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)

Steroid sulfatase of human placenta has been solubilized by treatment of the microsomal fraction with an amphoteric surface active agent, Miranol H2M and ultrasound. Criteria of solubility include non-sedimentation of the activity following centrifugation at 160,000 x g, its retention on Sepharose 6B and a single peak of activity after polyacrylamide gel electrophoresis. Enzyme activity was located in the same gel fractions for the two substrates tested; cholesterol sulfate and dehydroisoandrosterone sulfate. The addition of dithiothreitol was found necessary to maintain the stability of the enzyme indicating the presence of sulfhydryl groups in the molecule. A molecular weight of approximately 330,000 has been estimated from the elution volume of the enzyme system on a column of Sepharose 6B. It is believed that this protein represents a sulfatase enzyme complex composed of subunits with different specificities. From kinetic studies, a Km of 6.2 x 10(-5)M for the cleavage of dehydroisoandrosterone sulfate and a Km of 2 x 10(-6)M for the cleavage of cholesterol sulfate have been calculated.
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PMID:Solubilization and partial purification of steroid sulfatase of human placenta. 69 67

N-Acetylglucosamine-6-sulfate sulfatase, which liberates sulfate from the N-acetylglucosamine 6-sulfate residue at the nonreducing terminus of a 3H-labeled trisaccharide prepared from heparan sulfate, was purified 136-fold from human urine. The final N-acetylglucosamine-6-sulfate sulfatase preparation was free of all lysosomal sulfatases known to act on sulfated polysaccharides and gave a single band in polyacrylamide gel electrophoresis. The enzyme appears to be a glycoprotein with a molecular weight of around 97,000 and displays considerable charge heterogeneity. Multiple forms with pI values between 5.4 and 8.3 with a maximum at pH 7.7 were detected. The enzyme acts on the 3H-trisaccharide with a pH optimum at 5.5 and is active towards the sulfated monosaccharides N-acetylglucosamine 6-sulfate and glucose 6-sulfate. Although predominantly in exosulfatase, the enzyme catalyzes hydrolysis of sulfate from internal N-acetylglucosamine 6-sulfate moieties at a low rate. The Km for the 3H-trisaccharide, N-acetylglucosamine 6-sulfate, and glucose 6-sulfate were 0.15, 1.5, and 7.7 mM, respectively. The enzyme is inhibited by albumin, Hg2+, PO43-, SO42-, and CN-. Enzyme activity was highest in kidney and cultured fibroblasts but could be demonstrated in all human tissues tested.
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PMID:N-Acetylglucosamine-6-sulfate sulfatase from human urine. 76 21

Human N-acetylgalactosamine-6-sulfate sulfatase (6-sulfatase) activity is measured by using as a substrate a sulfated tetrasaccharide obtained by digesting purified chondroitin-6-sulfate (C-6-S) with testicular hyaluronidase. The amount of inorganic sulfate released is measured turbidimetrically. The enzyme from human kidney has a pH optimum of 4.8; its activity is augmented by low levels of NaCl and inhibited by phosphate and high levels of NaCl. Free glucuronate, acetylgalactosamine, inorganic sulfate, polymeric C-6-S, or tetrasaccharide obtained from chondroitin-4-sulfate do not affect the enzyme activity. The method may be used for the diagnosis of Morquio disease since extracts of Morquio fibroblasts are devoid of 6-sulfatase activity.
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PMID:N-acetylgalactosamine-6-sulfate sulfatase in man. Absence of the enzyme in Morquio disease. 82 Jul 16

The participation of tyramine oxidase in the regulation of arylsulfatase synthesis in Klebsiella aerogenes was studied. Arylsulfatase was synthesized when this organism was grown with methionine or taurine as the sulfur source (nonrepressing conditions) and was repressed by inorganic sulfate or cysteine; this repression was relieved by tyramine and related compounds (derepressing conditions). Under nonrepressing conditions, arylsulfatase synthesis was not regulated by tyramine oxidase synthesis. However, derepression of arylsulfatase and induction of tyramine oxidase synthesis by tyramine were both antagonized by glucose and other carbohydrate compounds. The derepressed synthesis of arylsulfatase, like that of tyramine oxidase, was released from catabolite repression by use of tyramine as the sole source of nitrogen. A mutant strain that exhibits constitutive synthesis of glutamine synthetase and high levels of histidase when grown in glucose-ammonium medium was subject to the catabolite repression of both tyramine oxidase and arylsulfatase syntheses. Mutants in which repression of arylsulfatase could not be relieved by tyramine could not utilize tyramine as the sole source of nitrogen and were defective in the gene for tyramine oxidase.
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PMID:Tyramine oxidase and regulation of arylsulfatase synthesis in Klebsiella aerogenes. 83 Jun 48

