@Article{phyton.2024.048786,
AUTHOR = {Dejin Mu, Lin Chen, Heze Wang, Zhaoliu Hu, Sihui Chen, Shi Chen, Nianhui Cai, Yulan Xu, Junrong Tang},
TITLE = {The Identification of Phenylalanine Ammonia-Lyase (PAL) Genes from <i>Pinus yunnanensis</i> and an Analysis of Enzyme Activity <i>in vitro</i>},
JOURNAL = {Phyton-International Journal of Experimental Botany},
VOLUME = {93},
YEAR = {2024},
NUMBER = {3},
PAGES = {503--516},
URL = {http://www.techscience.com/phyton/v93n3/55998},
ISSN = {1851-5657},
ABSTRACT = {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>.},
DOI = {10.32604/phyton.2024.048786}
}