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Uroporphyrinogen III synthase purified from rat liver is a monomer of Mr 36,000 by gel filtration and 28,000 by SDS/polyacrylamide-gel electrophoresis. The enzyme exists in two interconvertible forms separable on h.p.l.c. Both forms of the enzyme could be renatured with full activity after SDS/polyacrylamide-gel electrophoresis, demonstrating the absence of a reversibly bound cofactor. The enzyme activity could be inhibited by pyridoxal 5'-phosphate in the absence and in the presence of NaBH4, consistent with (an) essential lysine residue(s). The enzyme thus shows great similarity to that from Euglena gracilis.

biochemical journal

Rat liver uroporphyrinogen III synthase has similar properties to the enzyme from <i>Euglena gracilis</i>, including absence of a requirement for a reversibly bound cofactor for activity

Rat liver uroporphyrinogen III synthase has similar properties to the enzyme from Euglena gracilis, including absence of a requirement for a reversibly bound cofactor for activity