It was shown that at least four genes are specifically responsible for arylsulfatase synthesis in Klebsiella aerogenes. Mutations at chromosome site atsA result in enzymatically inactive arylsulfatase. Mutants showing constitutive synthesis of arylsulfatase (atsR) were isolated by using inorganic sulfate or cysteine as the sulfur source. Another mutation in which repression of arylsulfatase by inorganic sulfate or cysteine could not be relieved by tyramine was determined by genetic analysis to be on the tyramine oxidase gene (tyn). This site was distinguished from the atsC mutation site, which is probably concerned with the action or synthesis of corepressors of arylsulfatase synthesis. Genetic analysis with transducing phage PW52 showed that the order of mutation sites was atsC-atsR-atsA-tynA-tynB. On the basis of these results and previous physiological findings, we propose a new model for regulation of arylsulfatase synthesis.
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PMID:Genetic control of arylsulfatase synthesis in Klebsiella aerogenes. 85 36

The distribution of soluble arylsulfatase (aryl-sulfate sulfohydrolases, EC 3.1.6.1) in human tissues was investigated by DEAE-cellulose chromatography, All tissues examined contained arylsulfatase A and arylsulfatase B. In addition, brain singularly contained significant quantities (15-25% of total arylsulfatase) of a minor anionic arylsulfatase from designated arylsulfatase Bm, whereas only trace amounts of arylsulfatase Bm were found in liver, kidney, testis and placenta. Arylsulfatase B and arylsulfatase Bm had equal activity toward methyl-umbelliferyl sulfate, nitrocatechol sulfate and a physiological substrate UDP-N-acetylgalactosamine 4-sulfate, but both forms were inactive toward the arylsulfatase A substrates cerebroside sulfate and ascorbic acid 2-sulfate. Purified preparations of placental arylsulfatase B, brain arylsulfatase Bm, and urinary arylsulfatase A did not hydrolyze estrone sulfate, dehydroepiandrosterone sulfate or pregnenolone sulfate. The physico-chemical properties of arylsulfatase Band arylsulfatase Bm differed with respect to thermal lability, DEAE-cellulose chromatography, polyacrylamide gel electrophoresis and isoelectric focussing. In the latter technique, utilizing thin polyacrylamide slab gels, the isoelectric point for placental arylsulfatase B was 8.2, while brain arylsulfatase Bm resolved into 3 activity bands with pI values 6.8, 7.0 and 7.2. Although the physico-chemical properties differed, arylsulfatase B and arylsulfatase Bm appear to be functionally equivalent as well as generically related.
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PMID:Arylsulfatase of human tissue. Studies on a form of arylsulfatase B found predominantly in brain. 87 49

A radioimmunoassay using a commercially available antiserum was evaluated for measurement of serum unconjugated estriol in pregnancy. The evaluation showed an inter-assay variance of 12.1%, intra-assay variance of 6.8%, sensitivity of 0.2-0.6 ng/ml (0.7-2.1 nmol/l), and average recovery of 85.3%. The assay is specific for unconjugated estriol, showing less than 1% cross-reactivity with estriol-3-sulfate and estriol-16-glucuronide. Normal limits were established from 7 to 40 weeks' gestation using 175 serum samples. No diurnal variation could be demonstrated at 8 a.m. and 3 p.m. Eighty-nine serum specimens and 82 urine specimens obtained from 18 high-risk pregnancies were within normal limits except in cases of intruterine fetal death, pre-eclampsia, and suspected placental sulfatase deficiency. Serial urinary estriol levels fluctuated as much as 75%, while serial serum samples varied by only 30%.
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PMID:Evaluation of a radioimmunoassay for serum unconjugated estriol using commercial reagents. 90 77

