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

The distribution of O-glycosylhydrolases (fucoidan hydrolases, alpha-D-mannosidases, beta-D-glucosidases, and beta-D-galactosidases) in 30 species of marine invertebrates occurring in the Sea of Japan was studied. It is shown that fucoidanases and glycosidases are widespread in the animals analyzed. Some molluscan, annelid, and echinoderm species can probably serve as objects for isolation and detailed study of the fucoidan-hydrolyzing enzymes. Fucoidan hydrolase, alpha-L-fucosidase, and arylsulfatase from the marine mollusk Littorina kurila were isolated and described. It was found that alpha-L-fucosidase and arylsulfatase hydrolyze synthetic substrates and cannot hydrolyze natural fucoidan, whereas fucoidan hydrolase cleaves fucoidan to produce sulfated oligosaccharides and fucose.
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PMID:Distribution of O-glycosylhydrolases in marine invertebrates. Enzymes of the marine mollusk Littorina kurila that catalyze fucoidan transformation. 1273 73

Fucoidans belong to a structurally heterogeneous class of sulfated polysaccharides isolated from brown algae. They have a wide spectrum of biological activities. The complex structures of these polysaccharides hinder structure-activity relationships determination. Fucoidan sulfatases can make useful tools for the determination of the fine chemical structure of fucoidans. In this study, identification and preparation of two recombinant sulfatases able to catalyze the cleavage of sulfate groups from fragments of fucoidan molecules is described for the first time. Two genes of sulfatases swf1 and swf4 of the marine bacterium Wenyingzhuangia fucanilytica CZ1127T were cloned and the proteins were produced in Escherichia coli cells. Sulfatases SWF1 and SWF4 are assigned to S1_17 and S1_25 subfamilies of formylglycine-dependent enzymes of S1 family (SulfAtlas). Some molecular and biochemical characteristics of recombinant fucoidan sulfatases have been studied. Detailed specificity and catalytic features of sulfatases were determined using various sulfated fucooligosaccharides. Structures of products produced by SWF1 and SWF4 were established by nuclear magnetic resonance (NMR) spectroscopy. Based on the obtained data, the enzymes are classified as fucoidan exo-2O-sulfatase (SWF1) and fucoidan exo-3O-sulfatase (SWF4). In addition, we demonstrated the sequential action of sulfatases on 2,3-di-O-sulfated fucooligosacchrides, which indicates an exolitic degradation pathway of fucoidan by a marine bacterium W. fucanilytica CZ1127T.
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PMID:Fucoidan Sulfatases from Marine Bacterium Wenyingzhuangia fucanilytica CZ1127T. 3024 71