Stimulation of bacterial arylsulfatase activity by arylamines: evidence for substrate activation.
A number of arylamines (including tyramine and tryptamine) increased the in vitro activity of arylsulfatase from Pseudomonas sp. 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 enzymatic and acid-catalyzed hydrolyses. The recrystallized tryptamine salt of the substrate exhibited a reduced affinity for the enzyme but was hydrolyzed more rapidly than the potassium salt, which is normally employed as the assay substrate.
D001192:Arylsulfatases / Q000378:metabolism*; D055598:Chemical Phenomena; D002621:Chemistry; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D011549:Pseudomonas / Q000201:enzymology*; D013268:Stimulation, Chemical; D013329:Structure-Activity Relationship; D013429:Sulfatases / Q000378:metabolism*; D014363:Tryptamines / Q000494:pharmacology*; D014439:Tyramine / Q000494:pharmacology*
D014363:Tryptamines; D013429:Sulfatases; D001192:Arylsulfatases; D014439:Tyramine