George, James R. published the artcileStimulation of bacterial arylsulfatase activity by arylamines: evidence for substrate activation, Name: Potassium 4-nitrophenyl sulfate, the publication is Journal of Bacteriology (1981), 147(1), 69-74, database is CAplus and MEDLINE.
A number of arylamines (including tyramine and tryptamine) increased the in vitro activity of arylsulfatase from Pseudomonas species strain C12B. Amino acid analogs of these amines (e.g., tyrosine and tryptophan) failed to exert an effect. Stimulation of activity by tyramine could not be accounted for in terms of sulfotransferase activity for this phenol and no shift in the pH optimum for the enzyme occurred in the presence of tryptamine. Increased Vmax due to these amines was independent of enzyme concentration but varied significantly with substrate concentration Evidence is presented which suggests that arylamines enhance arylsulfatase activity by forming a salt linkage with the substrate and rendering it more susceptible to enzymic and acid-catalyzed hydrolysis. The recrystallized tryptamine salt of the substrate exhibited a reduced affinity for the enzyme but was hydrolyzed more rapidly than the K salt, which is normally employed as the assay substrate.
Journal of Bacteriology published new progress about 6217-68-1. 6217-68-1 belongs to esters-buliding-blocks, auxiliary class Salt,Nitro Compound,Sulfonate,Benzene, name is Potassium 4-nitrophenyl sulfate, and the molecular formula is C6H4KNO6S, Name: Potassium 4-nitrophenyl sulfate.
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