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Potent inhibition of specific diadenosine polyphosphate hydrolases by suramin
Author(s) -
Rotllán P,
Rodrı́guez-Ferrer C.R,
Asensio A.C,
Oaknin S
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00579-1
Subject(s) - suramin , polyphosphate , cytosol , chemistry , biochemistry , enzyme , intracellular , in vitro , phosphate
The cytosolic enzymes asymmetrical diadenosine tetraphosphate hydrolase (EC 3.6.1.17, Ap 4 Aase) and diadenosine triphosphate hydrolase (EC 3.6.1.29, Ap 3 Aase) are inhibited competitively by suramin. Ap 4 Aase and Ap 3 Aase were assayed in cytosolic rat brain extracts using fluorogenic analogues of the respective substrates diadenosine tetraphosphate (Ap 4 A) and diadenosine triphosphate (Ap 3 A). K i values for suramin as inhibitor of Ap 4 Aase and Ap 3 Aase were 5×10 −6 M and 3×10 −7 M, respectively. Results indicate that suramin or suramin‐like derivatives may be useful tools to investigate diadenosine polyphosphate cleaving enzymes and that the intracellular diadenosine polyphosphate metabolism may be a pharmacological target of suramin with biological and clinical implications.