Arylsulfatase from Streptomyces griseorubiginosus S980-14.
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.
Ueki
T
T
Bristol-Myers Squibb Research Institute, Tokyo, Japan.
Sawada
Y
Y
Fukagawa
Y
Y
Oki
T
T
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
D001192:Arylsulfatases; D002118:Calcium