Nonenzymatic synthesis of ∂-aminolevulinate (ALA) by cobalt (CO⁺⁺)

Abstract

Cobalt, a metal known to modulate the heme biosynthetic enzymes, is shown to be capable of catalysing the formation of ALA through a transamination reaction. The transamination reaction follows a double-displacement reaction kinetics. Further, it has also been shown that the product of the reaction catalysed by cobalt can be used by the enzyme ALA dehydratase as the substrate in the formation of porphobilinogen. The formation of ALA by cobalt can be inhibited by the intermediates of the heme biosynthetic pathway, mainly protoporphyrin. Heme, on the other hand, does not have any effect on the reaction at all concentrations tested.