Functional characterization of SlscADH1, a fruit-ripening-associated short-chain alcohol dehydrogenase of tomato

Copyright © 2012 Elsevier GmbH. All rights reserved.

Bibliographische Detailangaben
Veröffentlicht in:Journal of plant physiology. - 1979. - 169(2012), 15 vom: 15. Okt., Seite 1435-44
1. Verfasser: Moummou, Hanane (VerfasserIn)
Weitere Verfasser: Tonfack, Libert Brice, Chervin, Christian, Benichou, Mohamed, Youmbi, Emmanuel, Ginies, Christian, Latché, Alain, Pech, Jean-Claude, van der Rest, Benoît
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2012
Zugriff auf das übergeordnete Werk:Journal of plant physiology
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Aldehydes Phospholipids Volatile Organic Compounds n-hexanal 9DC2K31JJQ Alcohol Oxidoreductases EC 1.1.- Acetaldehyde mehr... GO1N1ZPR3B phenylacetaldehyde U8J5PLW9MR
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100 1 |a Moummou, Hanane  |e verfasserin  |4 aut 
245 1 0 |a Functional characterization of SlscADH1, a fruit-ripening-associated short-chain alcohol dehydrogenase of tomato 
264 1 |c 2012 
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500 |a Date Completed 11.04.2013 
500 |a Date Revised 07.12.2022 
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500 |a Citation Status MEDLINE 
520 |a Copyright © 2012 Elsevier GmbH. All rights reserved. 
520 |a A tomato short-chain dehydrogenase-reductase (SlscADH1) is preferentially expressed in fruit with a maximum expression at the breaker stage while expression in roots, stems, leaves and flowers is very weak. It represents a potential candidate for the formation of aroma volatiles by interconverting alcohols and aldehydes. The SlscADH1 recombinant protein produced in Escherichia coli exhibited dehydrogenase-reductase activity towards several volatile compounds present in tomato flavour with a strong preference for the NAD/NADH co-factors. The strongest activity was observed for the reduction of hexanal (K(m)=0.175mM) and phenylacetaldehyde (K(m)=0.375mM) in the presence of NADH. The oxidation process of hexanol and 1-phenylethanol was much less efficient (K(m)s of 2.9 and 23.0mM, respectively), indicating that the enzyme preferentially acts as a reductase. However activity was observed only for hexanal, phenylacetaldehyde, (E)-2-hexenal and acetaldehyde and the corresponding alcohols. No activity could be detected for other aroma volatiles important for tomato flavour, such as methyl-butanol/methyl-butanal, 5-methyl-6-hepten-2-one/5-methyl-6-hepten-2-ol, citronellal/citronellol, neral/nerol, geraniol. In order to assess the function of the SlscADH1 gene, transgenic plants have been generated using the technique of RNA interference (RNAi). Constitutive down-regulation using the 35S promoter resulted in the generation of dwarf plants, indicating that the SlscADH1 gene, although weakly expressed in vegetative tissues, had a function in regulating plant development. Fruit-specific down-regulation using the 2A11 promoter had no morphogenetic effect and did not alter the aldehyde/alcohol balance of the volatiles compounds produced by the fruit. Nevertheless, SlscADH1-inhibited fruit unexpectedly accumulated higher concentrations of C5 and C6 volatile compounds of the lipoxygenase pathway, possibly as an indirect effect of the suppression of SlscADH1 on the catabolism of phospholipids and/or integrity of membranes 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
650 7 |a Aldehydes  |2 NLM 
650 7 |a Phospholipids  |2 NLM 
650 7 |a Volatile Organic Compounds  |2 NLM 
650 7 |a n-hexanal  |2 NLM 
650 7 |a 9DC2K31JJQ  |2 NLM 
650 7 |a Alcohol Oxidoreductases  |2 NLM 
650 7 |a EC 1.1.-  |2 NLM 
650 7 |a Acetaldehyde  |2 NLM 
650 7 |a GO1N1ZPR3B  |2 NLM 
650 7 |a phenylacetaldehyde  |2 NLM 
650 7 |a U8J5PLW9MR  |2 NLM 
700 1 |a Tonfack, Libert Brice  |e verfasserin  |4 aut 
700 1 |a Chervin, Christian  |e verfasserin  |4 aut 
700 1 |a Benichou, Mohamed  |e verfasserin  |4 aut 
700 1 |a Youmbi, Emmanuel  |e verfasserin  |4 aut 
700 1 |a Ginies, Christian  |e verfasserin  |4 aut 
700 1 |a Latché, Alain  |e verfasserin  |4 aut 
700 1 |a Pech, Jean-Claude  |e verfasserin  |4 aut 
700 1 |a van der Rest, Benoît  |e verfasserin  |4 aut 
773 0 8 |i Enthalten in  |t Journal of plant physiology  |d 1979  |g 169(2012), 15 vom: 15. Okt., Seite 1435-44  |w (DE-627)NLM098174622  |x 1618-1328  |7 nnns 
773 1 8 |g volume:169  |g year:2012  |g number:15  |g day:15  |g month:10  |g pages:1435-44 
856 4 0 |u http://dx.doi.org/10.1016/j.jplph.2012.06.007  |3 Volltext 
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