VITAMINS
Online ISSN : 2424-080X
Print ISSN : 0006-386X
Distribution of Nicotinamide Methyltransferase and Fundamental Properties of the Enzyme in Hog Liver
Hiroshi TAGUCHIHideya MUTOKunikatsu INAMORIKatsuzumi OKUMURAYoshihide SHIMABAYASHI
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1988 Volume 62 Issue 10 Pages 559-564

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Abstract
Distribution of nicotinamide methyltransferase (EC 2. 1. 1. 1) was investigated widely with 150 kinds of samples in animals, plants and microorganisms. The enzyme activity was found solely in animals and mostly in mammalian livers. Fundamental properties of nicotinamide methyltransferase in hog liver ex-tract were elucidated: optimum pH for the reaction, 5.0; Km values for nicotinamide and S-adenosyl-L-methionine, 58μM and 41μM, respectively; optimum temperature for the reaction (incubation period: 1 hr), 42℃; activation energy, 10,060cal/mol; inhibitors, heavy metal ions and N^1_methylnicotinamide (pro-duct inhibition, 50% at 30μM). The relationship among nicotinarnide methyltransferase, nicotinate methyltransferase (EC 2. 1. 1. 7) and nicotinamidase (EC 3. 5. 1. 19) in nature was discussed.
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© 1988 THE VITAMIN SOCIETY OF JAPAN

この記事はクリエイティブ・コモンズ [表示 - 非営利 - 改変禁止 4.0 国際]ライセンスの下に提供されています。
https://creativecommons.org/licenses/by-nc-nd/4.0/deed.ja
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