George, J. Richard published the artcileTyramine-mediated enhancement of arylsulfatase purified from Pseudomonas C12B, Quality Control of 6217-68-1, the publication is Biochemical Society Transactions (1979), 7(5), 1082-3, database is CAplus and MEDLINE.
The Km and Vmax of arylsulfatase, purified to homogeneity from Pseudomonas C12B, acting on the K salt of p-nitrophenyl sulfate (I) alone were 2.34 × 10-5M and 5.5 × 10-3 μmol/min, resp. As the ratio of tryptamine in the assay mixture was increased, the Km and Vmax were increased until values of 8.00 × 10-5M and 8.52 × 10-3 μmol/min were obtained. Arylsulfatase had less affinity, therefore, for the tryptamine salt than for the K salt of I, but hydrolyzed the tryptamine salt at a faster rate. At a tryptamine/I ratio of 5:1, the Vmax was 1.54-fold greater than that obtained with I alone. Phenylamines appear, therefore, to activate the activity in vitro of arylsulfatase from Pseudomonas by forming a salt with the substrate, which weakens the O-S bond of the sulfate ester, allowing it to be more rapidly hydrolyzed by the enzyme.
Biochemical Society Transactions 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, Quality Control of 6217-68-1.
Referemce:
https://en.wikipedia.org/wiki/Ester,
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