Substrate-dependent arylsulfatase activity in the cyanobacterium plectonema 73110

Abstract

Arylsulfatase activity of the cyanobacterium Plectonem a 73110 is detected during growth on p-nitrophenyl sulfate as only sulfur source. A 60-fold purification of the soluble arylsulfatase yields a protein with an pH-optim um around 10 and K m data for p-nitrophenyl sulfate of 9.5 × 10-5 and for nitrocatechol sulfate of 3.4 × 10-5. The enzymatic activity is not effected by the cations Mg2+, Mn2+, K+ or Na+ used as chloride salts. The anions SO32- and SO42- did not inhibit this activity, however EDTA, thiols and triton X-100 decreased this activity to about 25% whereas SDS inhibited com pletely. Sulfate limitation is necessary for the developm ent of arylsulfatase activity in the presence of its substrate p-nitrophenyl sulfate. This arylsulfatase activity is partly bound to membranes. © 1986, Walter de Gruyter. All rights reserved.