation ceases rapidly. Thus inactivated FGE accumulates in which the cysteine pair Cys336/Cys341 in the catalytic site is oxidized to form disulfide bridges between either Cys336 and Cys341 or Cys341 and the CxPxR cysteine of the sulfatase. These results strongly suggest that the Cys336/Cys341 pair is directly involved in the ...

In our continuing quest to design efficient inhibitors of estrone sulfatase activity and to assess the recognition of estrone sulfate surrogates by estrone sulfatase, we synthesized and evaluated several sulfonate derivatives of 5,6,7,8-tetrahydronaphth-2-ol and estrone. 5,6,7,8-Tetrahydronaphth-2-methanesulfonate (11), and 5,6,7,8-tetrahydronaphth-2-(p-toluene)sulfonate (12) were found not to inhibit estrone sulfatase activity; estrone-3-methane-sulfonate (5), estrone-3-ethanesulfonate (6), estrone-3-butanesulfonate (7), and estrone-3-[(+)10-camphor]sulfonate (8) all weakly inhibited estrone sulfatase, and the best inhibitor, from this class of compounds, was estrone-3-(p-toluene)sulfonate (9). At 10 microM, it inhibited estrone sulfatase activity by 91%. These results emphasize some of the requirements needed for high-affinity binding to the enzyme.

Summary: To further our aim of synthesizing aldehyde-tagged proteins for research and biotechnology applications, we developed methods for recombinant production of aerobic formylglycinegenerating enzyme (FGE) in good yield. We then optimized the FGE biocatalytic reaction conditions for conversion of cysteine to formylglycine in aldehyde tags on intact monoclonal antibodies. During the development of these conditions, we discovered that pretreating FGE with copper(II) is required for high turnover rates and yields. After further investigation, we confirmed that both aerobic prokaryotic (Streptomyces coelicolor) and eukaryotic (Homo sapiens) FGEs contain a copper cofactor. The complete kinetic parameters for both forms of FGE are described, along with a proposed mechanism for FGE catalysis that accounts for the copper-dependent activity... Click here to download white paper. ...

Multiple sulfatase deficiency (MSD) is a rare disorder characterized by impaired activity of all known sulfatases. The gene mutated in this disease is SUMF1, which encodes a protein involved in a post-translational modification at the catalytic site of all sulfatases that is necessary for their func …

Sulfatases are enzymes essential for degradation and remodeling of sulfate esters. Formylglycine (FGly), the key catalytic residue in the active site, is unique to sulfatases. In higher eukaryotes, FGly is generated from a cysteine precursor by the FGly-generating enzyme (FGE). Inactivity of FGE results in multiple sulfatase deficiency (MSD), a fatal autosomal recessive syndrome. Based on the crystal structure, we report that FGE is a single-domain monomer with a surprising paucity of secondary structure and adopts a unique fold. The effect of all 18 missense mutations found in MSD patients is explained by the FGE structure, providing a molecular basis of MSD. The catalytic mechanism of FGly generation was elucidated by six high-resolution structures of FGE in different redox environments. The structures allow formulation of a novel oxygenase mechanism whereby FGE utilizes molecular oxygen to generate FGly via a cysteine sulfenic acid intermediate. Molecular basis for multiple sulfatase ...

Steroid sulfatases are responsible for the hydrolysis of 3beta-hydroxy steroid sulfates, such as cholesterol and pregnenolone sulfate, and have an important role in regulating the synthesis of estrogenic steroids, from estrone sulfate and dehydroepiandrosterone sulfate, in endocrine-dependent tumors. Although little is known about the mechanism by which the sulfate group is removed from a steroid nucleus, an active site-directed sulfatase inhibitor has been developed. This inhibitor, estrone-3-O-sulfamate (EMATE), was synthesized by treating the sodium salt of estrone with sulfamoyl chloride. This compound inhibited not only estrone sulfatase but also dehydroepiandrosterone sulfatase activity in placental microsomes and in intact MCF-7 breast cancer cells. Pretreatment of MCF-7 cells or placental microsomes with EMATE, followed by extensive washing or dialysis indicated irreversible inhibition. This was confirmed by showing that EMATE inhibited estrone sulfatase activity in placental microsomes in a

The relative activities of arylsulphatases A and B were measured in rat liver parenchymal and non-parenchymal cells, in peritoneal macrophages and in a number of rat tissues. Although absolute values cannot be obtained, it was shown that the arylsulphatase B/arylsulphatase A activity ratio is much higher in non-parenchymal cells than in parenchymal cells. The ratios in adrenals, brain and testis are very similar to each other but differ from those found in spleen, kidney and liver. These ratio variations may be caused by alterations in the activity of the B enzyme rather than the A enzyme. The relatively high B enzyme/A enzyme ratios in all rat tissues explains why the method devised for the independent assay of human arylsulphatases A and B cannot be employed with rat tissues.. ...