Extracts of isolated rat peritoneal mast cells were demonstrated to contain appreciable quantities of arysulfatase activity. The enzyme was inhibited by both phosphate and sulfate ions and demonstrated a pH optimum of 5.0. The enzyme was recovered in the eluate of DE-52 columns and appeared to have a m.w. of 150,000 of Sephadex G-200 gel filtration. These findings and the anomalous kinetic behavior of the enzyme suggest that at least part of the enzymatic activity is of the arylsulfatase IIA type. While spontaneous release of the enzyme was observed, challenge of isolated rat mast cells with a goat anti-rat IgE serum resulted in a significant increase in release of the enzyme. The arylsulfatase activity extracted from isolated rat mast cells demonstrated comparable activity in inactivating slow reacting substance of anaphylaxis (SRS-A) to that described for human eosinophil and lung arylsulfatase.
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PMID:Functional characterization of rat mast cell arylsulfatase activity. 99 97

Pseudomonas sp. IFO-13309 and Actinobacillus sp. IFO-13310, bacteria which exhibit a symbiotic growth in a medium containing keratin sulfate as a sole carbon source, were isolated from soil. Extracts of these organisms were shown to contain an endoglycosidase, a sulfatase, and exo-beta-D-galactosidase, and an exo-beta-D-N-acetylglucosaminidase which, together, catalyze an extensive cleavage of corneal keratan sulfate. The Pseudomonas extract was particularly rich in the endoglycosidase activity and poor in the exoglycosidase activities. The Actinobacillus extract, in sharp contrast, contained principally the exoglycosidases. The sulfatase activity did not show this marked difference in distribution. A sulfatase was purified from the crude extract of Actinobacillus. The purified sulfatase reacted little or not at all with keratan sulfate, but acted on 2-acetamido-2-deoxy-6-O-sulfo-D-glucose, 2-acetamido-2-deoxy-6-O-sulfo-beta-D-glucosyl-(1 leads to 3)-D-galactose, and a tetrasaccharide trisulfate having 2-acetamido-2-deoxy-6-O-sulfo-D-glucose at the nonreducing end (prepared from keratan sulfate with an endogalactosidase). The enzyme removed one sulfate group from the tetrasaccharide trisulfate, producing an oligosaccharide which, unlike the parent oligosaccharide, was susceptible to hydrolysis with exo-beta-D-N-acetylglucosaminidase. The data suggest that the nonreducing end is the only site at wich enzymatic desulfation is carried out.
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PMID:Sequential degradation of keratan sulfate by bacterial enzymes and purification of a sulfatase in the enzymatic system. 111 96

In Klebsiella aerogenes, arylsulfatase synthesis was repressed by inorganic sulfate, sulfite, sulfide, thiosulfate, and cysteine, but not by methionine under normal growth conditions. We isolated cysteine-requiring mutants (Cys minus), and mutants (AtsS minus, AtsR minus) in which the regulation of arylsulfatase synthesis was altered. In the cysteine auxotroph, enzyme synthesis was also repressed by inorganic sulfate or cysteine. Kinetic studies on mutants of the cysteine auxotroph showed that inorganic sulfate repressed arylsulfatase synthesis and that this was not due to cysteine formed by reduction of sulfate. Arylsulfatase synthesis in the AtsS minus mutant was not repressed by inorganic sulfate but was repressed by cysteine. This mutant strain had a normal level of inorganic sulfate transport. Another mutant strain, defective in the inorganic sulfate transport system, synthesized arylsulfatase in the presence of inorganic sulfate but not in the presence of cysteine. The AtsS minus mutant could synthesize the enzyme in the presence of inorganic sulfate but not cysteine. The AtsR minus mutant could synthesize the enzyme in the presence of either inorganic sulfate or cysteine. These results suggest that there are two independent functional corepressors of arylsulfatase synthesis in K. aerogenes.
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PMID:Regulation of arylsulfatase synthesis by sulfur compounds in Klebsiella aerogenes. 111 90


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