Sulfur regulation of heparinase and sulfatases in Flavobacterium heparinum.
Sulfur regulation of heparinase synthesis and sulfatase synthesis was studied in Flavobacterium heparinum. Heparinase synthesis was strongly repressed by sulfate and L-cysteine, while the activity of this enzyme showed little or no inhibition by these compounds. Heparinase was synthesized in the absence of heparin when L-methionine was used as the sole sulfur source. The sulfatases produced by F. heparinum, which include the sulfatases involved in heparin catabolism, were also studied. At least some of the sulfatase activity was regulated by sulfur compounds in a manner similar to heparinase regulation. L-Cysteic acid and taurine were not suitable sulfur sources to support the growth of F. heparinum.
D000645:Ammonium Sulfate / Q000494:pharmacology; D003545:Cysteine / Q000494:pharmacology*; D004794:Enzyme Repression; D005417:Flavobacterium / Q000201:enzymology* / Q000254:growth & development; D019763:Heparin Lyase; D007700:Kinetics; D008715:Methionine / Q000494:pharmacology*; D011133:Polysaccharide-Lyases / Q000096:biosynthesis*; D013429:Sulfatases / Q000096:biosynthesis*; D013431:Sulfates / Q000494:pharmacology*
D013431:Sulfates; D008715:Methionine; D013429:Sulfatases; D011133:Polysaccharide-Lyases; D019763:Heparin Lyase; D003545:Cysteine; D000645:Ammonium Sulfate