Sulfatases EC 3.1.6.- are enzymes of the esterase class that catalyze the hydrolysis of sulfate esters. These may be found on a range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. In the latter case the resultant N-sulfates can also be termed sulfamates. Sulfatases play important roles in the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodelling sulfated glycosaminoglycans in the extracellular space. Together with sulfotransferases, sulfatases form the major catalytic machinery for the synthesis and breakage of sulfate esters. Sulfatases are found in lower and higher organisms. In higher organisms they are found in intracellular and extracellular spaces. Steroid sulfatase is distributed in a wide range of tissues throughout the body, enabling sulfated steroids synthesized in the adrenals and gonads to be desulfated following ...

QSulf1 function was investigated with antisense phosphorothiolated oligonucleotides developed to disrupt QSulf1transcript accumulation in embryos (Fig. 2, B1 to B4) (19). QSulf1 antisense specifically inhibited activation of MyoD (Fig. 2, B5 to B8), but notMyf5 (Fig. 2, B9 to B12), in the epaxial somite muscle progenitors and did not disrupt expression of Pax3 orPax1 in the ventral somite (11). AsMyf5, Pax3, and Pax1 are Shh response genes (14, 20), QSulf1 does not function in Shh signaling. However, MyoD is Wnt-inducible (21-23), implicating QSulf1 in Wnt signaling, which is controlled by HSPGs (7, 24, 25), the likely substrate of QSulf1 activity.. To assess whether QSulf1 is secreted, we cotransfected 10T1/2 cells with QSulf1-myc along with a green fluorescent protein (GFP) expression vector to identify transfected cells (26). Unpermeabilized cells were reacted with antibodies to myc to detect cell surface-localized QSulf1-myc or with antibody to β-tubulin, as a control for cell permeability. ...

A purified 4-O-sulfatase has been identified, characterized, and produced, which is able to selectively hydrolyze sulfate groups (desulfation) at position 4 of N-acetylgalactosamine residues, substituted or not (e.g. chondroitin-4-sulfate). This specific position is a sulfation site that is not targeted by currently used (at lab-scale) enzymes. (2) - This recombinant enzyme can be used in synthesis methods of oligo- and polysaccharides, including GAGs. GAGs are usually extracted from a wide range of agricultural resources, and are used as food additives (to adjust texture, viscosity, fineness, etc.) - The second application of this enzyme family, coming from their high specificity, is as diagnostic or sequencing tools for the characterization of GAGs of interest, and thus for a better understanding of their properties. Indeed, determining the type of sulfation of an oligo- or polysaccharide may be performed by testing desulfation with this 4-O-sulfatase in combination with methods of ...

Lai, Rasha Elgag Elsadig, Karin Reimann, Cheng Har Yip and Leslie (2001) Inhibition of oestrone sulphatase activity in the MDA-MB-231 Breast Cancer Cell Line by Breast Cyst Fluid from Malaysian Women. Anticancer Research, 21. pp. 2693-2696. ...

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The ability to site-specifically conjugate a protein to a payload of interest (e.g., a fluorophore, small molecule pharmacophore, oligonucleotide, or other protein) has found widespread application in basic research and drug development. For example, antibody-drug conjugates represent a class of biotherapeutics that couple the targeting specificity of an antibody with the chemotherapeutic potency of a small molecule drug. While first generation antibody-drug conjugates (ADCs) used random conjugation approaches, next-generation ADCs are employing site-specific conjugation. A facile way to generate site-specific protein conjugates is via the aldehyde tag technology, where a five amino acid consensus sequence (CXPXR) is genetically encoded into the protein of interest at the desired location. During protein expression, the Cys residue within this consensus sequence can be recognized by ectopically-expressed formylglycine generating enzyme (FGE), which converts the Cys to a formylglycine (fGly) residue. The

Dodgson, K.S., Spencer, B. and Williams, K. (1956). „Studies on sulphatases. 13. The hydrolysis of substituted phenyl sulphates by the arylsulphatase of Alcaligenes metacaligenes. Biochem. J. 64: 216-221. PMID 13363831 ...

|strong|Mouse anti Human Sulfatase 2 (C-Terminal) antibody, clone 2B4|/strong| recognizes an epitope within the C-terminal (CT) subunit of Sulfatase 2 (Sulf-2). Sulf-2 is a novel extracellular heparan…

Dehydration of theophylline monohydrate powder-effects of particle size and sample weight. Int J Pharma 1994 106 33-40. Ahlneck C, Zografi G. The molecular basis of moisture effects on the physical and chemical stability of drugs in the solid state. Int J Pharm 1990 62 87-95. Ahmed S, Owen CP, James K, Patel CK, Patel M. Acid dissociation constant, a potential phys-icochemical factor in the inhibition of the enzyme estrone sulfatase ES . Bioorg Med Chem Lett 2001, 9 Apr 11.... ...

