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Involvement of snapdragon benzaldehyde dehydrogenase in benzoic acid biosynthesis
Author(s) -
Long Michael C.,
Nagegowda Dinesh A.,
Kaminaga Yasuhisa,
Ho Kwok Ki,
Kish Christine M.,
Schnepp Jennifer,
Sherman Debra,
Weiner Henry,
Rhodes David,
Dudareva Natalia
Publication year - 2009
Publication title -
the plant journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.058
H-Index - 269
eISSN - 1365-313X
pISSN - 0960-7412
DOI - 10.1111/j.1365-313x.2009.03864.x
Subject(s) - benzaldehyde , biochemistry , benzoic acid , biosynthesis , chemistry , dehydrogenase , stereochemistry , biology , enzyme , catalysis
Summary Benzoic acid (BA) is an important building block in a wide spectrum of compounds varying from primary metabolites to secondary products. Benzoic acid biosynthesis from l ‐phenylalanine requires shortening of the propyl side chain by two carbons, which can occur via a β‐oxidative pathway or a non‐β‐oxidative pathway, with benzaldehyde as a key intermediate. The non‐β‐oxidative route requires benzaldehyde dehydrogenase (BALDH) to convert benzaldehyde to BA. Using a functional genomic approach, we identified an Antirrhinum majus (snapdragon) BALDH, which exhibits 40% identity to bacterial BALDH. Transcript profiling, biochemical characterization of the purified recombinant protein, molecular homology modeling, in vivo stable isotope labeling, and transient expression in petunia flowers reveal that BALDH is capable of oxidizing benzaldehyde to BA in vivo . GFP localization and immunogold labeling studies show that this biochemical step occurs in the mitochondria, raising a question about the role of subcellular compartmentalization in BA biosynthesis.