When a mutant (Mao(-)) of Klebsiella aerogenes lacking an enzyme for tyramine degradation (monoamine oxidase) was grown with d-xylose as a carbon source, arylsulfatase was repressed by inorganic sulfate and repression was relieved by tyramine. When the cells were grown on glucose, tyramine failed to derepress the arylsulfatase synthesis. When grown with methionine as the sole sulfur source, the...

An arylsulfatase (EC 3.1.6.1) was extracted from Pseudomonas aeruginosa PA01 and purified 2700fold to homogeneity. Synthesis of this enzyme was repressed when sulfate, cysteine or thiocyanate was supplied as the sole sulfur source for growth, but derepressed with all other sulfur sources tested. The apparent molecular mass was determined by SDSPAGE to be 57 kDa, and the enzyme was presumed to b...

The aim of this study was to evaluate the actiion of Clostridium perfringens neuraminidase on the adherence of 28 strains of Pseudomonas aeruginosa which were isolated from humans, different animals and environment to human buccal epithelial cells (BECs). Two reference strainns--NCTC 6749 and ATCC 27853 were also examined. Incubation of cells with the enzyme significantly increased bacterial ad...

Saposin B is a small, nonenzymatic glycosphingolipid activator protein required for the breakdown of cerebroside sulfates (sulfatides) within the lysosome. The protein can extract target lipids from membranes, forming soluble protein-lipid complexes that are recognized by arylsulfatase A. The crystal structure of human saposin B reveals an unusual shell-like dimer consisting of a monolayer of a...

We previously demonstrated that an acidic variant form of lysosomal arylsulfatase B accumulated in chronic myelogenous leukemia (CML) cells was highly phosphorylated at its carbohydrate moiety (Uehara Y. et al. Cancer Res 435618. 1983). Since lysosomal hydrolases including the sulfatase underwent the posttranslational phosphorylation processing at the carbohydrate moiety, we investigated two en...

Streptoayces p. TI09-3 arylsulfatase (Es-2), which desulfated p-nitrophenyl sulfate as well as etoposide 4'-sulfate, was purified to protein homogeneity by sulfated cellulose aMnity and DEAE-cellulose column chromatographies. Es-2 required calcium for enzyme actiyity and was severely inhibited by SH and cheiating reEgents. Comparatiye characterization showed that, although distinct in recogniti...