Mouse anti Human Sulfatase 2 (C-Terminal) antibody, clone 2B4 recognizes an epitope within the C-terminal (CT) subunit of Sulfatase 2 (Sul

of FGE appeared to inhibit lipopolysaccharide (LPS)-enhanced heterotypic cell adhesion between THP-1 and BAECs. This result indicates that FGE blocks vascular inflammation. Then we found that FGE activates eNOS and Akt in BAECs. The phosphorylation of eNOS was maximally elevated 10 min after FGE treatment. Parallely, the phosphorylation of Akt was also maximally increased 10 min after FGE treatment. Consistently, it was found that FGE enhanced the production of nitric oxide. We then examined whether NO mediates THP-1 cell adhesion to BAECs. Both Akt and eNOS inhibitors appeared to reverse an inhibitory effect of FGE. These findings indicate that FGE inhibits LPS-enhanced heterotypic cell adhesion via Akt and eNOS. In conclusion, FGE plays an important role in prevention of inflammatory diseases. ...

Myc-DDK-tagged ORF clone of Homo sapiens sulfatase 1 (SULF1), transcript variant 1 as transfection-ready DNA - 10 µg - OriGene - cdna clones

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Research Project: A natural history study of Multiple Sulfatase Deficiency (MSD) in the fruit fly (Drosophila melanogaster) - The objective of discovering and validating phenotypes amenable for high- throughput drug screening, or screenotypes. Principle Investigator: Ethan Perlstein Ph.D.. Co-Applicant: Joshua Mast, Ph.D.. (An extract from Perlaras website). Perlara, a drug discovery platform company partnering with highly motivated families and drug developers to cure diseases thought too rare to matter, today announced a PerlQuest partnership with MSD Action Foundation (MSDAF), a research-focused charity based in Ireland. Multiple Sulfatase Deficiency (MSD) is an ultra-rare monogenic lysosomal disorder caused by mutations in the evolutionarily conserved gene SUMF1. MSD Action Foundation is aware of 62 living patients worldwide that are affected but the actual number is thought to be much higher. There are currently no approved treatments for MSD.. SUMF1 encodes a protein called ...

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1OIJ: Crystal Structure of the Alkylsulfatase Atsk: Insights Into the Catalytic Mechanism of the Fe(II) Alpha-Ketoglutarate-Dependent Dioxygenase Superfamily

Chemicals. Radiolabeled [4-14C]fluasterone (lot 9676-29-07 from Midwest Research Institute, Kansas, MO) had a radiochemical purity of approximately 97% and specific activity of 58.3 mCi/mmol. Fluasterone (lot 99973-1/91) was supplied by Proquina (Orizaba, Mexico). Standards of 16α-fluoro-5-androsten-17β-ol (17β-OH fluasterone) and 16α-fluoro-5-androsten-17α-ol (17α-OH fluasterone) were supplied by Dr. Marvin L. Lewbart (Department of Medicine, Jefferson Medical College, Philadelphia, PA). Sulfatase-free β-glucuronidase, bacterial from Escherichia coli, was supplied with phosphate buffer Sigma G8396 (Sigma-Aldrich, St. Louis, MO). β-Glucuronidase-free sulfatase, type VI, from Aerobacter aerogenes was supplied with 0.01 M Tris, pH 7.5, Sigma S1629 (Sigma-Aldrich). Soluene-350 tissue solubilizer and Ultima Gold scintillation mixture were purchased from PerkinElmer Life and Analytical Sciences (Waltham, MA).. Dosing and Collection of Biological Samples. Groups of male beagle dogs received ...

Heparan sulfate (HS) has been implicated in a wide range of cell signaling. Here we report a novel mechanism in which extracellular removal of 6-O-sulfate groups from HS by the endosulfatases, Sulf1 and Sulf2, is essential for axon guidance during development. In Sulf1/2 double knockout (DKO) mice, the corticospinal tract (CST) was dorsally displaced on the midbrain surface. In utero electroporation of Sulf1/2 into radial glial cells along the third ventricle, where Sulf1/2 mRNAs are normally expressed, rescued the CST defects in the DKO mice. Proteomic analysis and functional testing identified Slit2 as the key molecule associated with the DKO phenotype. In the DKO brain, 6-O-sulfated HS was increased, leading to abnormal accumulation of Slit2 protein on the pial surface of the cerebral peduncle and hypothalamus, which caused dorsal repulsion of CST axons. Our findings indicate that postbiosynthetic desulfation of HS by Sulfs controls CST axon guidance through fine-tuning of Slit2 presentation.

