A novel route of ATP formation has been identified using erythrocytes from patients deficient in four different enzymes associated with ATP formation. It entails prior adenine production from deoxyadenosine (or adenosine) in a reaction involving S-adenosylhomocysteine hydrolase. The postulated route has been demonstrated in human erythrocytes which, unlike other human cells, cannot form ATP from IMP. It is based on studies by others using purified S-adenosylhomocysteine hydrolase preparations in vitro. The results provide the first confirmation that this reaction occurs in intact human cells in vitro and thus most probably in vivo. This adenine production is normally masked in intact cells by further metabolism to ATP. Clinical significance for such a route is suggested by the fact that some adenosine analogues with potent oncostatic and antiviral properties also release adenine (or analogues) in vitro.
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February 01 1989
ATP formation from deoxyadenosine in human erythrocytes: Evidence for a hitherto unidentified route involving adenine and S-adenosylhomocysteine hydrolase
H. A. Simmonds;
H. A. Simmonds
1Purine Research Laboratory, Clinical Science Laboratories, UMDS Guy's Hospital, London Bridge, London SE1 9RT, UK
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L. D. Fairbanks;
L. D. Fairbanks
1Purine Research Laboratory, Clinical Science Laboratories, UMDS Guy's Hospital, London Bridge, London SE1 9RT, UK
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J. A. Duley;
J. A. Duley
1Purine Research Laboratory, Clinical Science Laboratories, UMDS Guy's Hospital, London Bridge, London SE1 9RT, UK
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G. S. Morris
G. S. Morris
1Purine Research Laboratory, Clinical Science Laboratories, UMDS Guy's Hospital, London Bridge, London SE1 9RT, UK
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Publisher: Portland Press Ltd
Received:
July 11 1988
Online ISSN: 1573-4935
Print ISSN: 0144-8463
© 1989 Plenum Publishing Corporation
1989
Biosci Rep (1989) 9 (1): 75–85.
Article history
Received:
July 11 1988
Citation
H. A. Simmonds, L. D. Fairbanks, J. A. Duley, G. S. Morris; ATP formation from deoxyadenosine in human erythrocytes: Evidence for a hitherto unidentified route involving adenine and S-adenosylhomocysteine hydrolase. Biosci Rep 1 February 1989; 9 (1): 75–85. doi: https://doi.org/10.1007/BF01117513
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