Effect of enzymatic sulfation on biochemical and pharmacological properties of catecholamines and tyrosine-containing peptides.
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.
Konishi-Imamura
L
L
Faculty of Pharmaceutical Sciences, Toyama Medical and Pharmaceutical University, Japan.
Kim
D H
DH
Kobashi
K
K
D000818:Animals; D002395:Catecholamines / Q000737:chemistry / Q000494:pharmacology*; D010450:Endopeptidases / Q000378:metabolism; D006339:Heart Rate / Q000187:drug effects; D066298:In Vitro Techniques; D010455:Peptides / Q000494:pharmacology*; D051381:Rats; D013379:Substrate Specificity; D013431:Sulfates; D015238:Sulfotransferases / Q000378:metabolism; D014443:Tyrosine / Q000737:chemistry / Q000494:pharmacology*
D002395:Catecholamines; D010455:Peptides; D013431:Sulfates; D014443:Tyrosine; D015238:Sulfotransferases; D010450:Endopeptidases