Abstract
Halophosphonate ATP analogues pp[CHBr]pA and p[CHBr]ppA synthesised from bromomethylenebisphosphonate and adenosine derivatives, proved to be effective competitive inhibitors of Ac-CoA-carboxylase (CE 6.4.1.2) from rat liver (Ki = 0,2 mM). The inhibitory effects of both analogues were reversible and higher than those of some other ATP analogues. Another enzyme, Ac-CoA-synthetase (CE 6.2.1.1), with a different mode of ATP-cleavage showed wider specificity to ATP-analogues than Ac-CoA-carboxylase.
MeSH terms
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Acetate-CoA Ligase / antagonists & inhibitors*
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Acetyl-CoA Carboxylase / antagonists & inhibitors*
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Adenosine
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Adenosine Triphosphate / analogs & derivatives
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Animals
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Chemical Phenomena
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Chemistry
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Coenzyme A Ligases / antagonists & inhibitors*
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Cytosol / enzymology
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Diphosphonates
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In Vitro Techniques
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Ligases / antagonists & inhibitors*
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Liver / enzymology
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Myocardium / ultrastructure
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Rabbits
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Rats
Substances
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5'-adenylyl (beta,gamma-bromomethylene)diphosphonate
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Diphosphonates
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bromomethylenebis(phosphonic acid)
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Adenosine Triphosphate
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5'-adenylyl (alpha,beta-bromomethylene)diphosphonate
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Ligases
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Coenzyme A Ligases
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Acetate-CoA Ligase
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Acetyl-CoA Carboxylase
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Adenosine