Characterization of Arylamine N-acetyltransferase in Enterobacter Aerogenes

CMUR > China Medical University Hospital > Jurnal articles > Item 310903500/2616

Please use this identifier to cite or link to this item: http://ir.cmu.edu.tw/ir/handle/310903500/2616

Title:	Characterization of Arylamine N-acetyltransferase in Enterobacter Aerogenes
Authors:	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)
Contributors:	中國附醫檢驗醫學部生化組
Date:	1998-07
Issue Date:	2009-08-20 17:32:14 (UTC+8)
Abstract:	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.
Relation:	MICROBIOLOGY 94(379):133~143
Appears in Collections:	[China Medical University Hospital] Jurnal articles

Files in This Item:

File	Size	Format
	0Kb	Unknown	313	View/Open