RESUMO
Objective: This study aimed at cloning the phenylalanine ammonia-lyase (PAL) gene from Curcuma longa (CurPAL) and analyzing the bioinformatics. Methods: PAL gene was cloned by RT-PCR and RACE strategy with the template of RNA extracted from C. longa leaves. The bioinformatic analysis of this gene and its corresponding protein were performed. Results: One unique sequence of PAL, named as CurPAL (GenBank NO. KJ780359), was cloned from C. longa. The full-length of CurPAL cDNA was 1 293 bp, including 243 bp of 5'-UTR, 123 bp of 3'-UTR, and 927 bp of ORF encoding 308 amino acids. The molecular weight and theroretical isoelectric point (pI) of the deduced CurPAL protein were 33 000 and 5.76, respectively. The protein of CurPAL was stable and soluble. The domination sites and catalytic active sites in PAL protein of Nerium oleander were also found in CurPAL. It was found that the amino acid sequence of CurPAL had more than 75% homology with PAL of Prunus salicina, Camellia chekiangoleosa, Capsicum chinense, and Musa acuminate via multiple alignments. It revealed that CurPAL had closer relationship with PALs from Zingiberales plants than from other plants by phylogenetic tree analysis. Secondary and tertiary structures indicate that CurPAL is a full α protein contained by homotetramer. Conclusion: The cDNA encoding PAL from C. longa is cloned and reported for the first time. This work provides a scientific basis for exploring the biosynthetic pathway of the medicinal ingredient and improving its quality in C. longa.