title: Arylsulfatase from Streptomyces griseorubiginosus S980-14.
abstract: A new arylsulfatase designated Es-1, which desulfated etoposide 4'-sulfate and p-nitrophenyl sulfate, was isolated from Streptomyces griseorubiginosus S980-14 and purified to protein homogeneity by ammonium sulfate fractionation, ion exchange column chromatography, and chromatofocusing. The enzyme was active in monomeric form with an approximate molecular weight of 45,000, had a pI value of 4.95, and required calcium for full activity. At an optimum reaction pH of 8.5, iodoacetate, mercurous chloride, and EDTA severely inhibited the activity of Es-1 arylsulfatase.
authors.affiliation: Bristol-Myers Squibb Research Institute, Tokyo, Japan.
authors.forename: T
authors.initials: T
authors.lastname: Ueki
authors.forename: Y
authors.initials: Y
authors.lastname: Sawada
authors.forename: Y
authors.initials: Y
authors.lastname: Fukagawa
authors.forename: T
authors.initials: T
authors.lastname: Oki
mesh_terms: D001192:Arylsulfatases / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism*; D002118:Calcium / Q000378:metabolism; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D007700:Kinetics; D013302:Streptomyces / Q000201:enzymology*; D013379:Substrate Specificity
chemical_list: D001192:Arylsulfatases; D002118:Calcium