Abstract
The isolation of carbocyclic coformycin as the herbicidally active component from a fermentation of Saccharothrix species was described previously (B.D. Bush, G.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' 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'-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'-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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Claims 7
Claim · model-written summary
Carbocyclic coformycin rapidly increased ATP in treated pea seedlings.
- Taxon
- pea
Lathyrus oleraceuse0 - Material
- Onwarde0
- Organ / stage
- seedlingse0
- Treatment
- carbocyclic coformycine0
- Outcome
- ATP levelse0
- Direction
- increasee0
Not reportedComparator
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“When pea (Pisum sativum L. var Onward) seedlings are treated with carbocyclic coformycin, there is a very rapid and dramatic increase in ATP levels”
Claim · model-written summary
Carbocyclic coformycin treatment decreased extractable AMP deaminase activity in pea seedlings.
- Taxon
- peaLathyrus oleraceuse0
- Treatment
- carbocyclic coformycine0
- Gene
- AMP deaminasee1
- Outcome
- extractable activity of AMP deaminasee1
- Direction
- decreasee1
Not reportedComparator
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“When pea (Pisum sativum L. var Onward) seedlings are treated with carbocyclic coformycin”
e1“a decrease in the extractable activity of AMP deaminase”
Claim · model-written summary
The decrease in AMP deaminase activity correlated with strong noncovalent binding of the phosphorylated natural product to the protein.
- Taxon
- peaLathyrus oleraceuse1
- Gene
- AMP deaminasee0
- Compound
- phosphorylated natural producte0
- Outcome
- extractable activity of AMP deaminasee0
Not reportedDirection
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“a decrease in the extractable activity of AMP deaminase that correlates with a strong, noncovalent association of the phosphorylated natural product with the protein”
e1“pea (Pisum sativum L. var Onward) seedlings”
Claim · model-written summary
The 5'-phosphate analog of carbocyclic coformycin was a potent, tight binding inhibitor of pea AMP deaminase.
- Taxon
- peaLathyrus oleraceuse0
- Gene
- AMP deaminasee0
- Compound
- 5'-phosphate analog of the carbocyclic coformycine0
- Outcome
- potent, tight binding inhibitor of AMP deaminasee0
Not reportedDirection
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“The 5'-phosphate analog of the carbocyclic coformycin was synthesized and shown to be a potent, tight binding inhibitor of AMP deaminase isolated from pea seedlings”
Claim · model-written summary
Carbocyclic coformycin was rapidly converted to its 5'-phosphate analog in vivo.
- Taxon
- peaLathyrus oleraceuse1
- Outcome
- rapid conversion of carbocyclic coformycin to the 5'-phosphate analoge0
Not reportedDirection
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“rapid conversion of carbocyclic coformycin to the 5'-phosphate analog could be demonstrated in vivo”
e1“pea (Pisum sativum L. var Onward) seedlings”
Claim · model-written summary
The authors identified AMP deaminase inhibition following phosphorylation as the primary mode of action of carbocyclic coformycin.
- Taxon
- peaLathyrus oleraceuse1
- Gene
- AMP deaminasee0
- Compound
- carbocyclic coformycine0
- Outcome
- inhibition of the enzyme AMP deaminasee0
Not reportedDirection
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“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' hydroxyl on the carbocyclic ring in vivo”
e1“pea (Pisum sativum L. var Onward) seedlings”
Claim · model-written summary
The authors propose that AMP deaminase inhibition kills the plant by perturbing its intracellular ATP pool.
- Taxon
- peaLathyrus oleraceuse1
- Gene
- AMP deaminasee0
- Outcome
- death of the plante0
- Qualifier
- perturbation of the intracellular ATP poole0
Not reportedDirection
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“It is proposed that inhibition of AMP deaminase leads to the death of the plant through perturbation of the intracellular ATP pool.”
e1“pea (Pisum sativum L. var Onward) seedlings”
The same questions in other papers
coformycin · molecular: metabolites · Lathyrus oleraceus (pea)Results agree
1 paper in the same direction as this paper
- negative
Claims are grouped by organism, treatment and what was measured or targeted. A paper counts as positive when any of its claims in the group is positive.