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Purification and properties of alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase (ACMSD), key enzyme of niacin synthesis from tryptophan, from hog kidney.

alpha-Amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase (ACMSD) (EC 4.1.1.45) was purified to a homogeneous state from hog kidney cytosol by ammonium sulfate fractionation, Butyl-Toyopearl 650, hydroxyapatite, DEAE-Sephadex, Toyopearl HW55, Superdex 200 and TSK-gel G3000SW chromatographies. The molecular weight of the enzyme was estimated to be 58,000 by TSK-gel G3000SW gel filtration. The optimum pH (constant concentration) was 7.5. The Km for alpha-amino-beta-carboxymuconate-epsilon-semialdehyde was 1.61 x 10(-5) M. The activity of purified enzyme was inhibited by some chemical modifying reagents such as monoiodoacetic acid and p-(chloromercuri) benzoic acid. A sulfhydryl group was deduced to exist in the active site of the enzyme.