Six phenylalanine ammonia-lyases from Camellia sinensis: Evolution, expression, and kinetics
 
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Title


Six phenylalanine ammonia-lyases from Camellia sinensis: Evolution, expression, and kinetics


Authors


Yingling Wu, Wenzhao Wang, Yanzhi Li, Xinlong Dai, Guoliang Ma, Dawei Xing, Mengqing Zhu, Liping Gao*, Tao Xia*


Journal


Plant Physiology and Biochemistry 118 (2017) 413-421


Abstract


Phenylalanine ammonia-lyase (PAL), the branch point enzyme controlling the flow of primary metabolism into second metabolism, converts the L-phenylalanine (L-Phe) to yield cinnamic acid. Based on the sequencing data available from eight transcriptome projects, six
PAL genes have been screened out, cloned, and designated as CsPALa-CsPALf. The phylogenetic tree showed that CsPALs were divided into three subgroups, PALa and PALb, PALc and PALd, and PALe and PALf. All six CsPALs exhibited indiscriminate cytosolic locations in epidermis cells and mesophyll cells. Then, the expression profiles of six PAL genes were qualitatively investigated and they displayed tissue-/induced-expression specificity in several tissues or under different exogenous treatments. Furthermore, in vitro enzymatic assays showed that all six recombinant proteins were characterized by the strict substrate specificity toward L-Phe, but no activity toward L-Tyr, and they displayed subtle differences in kinetics and enzymatic properties. These results indicate that CsPALs play both distinct and overlapping roles in plant growth and responses to environmental cues.




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  • six phenylalanine ammonia-lyases(吴英玲、高丽萍、夏涛,2017).pdf
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