Characterization of Arylamine N-acetyltransferase in Enterobacter Aerogenes

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題名:	Characterization of Arylamine N-acetyltransferase in Enterobacter Aerogenes
作者:	鄒梅芬(Mei-Fen Tsou);鍾景光(Jing-Gung Chung);吳禮字(Lii-Tzu Wu);鄭庚申(Ken-Sheng Cheng);(Hung CF)
貢獻者:	中國附醫檢驗醫學部生化組
日期:	1998-07
上傳時間:	2009-08-20 17:32:14 (UTC+8)
摘要:	N-acetyltransferase (NAT) activity was determined by incubation of purified Enterobacter aerogenes enzyme with 2-aminofluorene (2-AF) as the substrate, followed by high pressure liquid chromatography assays. The NAT activity from E. aerogenes was 0.58 +/- 0.08 nmol/min/mg protein for 2-AF. The values of apparent K(m) and Vmax were 0.72 +/- 0.14 mM and 2.45 +/- 0.29 nmol/min/mg protein, respectively, for 2-AF. The optimal pH value for the enzyme activity was 7.5 for the 2-AF tested. The optimal temperature for enzyme activity was 37 degrees C for the 2-AF substrate. The molecular weight of NAT from E. aerogenes was 44.9 kD. Among a series of divalent cations and salts, Zn2+, Ca2+, and Fe2+ were demonstrated to be the most potent protease inhibitors, and only ethylenediaminetetraacetic acid significantly protected the NAT. Iodoacetamide, in contrast to other agents, markedly inhibited NAT.
關聯:	MICROBIOLOGY 94(379):133~143
顯示於類別:	[台中附設醫院] 期刊論文

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