A peroxisomal heterodimeric enzyme is involved in benzaldehyde synthesis in plants

Xing-Qi Huang, Renqiuguo Li, Jianxin Fu and Natalia Dudareva ()
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Xing-Qi Huang: Purdue University
Renqiuguo Li: Purdue University
Jianxin Fu: Purdue University
Natalia Dudareva: Purdue University

Nature Communications, 2022, vol. 13, issue 1, 1-15

Abstract: Abstract Benzaldehyde, the simplest aromatic aldehyde, is one of the most wide-spread volatiles that serves as a pollinator attractant, flavor, and antifungal compound. However, the enzyme responsible for its formation in plants remains unknown. Using a combination of in vivo stable isotope labeling, classical biochemical, proteomics and genetic approaches, we show that in petunia benzaldehyde is synthesized via the β-oxidative pathway in peroxisomes by a heterodimeric enzyme consisting of α and β subunits, which belong to the NAD(P)-binding Rossmann-fold superfamily. Both subunits are alone catalytically inactive but, when mixed in equal amounts, form an active enzyme, which exhibits strict substrate specificity towards benzoyl-CoA and uses NADPH as a cofactor. Alpha subunits can form functional heterodimers with phylogenetically distant β subunits, but not all β subunits partner with α subunits, at least in Arabidopsis. Analysis of spatial, developmental and rhythmic expression of genes encoding α and β subunits revealed that expression of the gene for the α subunit likely plays a key role in regulating benzaldehyde biosynthesis.

Date: 2022
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DOI: 10.1038/s41467-022-28978-2

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