Phenylalanine ammonia-lyase (PAL EC 4.3.1.5) is the first committed enzyme of phenylpropanoid pathway. A PAL gene, designated as BOPAL2, was cloned from a Bambusa oldhamii cDNA library. The open reading frame of BoPAL2 was 2142 bp in size encoding a 713-amino acid polypeptide. BoPAL2 was heterologous expressed in Escherichia coli and Pichia pastoris. The recombinant proteins were exhibited PAL and tyrosine ammonia-lyase activities. The recombinant BoPAL2 had a subunit mass of 80 kDa and existed as a homotetramer. The optimum temperature and pH of BoPAL2 were 50-60 degrees C and 8.5-9.0, respectively. The K-m and k(cat) values of BoPAL2 expressed in E. coli were 250 mu M and 10.12 s(-1). The K-m and k(cat) values of BoPAL2 expressed in P. pastoris were 331 mu M and 16.04 s(-1). The recombinant proteins had similar biochemical properties and kinetic parameters with PALs reported in other plants. (C) 2010 Elsevier Inc. All rights reserved.