A new type of Streptomycete arylsulfatase with high affinity to the sulfuryl moiety of the substrate.
Streptomyces sp. T109-3 arylsulfatase (Es-2), which desulfated p-nitrophenyl sulfate as well as etoposide 4'-sulfate, was purified to protein homogeneity by sulfated cellulose affinity and DEAE-cellulose column chromatographies. Es-2 required calcium for enzyme activity and was severely inhibited by SH and chelating reagents. Comparative characterization showed that, although distinct in recognition of the binding moiety of substrate, Es-1 (Streptomyces griseorubiginosus S980-14 arylsulfatase) and Es-2 shared high desulfating activity on etoposide 4'-sulfate and many other common enzymological characteristics, which suggested they would be acceptable as the enzyme component of antitumor antibody-enzyme conjugates for target chemotherapy.
Ueki
T
T
Bristol-Myers Squibb Research Institute, Tokyo, Japan.
Sawada
Y
Y
Fukagawa
Y
Y
Oki
T
T
D000595:Amino Acid Sequence; D000818:Animals; D001192:Arylsulfatases / Q000097:blood / Q000302:isolation & purification / Q000378:metabolism*; D002118:Calcium / Q000378:metabolism; D002417:Cattle; D002846:Chromatography, Affinity; D002848:Chromatography, DEAE-Cellulose; D004591:Electrophoresis, Polyacrylamide Gel; D004795:Enzyme Stability; D005047:Etoposide / Q000031:analogs & derivatives* / Q000378:metabolism; D007700:Kinetics; D008670:Metals; D008969:Molecular Sequence Data; D013302:Streptomyces / Q000201:enzymology*; D013379:Substrate Specificity; D013463:Sulfuric Acid Esters / Q000378:metabolism*
D008670:Metals; D013463:Sulfuric Acid Esters; C094687:etoposide 4'-sulfate; D005047:Etoposide; D001192:Arylsulfatases; D002118:Calcium