Pyruvate Caroxylase and Oxaloetetoxification

In rat liver cells, physiologically relevant concentrations of oxaloet inhibit citric acid cyclic activity by a whopping 48%. As would be expected, this leads to the reduction in the amount of mitochondrial NADH. The enzyme binds 15 times more strongly than pyruvate does and tucks itself into exactly right down to the specific amino acid in the active site. It can metabolize other known substrates such as alficinobutyrate. If that's true, it would mean we possess the first step ofoxaloetetoxification expected from bacterial metabolism.