The Sulfs are 6-O endosulfatases that act on the trisulfated disaccharide unit (-IdoA(2-OSO3)-GlcNSO3(6-OSO3)-) which is the most common unit in heparin but is largely confined to the S-domains of HS [15-17]. As the heterogeneous pattern of sulfation within S domains is known to dictate the binding specificity of many proteins for heparin/HS [7], the Sulfs could potentially regulate those interactions with a dependence on the presence of trisulfated disaccharides within the binding motif. Here, we have employed Sulf-2 as a tool to explore the binding requirements of several proteins, some of which had been previously characterized and others whose binding requirements were largely unknown. Previous work has shown that QSulf-1 treatment of soluble recombinant form of an HSPG (Glypican-1) reduced its ability to bind a Wnt ligand [16]. Also, the interaction of Noggin with cell surface HSPGs was diminished by the overexpression of QSulf-1 in the cells [17]. In the present study we have taken ...

multiple sulfatase deficiency [DISEASE] OR juvenile sulfatidosis, Austin type [DISEASE] OR NCT01963650 [ID-NUMBER] OR NCT01536327 [ID-NUMBER] OR NCT01043640 [ID-NUMBER] OR NCT00383448 [ID-NUMBER] (5 records ...

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Bouchet, P. (2013). Charonia rubicunda (Perry, 1811). In: MolluscaBase (2017). Accessed through: Odido, M.; Appeltans, W.; BelHassen, M.; Mussai, P.; Nsiangango, S.E.; Vandepitte, L.; Wambiji, N.; Zamouri, N. Jiddou, A.M. (Eds) (2017). African Register of Marine Species at http://marinespecies.org/afremas/aphia.php?p=taxdetails&id=717009 on 2017-12- ...

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Many steps are necessary for the correct synthesis and processing of lysosomal enzymes.. Lysosomal Storage Disorders (LSDs) are caused by genetic defects that affect the synthesis or processing of lysosomal hydrolases. Therefore, a lysosomal disorder can be due to a defect in a specific hydrolase, by deficiencies in activator proteins, in the receptors or in the trafficking of enzymes.. The EUCLYD consortium will be focusing on four specific LSDs, namely Gaucher disease, Pompe disease, Mucopolysaccharidosis VI (MPS VI) and Multiple Sulfatase Deficiency (MSD), as prototypes of disorders with different stored materials in various organs and tissues outside the CNS.. The issues to be investigated in the proposed project are: i. pathophysiology and mechanisms underlying the symptoms and leading to devastating clinical consequences; ii. natural history, and iii. testing of novel therapeutic approaches. These issues will be addressed by patients studies and with animal models recapitulating the ...

E. coli Source ß-Glucuronidases ß-Glucuronidase is a ~290 kDa tetrameric protein with an isoelectric point of 4.8.1 Unlike the enzyme preparations from mollusks that naturally contain ß-glucuronidase and sulfatase activities in almost equal amounts, the preparation of ß-glucuronidase from E. coli is essentially free of sulfatase activity. The enzyme from E. coli has a high rate of hydrolytic activity and it retains this activity during hydrolysis better than similar enzymes that are more sensitive to changes in the concentration of ß-glucuronide conjugates. The enzyme preparation from E. coli has been shown to be useful for determining the presence of androsterone, 17-hydroxycorticosteroids, and estriol in urine.2 The E. coli enzyme has also been shown to be more active against estrogen conjugates than other sources of the enzyme.3 Optimal pH: 6-7 References1. Kim, D-H, et al., Biol. Pharm.

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Hodges, J.K.; Henderson, C.; Hearn, J.P., 1983: Relationship between ovarian and placental steroid production during early pregnancy in the marmoset monkey (Callithrix jacchus)

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1AUK: Crystal structure of human arylsulfatase A: the aldehyde function and the metal ion at the active site suggest a novel mechanism for sulfate ester hydrolysis.

Furcellaran is anionic partly sulphated polysaccharide which is classified together with carrageenan (E407).. The structure of furcellaran is similar to that of kappa carrageenan and has been described as a hybrid of kappa/beta carrageenans complex. The essential difference is that kappa carrageenan has one sulphate ester residue per two sugars, while furcellaran has one sulphate ester residue per three or four sugar residues.. Furcellaran is polysaccharide consisting of repeated disaccharide units of beta (R1 = R2 = H) and kappa carrageenan (R1 = SO3-, R2 = H). The structures of repeating disaccharide units of furcellaran and carrageenan are shown in figure 1.. ...

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