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Abstract
A cell-free extract of the anaerobic eubacterium, Clostridium thermoaceticum, catalyses the synthesis of 5-aminolevulinic acid (ALA) from glutamate via the C 5 pathway. The enzyme reaction resembles that of higher plants and algae in cofactor requirements and sensitivity to ribonuclease. From the phylogenetic distribution it is proposed that the C 5 pathway evolved earlier than the ALA synthase pathway.
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