Fluoroacetate, biochemical mechanism

The biochemical mechanism of the toxicity of fluoroacetate in mammals was first elucidated by the notable researches of the late Sir Rudolph Peters, who showed that in liver and kidney, the compound was metabolically transformed into an even more toxic fluorocitric acid isomer, a powerful inhibitor of the tricarboxylic acid cycle. These results together with those of others, Li ecq, Bergmann,... 

So far only a few dozen organofluorine compounds have been isolated from living organisms, for example fluoroacetic acid, 4-fluorothreonine and rw-fluoro-oleic acid [244-246], The reason that nature has not invested in fluorine chemistry could be a combination of low availability of water-dissolved fluoride in the environment due to its tendency to form insoluble fluoride salts, and the low reactivity of water-solvated fluoride ion. However, in 2002, O Hagan and collaborators [247] published the discovery of a biochemical fluorination reaction in a bacterial protein extract from Streptomyces cattleya converting S-adenosyl-L-methionine (SAM) to 5 -fluoro-5 deoxyadenosine (5 -FDA). The same protein extract contained also the necessary enzymatic activity to convert 5 -FDA into fluoroacetic acid. In 2004, the same authors published the crystal structure of the enzyme and demonstrated a nucleophilic mechanism of fluorination [248,249]. 

Administration of fluoroacetate to animals leads to inhibition of a particular enzyme. Name the enzyme that is inhibited, and briefly describe the mechanism and the biochemical and pathological consequences. 

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