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• W2022146761 abstract "Until now, the catabolism of adenosine(5')triphospho(5')adenosine (Ap3A) and adenosine(5')tetraphospho(5')adenosine (Ap4A) has been thought to commence with either hydrolytic or phosphorolytic cleavage of their oligophosphate chains, depending on the organism. Here, we show that in the extracts from the retractile 'foot' of the snail Helix pomatia deamination predominates; the adenosine moieties of these and other adenosine(5')oligophospho(5')adenosines (ApnAs) undergo successive deamination leading, via an inosine(5')oligophospho(5')adenosine (IpnA), to the corresponding inosine(5')oligophospho(5')inosine (IpnI). The reactions are catalyzed by the non-specific adenylate deaminase described earlier (Stankiewicz, A.J. (1983) Biochem. J. 215, 39-44). We describe TLC and HPLC systems which allow the separation of any of the deaminated derivatives from its parent compound; Ap2A, Ap3A, Ap4A or Ap5A. The Km values for these substrates are 20, 22, 32 and 39 microM, respectively, whereas the Km for 5'-AMP is 12 microM. Relative substrate specificities for these compounds amount to 25, 18, 14, 7 and 100. The enzyme was shown also to deaminate phosphonate and thiophosphate analogues of Ap3A." @default.
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• W2022146761 date "1995-01-18" @default.
• W2022146761 modified "2023-10-14" @default.
• W2022146761 title "Conversion of adenosine(5′)oligophospho(5′)adenosines into inosn(5′)oligophospho(5′)inosines by non-specific adenylate deaminase from the snail Helix pomatia" @default.
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• W2022146761 doi "https://doi.org/10.1016/0304-4165(94)00110-j" @default.
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