Involvement of snapdragon benzaldehyde dehydrogenase in benzoic acid biosynthesis
Involvement of snapdragon benzaldehyde dehydrogenase in benzoic acid biosynthesis
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DOI：
10.1111/j.1365-313x.2009.03864.x
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发表时间：
2009-07-01
期刊：
影响因子：
7.2
通讯作者：
Dudareva, Natalia
中科院分区：
文献类型：
--
作者：
Long, Michael C.;Nagegowda, Dinesh A.;Dudareva, Natalia
P>苯甲酸 (BA) 是从初级代谢物到次级产物的多种化合物的重要组成部分。从 L-苯丙氨酸生物合成苯甲酸需要将丙基侧链缩短两个碳，这可以通过 β 氧化途径或非 β 氧化途径发生，苯甲醛作为关键中间体。非β氧化途径需要苯甲醛脱氢酶（BALDH）将苯甲醛转化为BA。使用功能基因组方法，我们鉴定了金鱼草 BALDH，它与细菌 BALDH 具有 40% 的同一性。转录谱分析、纯化重组蛋白的生化表征、分子同源性建模、体内稳定同位素标记以及矮牵牛花中的瞬时表达表明 BALDH 能够在体内将苯甲醛氧化为 BA。 GFP 定位和免疫金标记研究表明，这一生化步骤发生在线粒体中，引发了关于亚细胞区室化在 BA 生物合成中的作用的问题。
P>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 beta-oxidative pathway or a non-beta-oxidative pathway, with benzaldehyde as a key intermediate. The non-beta-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.