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- W2017292763 abstract "A new series of 5′-thioadenosine derivatives 1–4 were synthesized for selectively targeting 195Cys of human AdoHcy hydrolase. Their incubation with the enzyme resulted in time- and concentration-dependent inactivation, without major modifications of the NAD+/NADH ratio. The electrospray mass analysis of the inactivated enzyme with 1, 2, 3, and 4b showed that inhibition was accompanied by the formation of a specific and covalent labeling of each AdoHcy hydrolase subunit. Proteolytic cleavage (endo-Lys-C) and subsequent peptide characterization of the labeled enzyme revealed that 195Cys was the residue modified during the inactivation process." @default.
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- W2017292763 date "2004-12-01" @default.
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- W2017292763 title "Inactivation of human S-adenosylhomocysteine hydrolase by covalent labeling of cysteine 195 with thionucleoside derivatives" @default.
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- W2017292763 doi "https://doi.org/10.1016/j.bmcl.2004.09.051" @default.
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