MassIVE MSV000088175

Partial Public

Heterodimeric enzyme is involved in benzaldehyde synthesis in plants

Description

Benzaldehyde, the simplest aromatic aldehyde, is one of the most wide-spread volatiles that serves as a pollinator attractant, flavor, and antifungal compound. 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 beta-oxidative pathway in peroxisomes by a heterodimeric enzyme consisting of alpha and beta subunits, which belong to the NAD(P)-binding Rossmann-fold superfamily. Both subunits are alone catalytically inactive, but form an active benzaldehyde synthase when mixed in equal amounts. The enzyme exhibits strict substrate specificity towards benzoyl-CoA and uses NADPH as a cofactor. Alpha subunits can form functional hybrid heterodimers with phylogenetically distant bata subunits, but not all beta subunits partner with alpha subunits, at least in Arabidopsis. Analysis of spatial, developmental and rhythmic expression of genes encoding alpha- and beta- subunits revealed that expression of the gene for the alpha subunit correlates with benzaldehyde emission and likely plays a key role in regulating of benzaldehyde biosynthesis. [doi:10.25345/C55261] [dataset license: CC0 1.0 Universal (CC0 1.0)]

Keywords: Benzaldehyde, Petunia, Proteomics, Stable Isotope Labeling

Contact

Principal Investigators:
(in alphabetical order)
Natalia Dudereva, Purdue University, USA
Submitting User: uma_aryal
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