Purification and Properties of .ALPHA.-Amino-.BETA.-Carboxymuconate-.EPSILON.-Semialdehyde Decarboxylase (ACMSD), Key Enzyme of Niacin Synthesis from Tryptophan, from Hog Kidney.
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概要
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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.
- 財団法人 学会誌刊行センターの論文
著者
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Sanada Hiroo
Department Of Agricultural Chemistry Faculty Of Horticulature Chiba University
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OHTA Takeo
Department of Bioproduction Science, Faculty of Horticulture, Chiba University
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Egashira Y
Department Of Bioproduction Science Faculty Of Horticulture Chiba University
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Egashira Yukari
Department Of Bioproduction Science Faculty Of Horticulture Chiba University
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KOUHASHI Hanae
Department of Bioproduction Science, Faculty of Horticulture, University of Chiba
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SANADA Hiroo
Department of Bioproduction Science, Faculty of Horticulture, University of Chiba
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OHTA Takeo
Department of Bioproduction Science, Faculty of Horticulture
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OHTA Takeo
Department of Bioproduction Science, Faculty of Horticulture, University of Chiba
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EGASHIRA Yukari
Department of Bioproduction Science, Faculty of Horticulture, University of Chiba
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OHTA Takeo
Department of Agricultural Chemistry, Faculty of Agriculture, The University of Tokyo
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