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Six Phenylalanine Ammonia-Lyases from Camellia sinensis: Evolution, Expression, and Kinetics
Wu Yingling 1 #,Wang Wenzhao 1,Li Yanzhi 1,Dai Xinglong 2,Ma Guoliang 1,Xing Dawei 1,Zhu Mengqing 2,Gao Liping 2,Xia Tao 1 *
1.State Key Laboratory of Tea Plant Biology and Utilization, Anhui Agricultural University, Hefei, Anhui 230036, China
2.School of Life Science, Anhui Agricultural University, Hefei, Anhui 230036, China
*Correspondence author
#Submitted by
Subject:
Funding: Natural Science Foundation （No.No.31270730）, the Special Foundation for Independent Innovation of Anhui Province, China （No. No.13Z03012）, the Natural Science Foundation of Anhui Province, China （No. No. 1708085MC58）, the Specialized Research Fund for the Doctoral Program of Higher Education （No. No. 20133418130001）, Natural Science Foundation （No.No.31570694）, Natural Science Foundation （No.No.31200229）, Natural Science Foundation （No.No.31470689）
Opened online:28 April 2017
Accepted by: none
Citation: Wu Yingling,Wang Wenzhao,Li Yanzhi.Six Phenylalanine Ammonia-Lyases from Camellia sinensis: Evolution, Expression, and Kinetics[OL]. [28 April 2017] http://en.paper.edu.cn/en_releasepaper/content/4726835
 
 
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 abiotic stresses. 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 provide evidence for the identification and characterization of CsPAL genes and that they have both distinct and overlapping roles in plant growth, development, and responses to environmental cues.
Keywords:Phenylalanine Ammonia-Lyase; Camellia sinensis;Evolution; Expression; Kinetics
 
 
 

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