Arabidopsis thaliana defense-related protein ELI3 is an aromatic alcohol:NADP(+) oxidoreductase

被引:79
作者
Somssich, IE
Wernert, P
Kiedrowski, S
Hahlbrock, K
机构
[1] Max Planck Inst. F. Z., Department of Biochemistry
[2] Max Planck Inst. F. Z., Department of Biochemistry, D-50829 Köln
[3] Bayer AG, D-51368 Leverkusen, Landwirtschaftszentrum
关键词
benzyl alcohol dehydrogenase; disease resistance; fungal elicitor;
D O I
10.1073/pnas.93.24.14199
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
We expressed a cDNA encoding the Arabidopsis thaliana defense-related protein ELI3-2 in Escherichia coli to determine its biochemical function. Based on a protein database search, this protein was recently predicted to be a mannitol dehydrogenase [Williamson, J. D., Stoop, J. M. H., Massel, M. O., Conkling, M. A. & Pharr, D. R3. (1995) Proc. Natl. Acad. Sci. USA 92, 7148-7152]. Studies on the substrate specificity now revealed that ELI3-2 is an aromatic alcohol: NADP(+) oxidoreductase (benzyl alcohol dehydrogenase). The enzyme showed a strong preference for various aromatic aldehydes as opposed to the corresponding alcohols. Highest substrate affinities were observed for 2-methoxybenzaldehgde, 3-methoxybenzaldehyde, salicylaldehyde, and benzaldehyde, in this order, whereas mannitol dehydrogenase activity could not be detected. These and previous results support the notion that ELI3-2 has an important role in resistance-related aromatic acid-derived metabolism.
引用
收藏
页码:14199 / 14203
页数:5
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