Cloning and sequence analysis of full-length cDNA of phenylalanine ammonia-lyase of Pinus massoniana.

Phenylalanine ammonia-lyase(PAL) is the key enzyme and rate-limiting enzyme that linked primary metabolism to secondary metabolism and plays a crucial role in disease resistance.It catalyzes phenylalanine ammonia into β-phenylacrylic acid and improves the synthesization of flavone and lignose.The full-length cDNA of phenylalanine ammonia-lyase was obtained by RT-PCR and RACE from Pinus massoniana.It consists of 2 700 nucleotides,with a 2 154 bp open read frame and encodes a protein of 717 amino acids.The theoretical molecular weight of the putative protein was 78 200 and the pI was 5.81.Phylogenetic analysis indicated that,compared with PAL homologous proteins from Pinus taeda,Pinus sylvestris and Pinus pinaster,the amino acid sequence identities were 98.2%、99.4% and 97.8% respectively.