Agmatine is essential for the cell growth of Thermococcus kodakaraensis

被引:47
作者
Fukuda, Wakao [2 ]
Morimoto, Nanako [1 ]
Imanaka, Tadayuki [3 ]
Fujiwara, Shinsuke [1 ,2 ]
机构
[1] Kwansei Gakuin Univ, Dept Biosci, Grad Sch Sci & Technol, Sanda, Hyogo 6691337, Japan
[2] Kwansei Gakuin Univ, Nanobiotechnol Res Ctr, Grad Sch Sci & Technol, Sanda, Hyogo 6691337, Japan
[3] Ritsumeikan Univ, Dept Biotechnol, Coll Life Sci, Shiga, Japan
关键词
archaea; polyamine; thermophile;
D O I
10.1111/j.1574-6968.2008.01303.x
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
TK0149 (designated as Tk-PdaD) of a hyperthermophilic archaeon, Thermococcus kodakaraensis, was annotated as pyruvoyl-dependent arginine decarboxylase, which catalyzes agmatine formation by the decarboxylation of arginine as the first step of polyamine biosynthesis. In order to investigate its physiological roles, Tk-PdaD was purified as a recombinant form, and its substrate dependency was examined using the candidate compounds arginine, ornithine and lysine. Tk-PdaD, expressed in Escherichia coli, was cleaved into alpha and beta subunits, as other pyruvoyl-dependent enzymes, and the resulting subunits formed all (alpha beta)(6) complex. The Tk-PdaD complex catalyzed the decarboxylation of arginine but not that of ornithine and lysine. A gene disruptant lacking Tk-pdaD was constructed, showing that it grew only in tire medium in the presence of agmatine but not in the absence of agmatine. The obtained results indicate that Tk-pdaD encodes a pyruvoyl-dependent arginine decarboxylase and that agmatine is essential for the cell growth of T. kodakaraensis.
引用
收藏
页码:113 / 120
页数:8
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