Journal of Nutritional Science and Vitaminology
Online ISSN : 1881-7742
Print ISSN : 0301-4800
ISSN-L : 0301-4800
Purification and Properties of α-Amino-β-Carboxymuconate-ε-Semialdehyde Decarboxylase (ACMSD), Key Enzyme of Niacin Synthesis from Tryptophan, from Hog Kidney
Yukari EGASHIRAHanae KOUHASHITakeo OHTAHiroo SANADA
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1996 Volume 42 Issue 3 Pages 173-183

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Abstract

α-Amino-β-carboxymuconate-ε-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 α-amino-β-carboxymuconate-ε-semialdehyde was 1.61×10-5M. 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.

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