TY  - EJOU
AU  - Mu, Dejin 
AU  - Chen, Lin 
AU  - Wang, Heze 
AU  - Hu, Zhaoliu 
AU  - Chen, Sihui 
AU  - Chen, Shi 
AU  - Cai, Nianhui 
AU  - Xu, Yulan 
AU  - Tang, Junrong 

TI  - The Identification of Phenylalanine Ammonia-Lyase (PAL) Genes from <i>Pinus yunnanensis</i> and an Analysis of Enzyme Activity <i>in vitro</i>
T2  - Phyton-International Journal of Experimental Botany

PY  - 2024
VL  - 93
IS  - 3
SN  - 1851-5657

AB  - Phenylalanine ammonia lyase (PAL) is the rate-limiting and pivotal enzyme of the general phenylpropanoid pathway, but few reports have been found on <i>PAL</i> genes in <i>Pinus yunnanensis</i>. In the present study, three <i>PAL</i> genes were cloned and identified from <i>P. yunnanensis</i> seedlings for the first time, namely, <i>PyPAL-1</i>, <i>PyPAL-2</i>, and <i>PyPAL-3</i>. Our results indicated that the open-reading frames of <i>PyPAL</i> genes were 2184, 2157, and 2385 bp. Phylogenetic tree analysis revealed that <i>PyPALs</i> have high homology with other known <i>PAL</i> genes in other plants. <i>In vitro</i> enzymatic analysis showed that all three <i>PyPAL</i> recombinant proteins could catalyze the deamination of L-phenylalanine to form trans-cinnamic acid, but only PAL1 and PAL2 can catalyze the conversion of L-tyrosine to <i>ρ</i>-coumaric acid. Three <i>PyPAL</i> genes were expressed in different tissues in 1-year-old <i>P. yunnanensis</i>, and such genes had different expression patterns. This study lays a foundation for further understanding of the biosynthesis of secondary metabolites in <i>P. yunnanensis</i>.
KW  - <i>Pinus yunnanensis</i>; phenylalanine ammonia-lyase; enzyme activity <i>in vitro</i>; functional analysis; secondary metabolites

DO  - 10.32604/phyton.2024.048786