Effect of Enzymatic Sulfation on Biochemical and Pharmacological Properties of Catecholamines and Tyrosine-Containing Peptides.

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Abstract
Substrate specificity of a novel sulfotransferase produced by Eubacterium A-44 isolated from human feces has been studied. Phenolic drugs, catecholamines, were good acceptors of this bacterial enzyme. With regard to dopamine, sulfation mostly occurred at the 4-aromatic hydroxy group. We also investigated the effects of enzymatic sulfation on pharmacologically active phenolic compounds. Sulfation of phenolic compounds generally led to inactivation (e.g. tyramine and Leu-enkephalin), with the exception of cholecystokinin (CCK) and some gastrointestinal peptides. Proteolytic hydrolysis in vitro did not occur at the C-terminal of the sulfated tyrosine residues of peptides such as Leu-enkephalin and kyotorphin. These results suggest that the sulfation by bacterial enzyme plays an important role in detoxification, activation and stability of phenolic compounds in the human body.

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