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- W2007422078 abstract "Abstract To elucidate potential toxic properties of S-adenosylhomocysteine and 5′-methylthioadenosine, we have examined the inhibitory properties of these compounds upon enzymes involved with adenosine metabolism. S-Adenosylhomocysteine, but not S-adenosylmethionine, was a noncompetitive inhibitor of adenosine kinase with Ki values ranging from 100 to 400 μ m . Methylthioadenosine competitively inhibited adenosine kinase with variable adenosine below 1 μ m with a Ki of 120 μ m , increased adenosine kinase activity when the adenosine concentration exceeded 2 μ m , and did not appear to be a substrate for adenosine kinase. Methylthioadenosine inactivated S-adenosylhomocysteine hydrolase from erythrocytes, B-lymphoblasts, and T-lymphoblasts with Ki values ranging from 65 to 117 μ m and “k2” from 0.30 to 0.55 min−1. Adenosine deaminase was not inhibited by 5′-methylthioadenosine up to 1000 μ m . To clarify how 5′-methylthioadenosine might accumulate, 5′-methylthioadenosine phosphorylase was evaluated. This enzyme was not blocked by up to 500 μ m adenosine, deoxyadenosine, S-adenosylhomocysteine, or S-adenosylmethionine and was not decreased in erythrocytes from patients with adenosine deaminase deficiency, purine nucleoside phosphorylase deficiency, or hypogammaglobulinemia. These observations suggest that the inhibitory properties of 5′-methylthioadenosine upon adenosine kinase and S-adenosylhomocysteine hydrolase may contribute to the toxicity of the exogenously added compound. The toxicity resulting from S-adenosylhomocysteine accumulation intracellularly may be related to adenosine kinase inhibition in addition to disruption of transmethylation reactions." @default.
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- W2007422078 date "1982-04-01" @default.
- W2007422078 modified "2023-10-18" @default.
- W2007422078 title "Adenosine metabolism: Modification by S-adenosylhomocysteine and 5′-methylthioadenosine" @default.
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- W2007422078 doi "https://doi.org/10.1016/0003-9861(82)90308-3" @default.
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