Open AccessArabidopsis thaliana defense-related protein ELI3 is an aromatic alcohol:NADP + oxidoreductase
Author(s) -
Imre E. Somssich,
Petra Wernert,
Siegrid Kiedrowski,
Klaus Hahlbrock
Publication year - 1996
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.93.24.14199
Subject(s) - oxidoreductase , arabidopsis thaliana , arabidopsis , chemistry , biochemistry , alcohol , biology , enzyme , gene , mutant
We expressed a cDNA encoding theArabidopsis thaliana defense-related protein ELI3-2 inEscherichia 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. M. (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-methoxybenzaldehyde, 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.