Coenzyme Saturation of Transaminases

A number of studies have measured the activation of plasma transaminases by pyridoxal phosphate added in vitro; however, it is difficult to interpret the results, because plasma transaminases arise largely accidentally, as a result of cell turnover, and the amount released will depend on tissue damage. Furthermore, there is a considerable amount of pyridoxal phosphate in plasma, largely associated with serum albumin, and the extent to which plasma transaminases are saturated will depend largely on the relative affinity of albumin and the enzyme concerned for the coenzyme, rather than reflecting the availability of pyridoxal phosphate for intracellular metabolism. Studies on erythrocyte transaminase activation coefficient are easier to interpret, because the extent to which the enzymes are saturated depends mainly on the availability of pyri-doxal phosphate.

It seems likely that it is normal for a proportion of pyridoxal phosphate-dependent enzymes to be present as inactive apoenzyme, without coenzyme. This maybe a mechanism of metabolic regulation. It is possible that increasing the intake ofvitamin B6, to ensure complete saturation ofpyridoxalphosphate-dependent enzymes, may not be desirable.

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