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 venom of Naja nigricolis was found to contain a high level of the enzyme aryl sulfatase. The enzyme was isolated from the venom of N. nigriclois and purified to electrophoretic homogeneity by gel chromatography on Sephadex G-100, DEAE-cellulose, and phenyl-sepharose columns. The enzyme was optimally active at pH 5 and 40 degrees C. Arrhenius plot for the determination of the activation energy (E(a)) gave the value 25 kJ/mol with a half-life (t(1/2)) of 5 min at 50 degrees C. It was highly activated by Fe(2+) and Ca(2+) and inhibited by Co(2+) and Mn(2+). The enzyme catalyzed the hydrolysis of the fluorescent compound methylumbelliferyl-sulfate (MU-SO(4)). Double reciprocal plots of initial velocity data, using MU-SO(4) as substrate, gave a K(M) value of 110 microM and V(max) of 225 micromol min(-1) x mg(-1). N. nigricolis Aryl sulphatase also hydrolyzed chondroitin-4-sulphate. It was inhibited competitively by N-acetyl glucosamine sulfate (GlcNAc-SO(4)), glucose-6-sulfate (Glc-6-SO(4)), and glucose 1-sulfate (Glc-1-SO(4)). Extrapolated inhibition binding constants (K(i)) gave the values of 3, 25, and 315 microM for GlcNAc-SO(4), Glc-6-SO(4), and Glc-1-SO(4) respectively.
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PMID:Aryl sulfatase from Naja nigricolis venom: characterization and possible contribution in the pathology of snake poisoning. 1261 48

Arylsulfatase cloned from a marine aerobic Gram-negative bacterium, Pseudoalteromonas carrageenovora, was overexpressed in Escherichia coli with 10 microM IPTG induction. The expressed recombinant arylsulfatase was purified to homogeneity from the harvested cells through osmotic disruption and column chromatography methods, such as DEAE-cellulose anion exchange chromatography and Heparin-Sepharose affinity chromatography. The purified arylsulfatase was kinetically characterized using the synthetic substrate of phenolic ester, p-nitrophenyl sulfate (pNPS). One unit of arylsulfatase catalyzes the liberation of 1.0 micromol p-nitrophenol from pNPS per minute. The purified enzyme has a specific activity of 468 U/mg with a purification yield of 27% from the cell lysate, and exhibited an estimated molecular mass of 33 kDa in SDS-PAGE analysis. The precursor polypeptide of 36 kDa was processed by releasing a putative signal peptide, and the mature arylsulfatase of 33.1 kDa with a N-terminal sequence of S-E-T-K-N was trafficked to periplasmic space. The enzyme had optimum reaction conditions for activity at pH 7.0 and at a temperature range of 40-45 degrees C. The apparent K(M) and k(cat) of the enzyme for hydrolysis of pNPS at pH 7.0 and at 45 degrees C were determined to be 1.15 mM and 1000 s-1, respectively. Based on inhibitor studies along with optimal pH values and preferential periplasmic location of the enzyme, we suggest that the recombinant arylsulfatase from P. carrageenovora is probably similar to the Klebsiella sulfatase with serine residue in the active site.
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PMID:Purification and characterization of the recombinant arylsulfatase cloned from Pseudoalteromonas carrageenovora. 1559 66

The activation of the preemergent herbicide 2-(2,4-dichlorophenoxy)ethyl sulfate (Crag herbicide) is initiated by soil microorganisms that are presumed to act by removing the ester sulfate group via some type of sulfatase enzyme. An enrichment technique with the herbicide as the sole source of sulfur led to the isolation of several pure cultures that could produce 2-(2,4-dichlorophenoxy)ethanol from the herbicide. One of these, a strain of Pseudomonas putida, was particularly active. Polyacrylamide gel zymograms of extracts of cells grown on nutrient broth showed the presence of three secondary and three primary alkylsulfatases. One of the latter enzymes was active toward Crag herbicide as well as sodium dodecyl sulfate. Maximum activity was obtained in the late-stationary phase of growth, and enzyme yields were not affected by either the presence or the absence of the herbicide in the growth medium. The enzyme was purified 2,670-fold to homogeneity by a combination of streptomycin sulfate treatment, heat treatment, and column chromatography on DEAE-cellulose, Sephacryl 200-S, and butyl agarose. The pure enzyme was tetrameric (molecular weight, 295,000) and most active at pH 6.0. Saturation kinetics with inhibition by excess substrate were observed for Crag herbicide and octyl sulfate. 2-Butox-yethyl sulfate was a relatively poor substrate, and dodecyltriethoxy sulfate was not hydrolyzed at all. Enzymatic hydrolysis of each substrate in the presence of H(2)O led to incorporation of O exclusively into SO(4) ions in all three cases. The Crag herbicide sulfatase therefore acts by cleaving the O-S bond of the C-O-S ester linkage, in contrast with other alkylsulfatases acting on long-chain alkyl sulfates.
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PMID:Initiation of Activation of a Preemergent Herbicide by a Novel Alkylsulfatase of Pseudomonas putida FLA. 1634 34

Sinalbin was identified as a chemical component of insect anti-xenosis and antibiosis resistance mechanisms in seedlings ofSinapis alba by DEAE-Sephadex chromatography, HPLC, treatment with sulfatase and myrosinase, various feeding tests using artificial and natural substrates, and by measuring sinalbin concentrations in cotyledons and leaves during seedling development. The effects of sinaibin on feeding were dependent upon the insect species and upon the rapidly changing profile of sinaibin concentrations in the developing seedling. The high concentrations of sinalbin found in young cotyledons (up to 20 mM) and leaves (up to 10 mM) deterred the feeding of the flea beetle,Phyllotreta cruciferae Goeze and larvae of the bertha armyworm,Mamestra configurata Walker. The protection that sinalbin confers upon the vulnerable, newly emerged seedling (and upon tiny, young leaves) appears critical for the first few days of survival ofS. alba under feeding pressure from flea beetles in the field. The lower concentrations of sinaibin found in older cotyledons and leaves (2-3 mM) offer little or no protection againstP. cruciferae and may actually stimulate the feeding of this crucifer specialist. These concentrations of sinaibin, however, are still effective in reducing the level of feeding by larvae of the more generalist feederM. configurata.
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PMID:Developmental profile of sinalbin (p-hydroxybenzyl glucosinolate) in mustard seedlings,Sinapis alba L., and its relationship to insect resistance. 2425 79


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