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PLANT PHYSIOLOGY , Vol 114, Issue 1 119-129, Copyright © 1997 by American Society of Plant Biologists
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BIOCHEMISTRY AND ENZYMOLOGY |
Adenosine-5[prime]-Phosphate Deaminase (A Novel Herbicide Target)
J. E. Dancer, R. G. Hughes and S. D. Lindell
Department of Biochemistry, AgrEvo UK Limited, Chesterford Park, Saffron Walden, Essex, CB10 1XL, United Kingdom (J.E.D., R.G.H., S.D.L)
The isolation of carbocyclic coformycin as the herbicidally active
component from a fermentation of Saccharothrix species was described
previously (B.D. Bush, C.V. Fitchett, D.A. Gates, D. Langley [1993]
Phytochemistry 32: 737-739). Here we report that the primary mode of action
of carbocyclic coformycin has been identified as inhibition of the enzyme
AMP deaminase (EC 3.5.4.6) following phosphorylation at the 5[prime]
hydroxyl on the carbocyclic ring in vivo. When pea (Pisum sativum L. var
Onward) seedlings are treated with carbocyclic coformycin, there is a very
rapid and dramatic increase in ATP levels, indicating a perturbation in
purine metabolism. Investigation of the enzymes of purine metabolism showed
a decrease in the extractable activity of AMP deaminase that correlates
with a strong, noncovalent association of the phosphorylated natural
product with the protein. The 5[prime]-phosphate analog of the carbocyclic
coformycin was synthesized and shown to be a potent, tight binding
inhibitor of AMP deaminase isolated from pea seedlings. Through the use of
a synthetic radiolabeled marker, rapid conversion of carbocyclic coformycin
to the 5[prime]-phosphate analog could be demonstrated in vivo. It is
proposed that inhibition of AMP deaminase leads to the death of the plant
through perturbation of the intracellular ATP pool.
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