Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.6.1 (sulfatase)
 3,205 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The effects were studied of the total triterpenic fraction of Centella asiatica on serum levels of the uronic acids and lysosomal enzymes involved in mucopolysaccharide metabolism (beta-glycuronidase, beta-N-acetylglucosaminidase, arylsulfatase) in patients with varicose veins. The basal levels of uronic acids (467.7 +/- 69.3 micrograms/ml) and of lysosomal enzymes (beta-glycuronidase 1.8 +/- 0.4 microM/min/l, beta-N-acetylglucosaminidase 23.1 +/- 0.4 microM/min/l, arysulfatase 0.078 +/- 0.003 microM/min/l) were elevated, indicating an increased mucopolysaccharide turnover in subjects with varicose veins. During treatment with Centella asiatica extract (60 mg/day for three months), these levels fell progressively. At the end of treatment the serum uronic acid (231.8 +/- 51.5 micrograms/ml), beta-glycuronidase (1.2 +/- 0.05 microM/min/l), beta-N-acetylglucosaminidase (17.7 +/- 0.7 microM/min/l) and arysulfatase (0.042 +/- 0.003 microM/min/l) levels were highly significantly lower than the basal levels (p less than 0.01). The results of this trial provide an indirect confirmation of regulatory effects of the extract of Centella asiatica on metabolism in the connective tissue of the vascular wall.
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PMID:Effects of Centella asiatica extract on mucopolysaccharide metabolism in subjects with varicose veins. 215 Apr 5

Aggrecan-derived chondroitin sulfate (CS) chains, released by beta-elimination, were derivatized with p-aminobenzoic acid or p-aminophenol; radioiodinated; and subjected to graded or complete degradations by chondroitin ABC lyase to generate linkage region fragments of the basic structure DeltaGlyUA-GalNAc-GlcUA-Gal-Gal-Xyl-R (where DeltaGlyUA represents 4, 5-unsaturated glycuronic acid, and R is the adduct), by chondroitin AC lyase to generate the shorter fragment DeltaGlyUA-Gal-Gal-Xyl-R, or by chondroitin C lyase to generate the same fragment when it was linked to a 6-O-sulfated or unsulfated GalNAc at the nonreducing end. Fragments were separated by size using gel chromatography, by charge using ion-exchange chromatography, and by size/charge using electrophoresis and then characterized by stepwise degradations from the nonreducing end by using mercuric acetate to remove all terminal DeltaGlyUA, by bacterial glycuronidase to remove the same residue when linked to unsulfated or 6-O-sulfated GalNAc/Gal, by mammalian 4-sulfatase to remove sulfate from terminal GalNAc 4-O-sulfate, by chondro-4-sulfatase to remove 4-O-sulfate from other GalNAc/Gal residues, and by beta-galactosidase to remove terminal Gal. Results with CS from bovine nasal cartilage aggrecan show that, in nearly all chains, Xyl and probably also the first Gal are unsubstituted, whereas the second Gal is 4-O-sulfated in one CS chain out of five. The first disaccharide repeat is sulfated at C-4 of GalNAc in one chain out of three and unsulfated in the other two. A sulfated first disaccharide is always joined to an unsulfated GlcUA-Gal-Gal sequence. In contrast, CS from human articular cartilage usually has a sulfated first disaccharide repeat. In CS from young human cartilage, sulfate groups are mostly at C-4 of GalNAc in the major part of the chain, but at C-6 in the nonreducing distal portion. In CS from old cartilage, sulfation at C-6 of GalNAc is a major feature from the nonreducing end down to approximately positions 4 and 5 from the linkage region, where GalNAc 4-O-sulfate is common.
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PMID:Variations in the chondroitin sulfate-protein linkage region of aggrecans from bovine nasal and human articular cartilages. 891 Apr 87

Heparan sulfate glycosaminoglycans are structurally complex polysaccharides critically engaged in a wide range of cell and tissue functions. Any structure-based approach to study their respective biological functions is facilitated by the use of select heparan sulfate glycosaminoglycan-degrading enzymes with unique substrate specificities. We recently reported of one such enzyme, the Delta4,5-glycuronidase cloned from Flavobacterium heparinum and recombinantly expressed in Escherichia coli (Myette, J. R., Shriver, Z., Kiziltepe, T., McLean, M. W., Venkataraman, G., and Sasisekharan, R. (2002) Biochemistry 41, 7424-7434). In this study, we likewise report the molecular cloning of the 2-O-sulfatase from the same bacterium and its recombinant expression as a soluble, highly active enzyme. At the protein level, the flavobacterial 2-O-sulfatase possesses considerable sequence homology to other members of a large sulfatase family, especially within its amino terminus, where the highly conserved sulfatase domain is located. Within this domain, we have identified by sequence homology the critical active site cysteine predicted to be chemically modified as a formylglycine in vivo. We also present a characterization of the biochemical properties of the enzyme as it relates to optimal in vitro reaction conditions and a kinetic description of its substrate specificity. In particular, we demonstrate that in addition to the fact that the enzyme exclusively hydrolyzes the sulfate at the 2-O-position of the uronic acid, it also exhibits a kinetic preference for highly sulfated glucosamines within each disaccharide unit, especially those possessing a 6-O-sulfate. The sulfatase also displays a clear kinetic preference for disaccharides with beta1-->4 linkages but is able, nevertheless, to hydrolyze unsaturated, 2-O-sulfated chondroitin disaccharides. Finally, we describe the substrate-product relationship of the 2-O-sulfatase to the Delta4,5-glycuronidase and the analytical value of using both of these enzymes in tandem for elucidating heparin/heparan sulfate composition.
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PMID:The heparin/heparan sulfate 2-O-sulfatase from Flavobacterium heparinum. Molecular cloning, recombinant expression, and biochemical characterization. 1251 75