Kim S H, Virmani D, Wake K, MacDonald K, Kronstad J W, Ellis B E
Department of Wood Science, University of British Columbia, Vancouver, Canada.
Curr Genet. 2001 Aug;40(1):40-8. doi: 10.1007/s002940100230.
The enzyme L-phenylalanine ammonia-lyase (PAL) catalyzes the non-oxidative deamination of L-phenylalanine to form trans-cinnamic acid and ammonia. This enzyme is universally present in higher plants and it catalyzes the starting reaction for a central pathway that generates hundreds of different phenylpropanoid metabolites. Genes encoding PAL have been identified in fungi, but the role of the enzyme has not been determined. We cloned and characterized a gene that encodes PAL from the phytopathogenic fungus Ustilago maydis and we constructed fungal strains carrying a null mutation in the gene. These mutants behaved like wild-type strains in terms of growth, mating, and pathogenicity. These results indicate that PAL does not play a major role in the life cycle of U. maydis under laboratory conditions.
L-苯丙氨酸解氨酶(PAL)催化L-苯丙氨酸的非氧化脱氨反应,生成反式肉桂酸和氨。这种酶普遍存在于高等植物中,它催化一条核心途径的起始反应,该途径可产生数百种不同的苯丙烷类代谢产物。在真菌中已鉴定出编码PAL的基因,但该酶的作用尚未确定。我们从植物致病真菌玉米黑粉菌中克隆并鉴定了一个编码PAL的基因,并构建了该基因发生无效突变的真菌菌株。这些突变体在生长、交配和致病性方面表现得与野生型菌株相似。这些结果表明,在实验室条件下,PAL在玉米黑粉菌的生命周期中不发挥主要作用。