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

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., C...

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Published in:Proceedings of the National Academy of Sciences - PNAS 1996-11, Vol.93 (24), p.14199-14203
Main Authors: Somssich, I E, Wernert, P, Kiedrowski, S, Hahlbrock, K
Format: Article
Language:English
Subjects:
actividad enzimatica
activite enzymatique
alcohol dehydrogenase
alcohol deshidrogenasa
alcool deshydrogenase
aldehidos
aldehyde
aldehydes
arabidopsis thaliana
aromatic compounds
Biological Sciences
compose aromatique
compuestos aromaticos
defence mechanisms
enfermedades de las plantas
enzymic activity
maladie des plantes
mecanisme de defense
mecanismos de defensa
plant diseases
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Summary: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. and 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.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.93.24.14199